Autophosphorylation: a salient feature of protein kinases (original) (raw)
References
Fischer EH, Krebs EG: The conversion of phosphorylase b to phosphorylase a. J Biol Chem 216:121–132, 1955 PubMed Google Scholar
Krebs EG: The enzymology of control by phosphorylation. In: PD Boyer, EG Krebs (eds) The Enzymes. Academic Press, Orlando, 1986, pp 3–20 Google Scholar
Hunter T: A thousand and one protein kinases. Cell 50:823–829, 1987 PubMed Google Scholar
Flockhart DA, Corbin JD: Regulatory mechanisms in the control of protein kinases. CRC Crit Rev Biochem 13:133–186, 1982 Google Scholar
Hunter T, Cooper JA: Viral oncogenes and tyrosine phosphorylation. In: PD Boyer, EG Krebs (eds) The Enzymes. Academic Press, Orlando, FL, 1986, pp 192–246 Google Scholar
Krebs EG, Beavo JA: Phosphorylation-dephosphorylation of enzymes. Ann Rev Biochem 48: 923–959, 1979 PubMed Google Scholar
Forte LR, Thorne PK, Eber SL, Krause WJ, Freeman RH, Francis SH, Corbin JD: Stimulation of intestinal Cl transport by heat-stable enterotoxin: activation of cAMP-dependent protein kinase by cGMP. Am J Phys 263 (3): C607-C615, 1992 Google Scholar
Schumacher H, Müller D, Mukhopadhyay AK: Stimulation of testosterone production by atrial natriuretic peptide in isolated mouse leydig cells results from a promiscuous activation of cyclic AMP-dependent protein kinase by cyclic GMP. Mol Cell Endocrinol 90: 47–52, 1992 PubMed Google Scholar
Francis SH, Noblett BD, Todd BW, Wells JN, Corbin JD: Relaxation of vascular and tracheal smooth muscle by cyclic nucleotide analogs that preferentially activate purified cGMP-dependent protein kinase. Mol Pharmacol 34: 506–517, 1988 PubMed Google Scholar
Lincoln TM, Cornwell TL, Taylor AE: cGMP-dependent protein kinase mediates the reduction of Ca2+ by cAMP in vascular smooth muscle cells. Am J Physiol 258: C399-C407, 1990 PubMed Google Scholar
Jiang H, Colbran JL, Francis SH, Corbin JD: Direct evidence for cross-activation of cGMP-dependent protein kinase by cAMP in pig coronary arteries. J Biol Chem 267: 1015–1019, 1992 PubMed Google Scholar
Zetterqvist Ö, Ragnarsson U, Engström L: Substrate specificity of cyclic AMP-dependent protein kinase. In: BE Kemp (ed.) Peptides and Protein Phosphorylation. CRC Press, Boca Raton, FL, 1990, pp 171–187 Google Scholar
Erlichman J, Rosenfield R, Rosen OM: Phosphorylation of a cyclic adenosine 3′:5′-monophosphate-dependent protein kinase from bovine cardiac muscle. J Biol Chem 249: 5000–5003, 1974 PubMed Google Scholar
Rangel-Aldao R, Rosen OM: Mechanism of self-phosphorylation of a adenosine 3′:5′-monophosphate-dependent protein kinase from bovine cardiac muscle. J Biol Chem 251: 7526–7529, 1976 PubMed Google Scholar
Scott CW, Mumby MC: Phosphorylation of type II regulatory subunit of cAMP-dependent protein kinase in intact smooth muscle. J Biol Chem 260: 2274–2280, 1985 PubMed Google Scholar
Rosen OM, Erlichman J, Rubin CS: Molecular structure and characterization of bovine heart protein kinase. Adv Cyclic Nucleotide Res 5: 253–263, 1975 PubMed Google Scholar
Flockhart DA, Watterson DM, Corbin JD: Studies on the functional domains of the regulatory subunit of bovine heart adenosine 3′:5′-monophosphate-dependent protein kinase. J Biol Chem 255: 4435–4440, 1980 PubMed Google Scholar
Takio K, Smith SB, Krebs EG, Walsh KA, Titani K: Primary structure of the regulatory subunit of type-II cAMP-dependent protein kinase from bovine cardiac muscle. Proc Natl Acad Sci USA 79: 2544–2548, 1982 PubMed Google Scholar
Rangel-Aldao R, Rosen OM: Dissociation and reassociation of the phosphorylated and nonphosphorylated forms of adenosine 3′:5′-monophosphate-dependent protein kinase from bovine cardiac muscle. J Biol Chem 251: 3375–3380, 1976 PubMed Google Scholar
Rossi S, Guthmann M, Moreno S: Autophosphorylation of_mucor rouxii_ cAMP-dependent protein kinase and its role in holoenzyme activation. Cellular Signalling 4: 443–451, 1992 PubMed Google Scholar
Kuret J, Johnson KE, Nicolette C, Zoller MJ: Mutagenesis of the regulatory subunit of yeast cAMP-dependent protein kinase. J Biol Chem 263: 9149–9154, 1988 PubMed Google Scholar
Corbin JD, Sudgen PH, West L, Flockhart DA, Lincoln TM, McCarthy D: Studies on the properties and mode of action of the purified regulatory subunit of bovine heart adenosine 3′:5′-monophosphate-dependent protein kinase. J Biol Chem 253: 3997–4003, 1978 PubMed Google Scholar
Kemp BE, Graves DJ, Benjamini E, Krebs EG: Role of multiple basis residues in determining the substrate specificity of cyclic AMP-dependent protein kinase. J Biol Chem 252: 4888–4894, 1977 PubMed Google Scholar
Scott CW, Mumby MC: Autophosphorylation of rat liver type II cAMP-dependent protein kinase. Mol Endocrinol 3: 1815–1822, 1989 PubMed Google Scholar
Vereb G, Gergely P: The role of autophosphorylation of cAMP-dependent protein kinase II in the inhibition of protein phosphatase-1. Int J Biochem 21: 1137–1141, 1989 PubMed Google Scholar
Khatra BS, Printz R, Cobb CE, Corbin JD: Regulatory subunit of cAMP-dependent protein kinase inhibits phosphoprotein phosphatase. Biochem Biophys Res Commun 130: 567–573, 1985 PubMed Google Scholar
Jurgensen SR, Chock PB, Taylor S, Vandenheede JR, Merlevede W: Inhibition of the Mg(II)-ATP-dependent phosphoprotein phosphatase by the regulatory subunit of cAMP-dependent protein kinase. Proc Natl Acad Sci USA 82: 7565–7569, 1985 PubMed Google Scholar
Gergely P, Bot G: The control of phosphorylase phosphatase by cAMP-dependent protein kinase. FEBS Lett 82: 269–272, 1977 PubMed Google Scholar
Srivastava AK, Khandelwal RL, Chiasson J-L, Haman A: Inhibitory effect of the regulatory subunit of type I cAMP-dependent protein kinase on phosphoprotein phosphatase. Biochem Int 16: 303–310, 1988 PubMed Google Scholar
Shoji S, Ericsson LH, Walsh KA, Fischer EH, Titani K: Amino acid sequence of the catalytic subunit of bovine type II adenosine cyclic 3′,5′-phosphate-dependent protein kinase. Biochemistry 22: 3702–3709, 1983 PubMed Google Scholar
Shoji S, Titani K, Demaille JG, Fischer EH: Sequence of two phosphorylated sites in the catalytic subunit of bovine cardiac muscle adenosine 3′,5′-monophosphate-dependent protein kinase. J Biol Chem 254: 6211–6214, 1979 PubMed Google Scholar
Toner-Webb J, van Patten SM, Walsh DA, Taylor SS: Autophosphorylation of the catalytic subunit of cAMP-dependent protein kinase. J Biol Chem 267: 25174–25180, 1992 PubMed Google Scholar
Mobashery S, Kaiser ET: Identification of amino acid residues involved in substrate recognition by the catalytic subunit of bovine cyclic AMP dependent protein kinase: peptide-based affinity labels. Biochemistry 27: 3691–3696, 1988 PubMed Google Scholar
Knighton DR, Zheng J, Eyck LFT, Ashford VA, Xuong N-H, Taylor SS, Sawodski JM: Crystal structure of the catalytic subunit of cyclic adenosine monophosphate-dependent proteinkinase. Science 253: 407–414, 1991 PubMed Google Scholar
Knighton DR, Zheng J, Eyck LFT, Xuong N-H, Taylor SS, Sawodski JM: Structure of a peptide inhibitor bound to the catalytic subunit of cyclic adenosine monophosphate-dependent protein kinase. Science 253: 414–420, 1991 PubMed Google Scholar
Levin LR, Zoller MJ: Association of the catalytic and regulatory subunits of cyclic AMP-dependent protein kinase requires a negatively charged side group at a conserved threonine. Mol Cell Biol 10: 1066–1075, 1990 PubMed Google Scholar
Steinberg RA, Cauthron RD, Symcox MM, Shuntoh H: Autoactivation of catalytic (Cα) subunit of cyclic AMP-dependent protein kinase by phosphorylation of threonine 197. Mol Cell Biol 13: 2332–2341, 1993 PubMed Google Scholar
Huggenvik JI, Collard MW, Stofko RE, Seaholtz AF, Uhler MD: Regulation of the human enkephalin promoter by two isoforms of the catalytic subunit of cyclic adenosine 3′,5′-monophosphate-dependent protein kinase. Mol Endocrinol 5: 921–930, 1991 PubMed Google Scholar
Orellana SA, McKnight GS: Mutations in the catalytic subunit of cAMP-dependent protein kinase result in unregulated biological activity. Proc Natl Acad Sci USA 89: 4726–4730, 1992 PubMed Google Scholar
Lincoln TM, Hall CL, Park CR, Corbin JD: Guanosine 3′:5′-cyclic monophosphate binding proteins in rat tissues. Proc Natl Acad Sci USA 73: 2559–2563, 1976 PubMed Google Scholar
Walter U: Distribution of cyclic-GMP-dependent protein kinase in various rat tissues and cell lines determined by a sensitive and specific radioimmunoassay. Eur J Biochem 118: 339–346, 1981 PubMed Google Scholar
Lohmann SM, Walter U, Miller PE, Greengard P, De Camilli P: Immunohistochemical localization of cyclic GMP-dependent protein kinase in mammalian brain. Proc Natl Acad Sci USA 78: 653–657, 1981 PubMed Google Scholar
de Jonge HR: Cyclic GMP-dependent protein kinase in intestinal brushborders. Adv Cyclic Nucleotide Res 14: 315–333, 1981 PubMed Google Scholar
Lincoln TN, Johnson RM: Possible role of cyclic GMP-dependent protein kinase in vascular smooth muscle function. Adv Cyclic Nucleotide Res 17: 285–296, 1984 Google Scholar
Morgan JP, Morgan KG: Alteration of cytoplasmic ionized calcium levels in smooth muscle by vasodilators in the ferret. J Physiol 357: 539–551, 1984 PubMed Google Scholar
Cornwell TL, Lincoln TM: Regulation of intracellular Ca2+ levels in cultured vascular smooth muscle cells: reduction of Ca2+ by atriopeptin and 8-bromo-cyclic GMP is mediated by cyclic GMP-dependent protein kinase. J Biol Chem 264: 1146–1155, 1989 PubMed Google Scholar
Wernet W, Flockerzi V, Hofmann F: The cDNA of the two isoforms of bovine cGMP-dependent protein kinase. FEBS Lett 251: 191–196, 1989 PubMed Google Scholar
Ruth P, Landgraf W, Keilbach A, May B, Egleme C, Hofmann F: The activation of expressed cGMP-dependent protein kinase isozymes Iα and Iβ is determined by the different amino-termini. Eur J Biochem 202: 1339–1344, 1991 PubMed Google Scholar
Sandberg M, Natarajan V, Ronander I, Kalderon D, Walter U, Lohmann SM, Jahnsen T: Molecular cloning and predicted fulllength amino acid sequence of the type Iβ isozyme of cGMP-dependent protein kinase from human placenta. FEBS Lett 255: 321–329, 1989 PubMed Google Scholar
Takio K, Wade RD, Smith SB, Krebs EG, Walsh KA, Titani K: Guanosine cyclic 3′,5′-phosphate-dependent protein kinase, a chimeric protein homologous with two separate protein families. Biochemistry 23: 4207–4218, 1984 PubMed Google Scholar
Francis SH, Woodford TA, Wolfe L, Corbin JD: Types Iα and I_b_ cGMP-dependent protein kinase: alternative mRNA splicing may produce different inhibitory domains. Second Messengers and Phosphoproteins 12: 301–310, 1988–89 Google Scholar
de Jonge HR, Rosen OM: Self-phosphorylation of cyclic 3′:5′-monophosphate-dependent protein kinase from bovine lung: effect of cyclic adenosine 3′:5′-monophosphate, cyclic guanosine 3′:5′-monophosphate, and histone. J Biol Chem 252: 2780–2783, 1977 PubMed Google Scholar
Lincoln TM, Flockhart DA, Corbin JD: Studies on the structure and mechanism of activation of the guanosine 3′:5′-monophosphate-dependent protein kinase. J Biol Chem 253: 6002–6009, 1978 PubMed Google Scholar
Foster JL, Guttmann J, Rosen OM: Autophosphorylation of cGMP-dependent protein kinase. J Biol Chem 256: 5029–5036, 1981 PubMed Google Scholar
Hofmann F, Flockerzi V: Characterization of phosphorylated and native cGMP-dependent protein kinase. Eur J Biochem 130: 599–603, 1983 PubMed Google Scholar
Aitken A, Hemmings BA, Hofmann F: Identification of the residues on cyclic GMP-dependent protein kinase that are autophosphorylated in the presence of cyclic AMP and cyclic GMP. Biochim Biophys Acta 790: 219–225, 1984 PubMed Google Scholar
Hofmann F, Gesheimer H-P, Göbel C: cGMP-dependent protein kinase: Autophosphorylation changes the characteristics of binding site 1. Eur J Biochem 147: 361–365 (1985) PubMed Google Scholar
Landgraf W, Hullin R, Göbel C, Hofmann F: Phosphorylation of cGMP-dependent protein kinase increases the affinity for cyclic AMP. Eur J Biochem 154: 113–117, 1986 PubMed Google Scholar
Wolfe L, Corbin JD, Francis SH: Characterization of a novel isozyme of cGMP-dependent protein kinase from bovine aorta. J Biol Chem 264: 7734–7741, 1989 PubMed Google Scholar
Francis S, Smith J, Walsh K, Kumar S, Colbran J, Corbin J: Autophosphorylation of bovine aorta type Iβ cGMP-dependent protein kinase occurs at serine-63 in the inhibitory domain of the enzyme. FASEB J 7: A1123, 1993 (Abstract ÷413) Google Scholar
Smith JA, Francis SH, Corbin JD: Activation of the type Iβ isozyme of cGMP-dependent protein kinase by preincubation with MgATP and cAMP. FASEB J 6: A315, 1992 (Abstract ÷1813) Google Scholar
Smith J, Francis S, Chu D, Corbin J: Autophosphorylation of the cGMP-dependent protein kinase type Iβ occurs at physiological concentrations of enzyme and cGMP (or cAMP). FASEB J 7: A1123, 1993 (Abstract ÷414) Google Scholar
Kemp BE, Pearson RB: Intrasteric regulation of protein kinases and phosphatases. Biochem Biophys Acta 1094: 67–76, 1991 PubMed Google Scholar
Wyatt TA, Lincoln TM, Pryzwansky KB: Vimentin is transiently co-localized with and phosphorylated by cyclic GMP-dependent protein kinase in formyl-peptide-stimulated neutrophils. J Biol Chem 266: 21274–21280, 1991 PubMed Google Scholar
Carafoli E: Intracellular calcium homeostasis. Annu Rev Biochem 56: 395–433, 1987 PubMed Google Scholar
Sutherland EW, Wosilait WD: Inactivation and activation of liver phosphorylase. Nature 175: 169–170, 1955 PubMed Google Scholar
Walsh DA, Perkins JP, Brostrom CO, Ho ES, Krebs EG: Catalysis of the phosphorylase kinase activation reaction. J Biol Chem 246: 1968–1976, 1971 PubMed Google Scholar
Cohen P, Burchell A, Foulkes JG, Cohen PTW, Vanaman TC, Nairn AC: Identification of the Ca2+-dependent modulator protein as the fourth subunit of rabbit skeletal muscle phosphorylase kinase. FEBS Lett 92: 287–293, 1978 PubMed Google Scholar
Chan K-FJ, Graves DJ: Rabbit skeletal muscle phosphorylase kinase: catalytic and regulatory properties of the active αγδ and γδ complexes. J Biol Chem 257: 5948–5955, 1982 PubMed Google Scholar
Paudel HK, Carlson GM: Inhibition of the catalytic subunit of phosphorylase kinase by its α/β subunits. J Biol Chem 262: 11912–11915, 1987 PubMed Google Scholar
Fischer EH, Alaba JO, Brautigan DL, Kerrick WGL, Malencik DA, Moeschler HJ, Picton C, Pocinwong S: Evolutionary aspects of the structure and regulation of phosphorylase kinase. In: CH Li (ed.) Versitility of Proteins. Academic Press, Orlando, 1978, pp 133–149 Google Scholar
Killilea SD, Ky NM: Purification and partial characterization of bovine heart phosphorylase kinase. Arch Biochem Biophys 221: 333–342, 1983 PubMed Google Scholar
Krebs EG, Graves DJ, Fischer EH: Factors affecting the activity of muscle phosphorylase b kinase. J Biol Chem 234: 2867–2873, 1959 PubMed Google Scholar
Angelos KL, Ramachandran C, Walsh DA: Subunit phosphorylation and activation of phosphorylase kinase in perfused rat hearts. J Biol Chem 262: 3219–3226, 1987 PubMed Google Scholar
Fitzgerald TJ, Trempe MR, Carlson GM: Autophosphorylation of the α subunit of phosphorylase kinase from rabbit skeletal muscle. J Biol Chem 262: 11239–11246, 1987 PubMed Google Scholar
King MM, Fitzgerald TJ, Carlson GM: Characterization of initial autophosphorylation events in rabbit skeletal muscle phosphorylase kinase. J Biol Chem 258: 9925–9930, 1983 PubMed Google Scholar
Wang JH, Stull JT, Huang T-S, Krebs EG: A study on the autoactivation of rabbit muscle phosphorylase kinase. J Biol Chem 251: 4521–4527, 1976 PubMed Google Scholar
Cohen P: Phosphorylation of rabbit skeletal muscle phosphorylase kinase by cyclic GMP-dependent protein kinase. FEBS Lett 119: 301–306, 1973 Google Scholar
Hayakawa T, Perkins JP, Krebs EG: Studies on the subunit structure of rabbit skeletal muscle phosphorylase kinase. Biochemistry 12: 574–580, 1973 PubMed Google Scholar
Ramachandran C, Goriz J, Waelkens E, Merlevede W, Walsh DA: The interrelationship between c-AMP-dependent α and β subunit phosphorylation in the regulation of phosphorylase kinase activity. J Biol Chem 262: 3210–3218, 1987 PubMed Google Scholar
Cohen P: The role of calcium ions, calmodulin and troponin in the regulation of phosphorylase kinase from rabbit skeletal muscle. Eur J Biochem 111: 563–574, 1980 PubMed Google Scholar
Cohen P, Picton C, Klee CB: Activation of phosphorylase kinase from rabbit skeletal muscle by calmodulin and troponin. FEBS Lett 104: 25–30, 1979 PubMed Google Scholar
Erdödi F, Bakó E, Bot G, Gergely P: Autophosphorylation of phosphorylase kinase and its regulatory function in the dephosphorylation of phosphorylase_A_. Acta Biochim Biophys Hung 22: 425–438, 1987 PubMed Google Scholar
Drummond GI, Harwood JP, Powell CA: Studies on the activation of phosphorylase in skeletal muscle by contraction and by epinephrine. J Biol Chem 244: 4235–4240, 1969 PubMed Google Scholar
Sul HS, Cooper RH, Whitehouse S, Walsh DA: Cardiac phosphorylase kinase: modulation of the activity by cAMP-dependent and cAMP-independent phosphorylation of the α' subunit. J Biol Chem 257: 3484–3490, 1982 PubMed Google Scholar
Stull JT, Nunnelly MH, Michnoff CH: Calmodulin-dependent protein kinases. In: PD Boyer, EG Krebs (eds) The Enzymes. Academic Press, Orlando, 1986, pp 113–166 Google Scholar
Kramm KE, Stull JT: The function of myosin and myosin light chain kinase phosphorylation in smooth muscle. Annu Rev Pharmacol Toxicol 25: 593–620, 1985 PubMed Google Scholar
Sellers JR, Harvey EV: Purification of myosin light chain kinase from_limulus_ muscle. Biochemistry 23: 5821–5826, 1984 PubMed Google Scholar
Korn ED: Biochemistry of actomyosin-dependent cell motility (a review). Proc Natl Acad Sci USA 75: 588–599, 1978 PubMed Google Scholar
Sellers JR, Adelstein RS: Regulation of contractile activity. In: PD Boyer, EG Krebs (eds) The Enzymes. Academic Press, Orlando, 1987, pp381–418 Google Scholar
Edelman AM, Krebs EG: Phosphorylation of skeletal muscle myosin light chain kinase by the catalytic subunit of cAMP-dependent protein kinase. FEBS Lett 138: 293–298, 1982 PubMed Google Scholar
Foyt HL, Means AR: Characterization and analysis of an apparent autophosphorylation of chicken gizzard myosin light chain kinase. J Cyclic Nucleotide Protein Phosphorylation Res 10: 143–156, 1985 Google Scholar
Wolf H, Hoffman F: Purification of myosin light chain kinase from bovine cardiac muscle. Proc Natl Acad Sci USA 77: 5852–5855, 1980 PubMed Google Scholar
Gao Z-H, Moomaw CR, Hsu J, Slaughter CA, Stull JT: Autophosphorylation of skeletal muscle myosin light chain kinase. Biochemistry 31: 6126–6133, 1992 PubMed Google Scholar
Kemp BE, Pearson RB, Guerriero V Jr, Bagchi IC, Means AR: The calmodulin binding domain of chicken smooth muscle myosin light chain kinase contains a pseudosubstrate sequence. J Biol Chem 262: 2542–2548, 1987 PubMed Google Scholar
Guess U, Mayr GW, Heilmeyer LMG Jr: Steady-state kinetics of skeletal muscle myosin light chain kinase indicate a strong down regulation by products. Eur J Biochem 153: 327–334, 1985 PubMed Google Scholar
Mayr GW, Heilmeyer LMG Jr: Shape and substructure of skeletal muscle myosin light chain kinase. Biochemistry 22: 4316–4326, 1983 PubMed Google Scholar
Kennedy MB, Greegard P: Two calcium/calmodulin-dependent protein kinases, which are highly concentrated in brain, phosphorylate protein I at distinct sites. Proc Natl Acad Sci USA 78: 1293–1297, 1981 PubMed Google Scholar
Hanson PI, Schulman H: Neuronal Ca2+/calmodulin-dependent protein kinases. Annu Rev Biochem 61: 559–601, 1992 PubMed Google Scholar
Colbran RJ, Soderling TR: Calcium/calmodulin-dependent protein kinae II. Current Topics In Cellular Regulation 31: 181–221, 1990 PubMed Google Scholar
Berman RF, Hullihan JP, Kinnier WJ, Wison JE:In vivo phosphorylation of postsynaptic density proteins. Neuroscience 13: 965–971, 1984 PubMed Google Scholar
Gurd JW, Bissoon N:In vivo phosphorylation of the postsynaptic density glycoprotein gp180. J Neurochem 45: 1136–1140, 1985 PubMed Google Scholar
Gorelick FS, Wang JKT, Lai Y, Nairn AC, Greengard P: Autophosphorylation and activation of Ca2+/calmodulin-dependent protein kinase II in intact nerve terminals. J Biol Chem 263: 17209–17212, 1988 PubMed Google Scholar
Ohta Y, Ohba T, Fukunaga K, Miyamoto E: Serum and growth factors rapidly elicit phosphorylation of the Ca2+/calmodulin-dependent protein kinase II in intact quiescent rat 3Y1 cells. J Biol Chem 263: 11540–11547, 1988 PubMed Google Scholar
Ahmed Z, DePaoli-Roach AA, Roach PJ: Purification and characterization of a rabbit liver calmodulin-dependent protein kinase able to phosphorylate glycogen synthase. J Biol Chem 257: 8348–8355, 1982 PubMed Google Scholar
Bennet MK, Erondo NE, Kennedy MB: Purification and characterization of a calmodulin-dependent protein kinase that is highly concentrated in brain. J Biol Chem 258: 12735–12744, 1983 PubMed Google Scholar
Schworer CM, McClure RW, Soderling TR: Calmodulin-dependent protein kinases purified from rat brain and rabbit liver. Arch Biochem Biophys 242: 137–145, 1985 PubMed Google Scholar
McGuinness TL, Lai Y, Greegard P: Ca2+/calmodulin-dependent protein kinase II: Isozymic forms from rat forebrain and cerebellum. J Biol Chem 260: 1696–1704, 1985 PubMed Google Scholar
Kuret J, Schulman H: Mechanism of autophosphorylation of the multifunctional Ca2+/calmodulin-dependent protein kinase. J Biol Chem 260: 6427–6433, 1985 PubMed Google Scholar
Kwiatkowski AP, Shell DJ, King MM: The role of autophosphorylation in activation of the type II calmodulin-dependent protein kinase. J Biol Chem 263: 6484–6486, 1988 PubMed Google Scholar
LeVine H III, Sahyoun NE, Cautrecasas P: Calmodulin binding to the cytoskeletal neuronal calmodulin-dependent protein kinase is regulated by autophosphorylation. Proc Natl Acad Sci USA 82: 287–291, 1985 PubMed Google Scholar
Schworer CM, Colbran RJ, Keefer JR, Soderling TR: Ca2+/calmodulin-dependent protein kinase II: identification of a regulatory autophosphorylation site adjacent to the inhibitory and calmodulin-binding domains. J Biol Chem 263: 13486–13489, 1988 PubMed Google Scholar
Thiel G, Czernik AJ, Gorelick F, Nairn AC, Greengard P: Ca2+/calmodulin-dependent protein kinase II: identification of threonin-286 as the autophosphorylation site in the α subunit associated with the generation of Ca2+-independent activity. Proc Natl Acad Sci USA 85: 6337–6341, 1988 PubMed Google Scholar
Miller SG, Patton BL, Kennedy MB: Sequences of autophosphorylation sites in neuronal type II CaM kinase that control Ca2+-independent activity. Neuron 1: 593–604, 1988 PubMed Google Scholar
Lou LL, Schulman H: Distinct autophosphorylation sites sequentially produce autonomy and inhibition of the multifunctional Ca2+/calmodulin-depedent protein kinase. J Neurosci 9: 2020–2032, 1989 PubMed Google Scholar
Colbran RJ, Schworer CM, Hashimoto Y, Fong Y-L, Rich DP, Smith KM, Soderling TR: Calcium/calmodulin-dependent protein kinase II. Biochem J 258: 313–325, 1989 PubMed Google Scholar
Hashimoto Y, Schworer CM, Colbran RJ, Soderling TR: Autophosphorylation of Ca2+/calmodulin-dependent protein kinase II: effects on total and Ca2+-independent activities and kinetic parameters. J Biol Chem 262: 8051–8055, 1987 PubMed Google Scholar
Patton BL, Miller SG, Kennedy MB: Activation of type II calcium/calmodulin-dependent protein kinase by Ca2+-/calmodulin is inhibited by autophosphorylation of threonine within the calmodulin-binding domain. J Biol Chem 265: 11204–11212, 1990 PubMed Google Scholar
Colbran RJ, Soderling TR: Calcium/calmodulin-independent autophosphorylation sites of calcium/calmodulin-dependent protein kinase II: studies on the effect of phosphorylation of threonine 305/306 and serine 314 on calmodulin binding using synthetic peptides. J Biol Chem 265: 11213–11219, 1990 PubMed Google Scholar
Hanson P, Schulman H: Inhibitory autophosphorylation of multifunctional Ca2+/calmodulin-dependent protein kinase analyzed by site-directed mutagenesis. J Biol Chem 267: 17216–17224, 1992 PubMed Google Scholar
Colbran RJ: Inactivation of Ca2+/calmodulin-dependent protein kinase II by basal autophosphorylation. J Biol Chem 268: 7163–7170, 1993 PubMed Google Scholar
Lai Y, Nairn AC, Greengard P: Autophosphorylation reversibly regulates the Ca2+/calmodulin-dependent protein kinase II. Proc Natl Acad Sci USA 83: 4253–4257, 1986 PubMed Google Scholar
Miller SG, Kennedy MB: Regulation of brain type II Ca2+/calmodulin-dependent protein kinase by autophosphorylation: a Ca2+-triggered molecular switch. Cell 44: 861–870, 1986 PubMed Google Scholar
Schworer CM, Colbran RJ, Soderling TR: Reversible generation of a Ca2+-independent form of Ca2+(calmodulin)-dependent protein kinase II by an autophosphorylation mechanism. J Biol Chem 261: 8581–8584, 1987 Google Scholar
Payne ME, Fong Y-L, Ono T, Colbran RJ, Kemp BE, Soderling TR, Means AR: Calcium/calmodulin-dependent protein kinase II: characterization of distinct calmodulin binding and inhibitory domains. J Biol Chem 263: 7190–7195, 1988 PubMed Google Scholar
Colbran RJ, Fong Y-L, Schworer CM, Soderling TR: Regulatory interactions of the calmodulin-binding, inhibitory, and autophosphorylation domains of Ca2+/calmodulin-dependent protein kinase II. J Biol Chem 263: 18145–18151, 1988 PubMed Google Scholar
Colbran RJ, Smith MK, Schworer CM, Fong Y-L, Soderling TR: Regulatory domain of calcium/calmodulin-dependent protein kinase II: mechanism of inhibition and regulation by phosphorylation. J Biol Chem 264: 4800–4804, 1989 PubMed Google Scholar
Fong Y-L, Taylor WL, Means AR, Soderling TR: Studies of the regulatory mechanism of Ca2+/calmodulin-dependent protein kinase II: mutation of threonine 286 to alanine and aspartate. J Biol Chem 264: 16759–16763, 1989 PubMed Google Scholar
Meyer T, Hanson PI, Stryer L, Schulman H: Calmodulin trapping by calcium-calmodulin-dependent protein kinase. Science 256: 1199–1202, 1992 PubMed Google Scholar
Madison DV, Malenka RC, Nicoll RA: Phorbol esters block a voltage-sensitive chloride current in hippocampal pyramidal cells. Nature 321: 695–697, 1986 PubMed Google Scholar
Burgess SK, Sahyoun N, Blanchard SG, LeVine H III, Chang K-J, Cuatrecasas P: Phorbol ester receptors and protein kinase C in primary neuronal cultures: development and stimulation of endogenous phosphorylation. J Cell Biol 102: 312–319, 1986 PubMed Google Scholar
Nishizuka Y: Studies and perspectives of protein kinase C. Science 233: 305–312, 1986 PubMed Google Scholar
Huang K-P, Huang FL, Mahoney CW, Chen K-H: Protein kinase C subtypes and their respective roles. Prog in Brain Res 89: 143–155, 1991 Google Scholar
Nakanishi H, Exton JH: Purification and characterization of the ζ isoform of protein kinase C from bovine kidney. J Biol Chem 267: 16347–16354, 1992 PubMed Google Scholar
Leibersperger H, Gschwendt M, Marks F: Purification and characterization of a calcium-unresponsive, phorbol ester/phospholipid-activated protein kinase from porcine spleen. J Biol Chem 265: 16108–16115, 1990 PubMed Google Scholar
Schaap D, Parker PJ: Expression, purification, and characterization of protein kinase-ε. J Biol Chem 265: 7301–7307, 1990 PubMed Google Scholar
Osada S-I, Mizuno K, Saido TC, Akita Y, Suzuki K, Kuroki T, Ohno S: A phorbol ester receptor/protein kinase, nPKCη, a new member of the protein kinase C family predominantly expressed in lung and skin. J Biol Chem 265: 22434–22440, 1990 PubMed Google Scholar
Huang K-P, Chang K-FJ, Singh TJ, Nakabayashi H, Huang FL: Autophosphorylation of rat brain Ca2+-activated and phospholipid dependent protein kinase. J Biol Chem 261: 12134–12140, 1986 PubMed Google Scholar
Newton AC, Koshland DE Jr: Protein kinase C autophosphorylation by an intrapeptide reaction. J Biol Chem 262: 10185–10188, 1987 PubMed Google Scholar
Hannun YA, Bell RM: Rat brain protein kinase C: kinetic analysis of substrate dependence, allosteric regulation, and autophosphorylation. J Biol Chem 265: 2962–2972, 1990 PubMed Google Scholar
Kaibuchi K, Takai Y, Nishizuka Y: Protein kinase C and calcium ion in mitogenic response of macrophage-depleted human peripheral lymphocytes. J Biol Chem 260: 1366–1369, 1985 PubMed Google Scholar
Woodgett JR, Hunter T: Immunological evidence for two physiological forms of protein kinase C. Mol Cell Biol 7: 85–96, 1987 PubMed Google Scholar
Kubo K, Ohno S, Suzuki K: Primary structures of human protein kinase Cβ1 and βII differ only in their C-terminal sequences. FEBS Lett 223: 138–142, 1987 PubMed Google Scholar
Flint AJ, Paladini RD, Koshland DE Jr: Autophosphorylation of protein kinase C at three separated regions of its primary sequence. Science 249: 408–411, 1990 PubMed Google Scholar
Mochly-Rosen D, Koshland DE Jr: Domain structure and phosphorylation of protein kinase C. J Biol Chem 262: 2291–2297, 1987 PubMed Google Scholar
Wolf M, Cuatrecasas P, Sahyoun N: Interaction of protein kinase C with membranes is regulated by Ca2+, phorbol esters, and ATP. J Biol Chem 260: 15718–15722, 1985 PubMed Google Scholar
Ohno S, Konno Y, Akita Y, Yano A, Suzuki K: A point mutation at the putative ATP-binding site of protein kinase Cα abolishes the kinase activity and renders it down-regulation-insensitive: a molecular link between autophosphorylation and down-regulation. J Biol Chem 265: 6296–6300, 1990 PubMed Google Scholar
Chen SG, Kulju D, Halt S, Murakami K: Phosphotidylcholine-dependent protein kinase C activation: effects of cis-fatty acid and diacylgycerol on synergism autophosphorylation and Ca2+-dependency. Biochem J 284: 221–226, 1992 PubMed Google Scholar
El Touny S, Khan W, Hannun Y: Regulation of platelet protein kinase C by oleic acid: kinetic analysis of allosteric regulation and effects on autophosphorylation, phorbol ester binding, and susceptibility to inhibition. J Biol Chem 265: 16437–16443, 1990 PubMed Google Scholar
Szamel M, Rehermann B, Krebs B, Kurrle R, Resch K: Activation signals in human lymphocytes: incorporation of polyunsaturated fatty acids into plasm membrane phospholipids regulates IL-2 synthesis via sustained activation of protein kinase C. J Immunol 143: 2806–2813, 1989 PubMed Google Scholar
Bazzi MD, Nelsestuen GL: Autophosphorylation of protein kinase C may require a high order of protein-phospholipid aggreates. J Biol Chem 267: 22891–22896, 1992 PubMed Google Scholar
Sagata N, Oskarsson M, Copeland T, Brumbaugh J, Vande Woude GF: Function of c-mos proto-oncogene product in meiotic maturation in_Xenopus_ oocytes. Nature 335: 519–525, 1988 PubMed Google Scholar
Sagata N, Watanabe N, Vande Woude GF, Ikawa Y: The c-mos proto-oncogene product is a cytostatic factor responsible for meiotic arrest in vertebrate eggs. Nature 342: 512–518, 1989 PubMed Google Scholar
Sagata N, Daar I, Oskarsson M, Showalter SD, Vande Woude GF: The product of the_mos_ proto-oncogene as a candidate ‘initiator’ for oocyte maturation. Science 245: 643–646, 1989 PubMed Google Scholar
Watanabe N, Vande Woude GF, Ikawa Y, Sagata N: Specific proteolysis of the c-mos proto-oncogene product by calpain on fertilization of_Xenopus_ eggs. Nature 342: 505–511, 1989 PubMed Google Scholar
Barrett CB, Schroetke RM, Van der Hoorn FA, Nordeen SK, Maller JL: Ha-ra Val12,Thr-59 activates S6 kinase and p34cdc2 kinase in_Xenopus_ oocytes: evidence for c-mos xe-dependent and-independent pathways. Mol Cell Biol 10: 310–315, 1990 PubMed Google Scholar
Nishizawa M, Okazaki K, Furuno N, Watanabe N, Sagata N: The ‘second-codon rule’ and autophosphorylation govern the stability and activity of Mos during the meiotic cell cycle in_Xenopus_ oocytes. EMBO J 11: 2433–2446, 1992 PubMed Google Scholar
Al-Bagdadi F, Singh B, Arlinghaus RB: Evidence for involvement of the protein kinase C pathway in the activation of p37v-mos protein kinase. Oncogene 5: 1251–1257, 1990 PubMed Google Scholar
Singh B, Arlinghaus RB: The_mos_ proto-oncogene product: its role in oocyte maturation, metaphase arrest, and neoplastic transformation. Mol Carcinog 6: 82–189, 1992 Google Scholar
Ernst V, Levin DH, Leroux A, London IM: Site-specific phosphorylation of the α subunit of eukaryotic initiation factor eIF-2 by the heme-regulated and double-stranded RNA-activated eIF-2α kinases from rabbit reticulocyte lysates. Proc Natl Acad Sci USA 77: 1286–1290, 1980 PubMed Google Scholar
Sen GC, Taira H, Lengyel P: Interferon, double-stranded RNA, and protein phosphorylation: characteristics of a double-stranded RNA-activated protein kinase system partially purified from interferon-treated ehrlich ascites tumor cells. J Biol Chem 253: 5915–5921, 1978 PubMed Google Scholar
Fagard R, London IM: Relationship between phosphorylation and activity of heme-regulated eukaryotic initiation factor 2α kinase. Proc Natl Acad Sci USA 78: 866–870, 1981 PubMed Google Scholar
Farrell PJ, Hunt T, Jackson RJ: Analysis of phosphorylation of protein synthesis initiation factor eIF-2 by two-dimensional gel electrophoresis. Eur J Biochem 89: 517–521, 1978 PubMed Google Scholar
Ernst V, Levin DH, London IM:In situ phosphorylation of the α subunit of eukaryotic initiation factor 2 in reticulocyte lysates inhibited by heme deficiency, double-stranded RNA, oxidized glutathione, or the heme-regulated protein kinase. Proc Natl Acad Sci USA 76: 2118–2122, 1979 PubMed Google Scholar
Henderson AB, Miller AH, Hardesty B: Multistep regulatory system for activation of a cyclic AMP-independent eukaryotic initiation factor 2 kinase. Proc Natl Acad Sci USA 76: 2605–2609, 1979 PubMed Google Scholar
Wallis MH, Kramer G, Hardesty B: Partial purification and characterization of a 90000-dalton peptide involved in activation of the eIF-2α protein kinase of the hemin-controlled translational repressor. Biochemistry 19: 798–804, 1980 PubMed Google Scholar
Gross M, Mendelewski J: Control of protein synthesis by hemin: an association between the formation of the hemin-controlled translational repressor and the phosphorylation of a 100000 molecular weight protein. Biochim Biophys Acta 520: 650–663, 1978 PubMed Google Scholar
Ernst V, Levin DH, Foulkes JG, London IM: Effects of skeletal muscle protein phosphatase inhibitor-2 on protein synthesis and protein phosphorylation in rabbit reticulocyte lysates. Proc Natl Acad Sci USA 79: 7096–7096, 1982 Google Scholar
Galabru J, Hovanessian AG: Two interferon-induced proteins are involved in the protein kinase complex dependent on double-stranded RNA. Cell 43: 685–694, 1985 PubMed Google Scholar
Foulkes JG, Ernst V, Levin DH: Separation and identification of type 1 and type 2 protein phosphatases from rabbit reticulocyte lysates. J Biol Chem 258: 1439–1443, 1983 PubMed Google Scholar
Petryshyn R, Levin DH, London IM: Regulation of double-stranded RNA-activated eukaryotic initiation factor 2α kinase by type 2 protein phosphatase in reticulocyte lysates. Proc Natl Acad Sci USA 79: 6512–6516, 1982 PubMed Google Scholar
London IM, Levin DH, Matts RL, Thomas NSB, Petryshyn R, Chen J-J: Regulation of protein synthesis. In: P.D. Boyer, EG Krebs (eds) The Enzymes. Academic Press, Orlando, 1987, pp 359–380 Google Scholar
Katze MG, DeCorato D, Safer B, Galabru J, Hovanessian AG: Adenovirus VAI RNA complexes with the 68000 Mr protein kinase to regulate its autophosphorylation and activity. EMBO J 6: 689–697, 1987 PubMed Google Scholar
Petryshyn R, Chen J-J, London IM: Growth-related expression of a double-stranded RNA-dependent protein kinase in 3T3 cells. J Biol Chem 259: 14736–14742, 1984 PubMed Google Scholar
Wilden U, Hall SW, Kühn H: Phosphodiesterase activation by photoexcited rhodopsin is quenched when rhodopsin is phosphorylated and binds the intrinsic 48-kDa protein of rod outer segments. Proc Natl Acad Sci USA 83: 1174–1178, 1986 PubMed Google Scholar
Wilden U, Wüst E, Weyand I, Kühn H: Rapid affinity purification of retinal arrestin (48kDa protein) via its light-depedent binding to phosphorylated rhodopsin. FEBS Lett 207: 292–295, 1986 PubMed Google Scholar
Lee RH, Brown BM, Lolley RN: Autophosphorylation of rhodopsin kinase from retinal rod outer segments. Biochemistry 21: 3303–3307, 1982 PubMed Google Scholar
Palczewski K, McDowell JH, Hargrave PA: Autophosphorylation of rhodopsin kinase and its phosphorylation by protein kinases A and C. FASEB J 2: A994, 1988 (Abstract÷4058) Google Scholar
Kelleher DJ, Johnson GL: Characterization of rhodopsin kinase purified from bovine rod outer segments. J Biol Chem 265: 2632–2639, 1990 PubMed Google Scholar
Palczewski K, Buczylko J, Van Hooser P, Carr SA, Huddleston MJ, Crabb JW: Identification of the autophosphorylation sites in rhodopsin kinase. J Biol Chem 267: 18991–18998, 1992 PubMed Google Scholar
Lorenz W, Inglese J, Palczewski K, Onorato JJ, Caron MG, Lefkowitz RJ: The receptor kinase family: primary structure of rhodopsin kinase reveals similarities to the β-adrenergic receptor kinase. Proc Natl Acad Sci USA 88: 8715–8719, 1991 PubMed Google Scholar
Buczylko J, Gutmann C, Palczewski K: Regulation of rhodopsin kinase by autophosphorylation. Proc Natl Acad Sci USA 88: 2568–2572, 1991 PubMed Google Scholar
Yarden Y, Ullrich A: Growth factor receptor tyrosine kinases. Ann Rev Biochem 57: 443–478, 1988 PubMed Google Scholar
Rosen OM, Herrera R, Olowe Y, Petruzzelli LM, Cobb MH: Phosphorylation activates the insulin receptor tyrosine protein kinase. Proc Natl Acad Sci USA 80: 3237–3240, 1983 PubMed Google Scholar
White MF, Shoelson SE, Keutmann H, Kahn CR: A cascade of tyrosine autophosphorylation in the β-subunit activates the phosphotransferase of the insulin receptor. J Biol Chem 263: 2969–2980, 1988 PubMed Google Scholar
Herrera R, Rosen OM: Autophosphorylation of the insulin receptor_in vitro_. J Biol Chem 261: 11980–11985, 1986 PubMed Google Scholar
Perlman R, Bottaro DP, White MF, Kahn CR: Conformational changes in the α- and β-subunits of the insulin receptor identified by anti-peptide antibodies. J Biol Chem 264: 8946–8950, 1989 PubMed Google Scholar
Debant A, Clauser E, Ponzio G, Filloux C, Auzan C, Contreres J-O, Rossi B: Replacement of insulin receptor tyrosine residues 1162 and 1163 does not alter the mitogenic effect of the hormone. Proc Natl Acad Sci USA 85: 8032–8036, 1988 PubMed Google Scholar
Desbois C, Capeau J, Hainault I, Wicek D, Reynet C, Veissiere D, Caron M, Picard J, Guerre-Millo M, Cherqui G: Differential role of insulin receptor autophosphorylation sites 1162 and 1163 in long-term insulin stimulation of glucose transport, glycogenolysis, and protein synthesis. J Biol Chem 267: 13488–13497, 1992 PubMed Google Scholar
McClain DM, Maegawa H, Levy J, Huecksteadt T, Dull TJ, Lee J, Ullrich A, Olefsky JM: Properties of a human insulin receptor with a COOH-terminal truncation: I. insulin binding, autophosphorylation, and endocytosis. J Biol Chem 263: 8904–8911, 1988 PubMed Google Scholar
Maegawa H, McClain DM, Friedenberg C, Olefsky JM, Napier M, Lipiar T, Dull TJ, Lee J, Ullrich A: Properties of a human insulin receptor with a COOH-terminal truncation: II. truncated receptors have normal kinase activity but are defective in signalling metabolic effects. J Biol Chem 263: 8912–8917, 1988 PubMed Google Scholar
Thies RS, Ullrich A, McClain DA: Augmented mitogenesis and impaired metabolic signaling mediated by a truncated insulin receptor. J Biol Chem 264: 12820–12825, 1989 PubMed Google Scholar
Takata Y, Webster NJG, Olefsky JM: Mutation of the two carboxyl-terminal tyrosines results in an insulin receptor with normal metabolic signaling but enhanced mitogenic signaling properties. J Biol Chem 266: 9135–9139, 1991 PubMed Google Scholar
Takata Y, Webster NJG, Olefsky JM: Intracellular signaling by a mutant human insulin receptor lacking the carboxyl-terminal tyrosine autophosphorylation sites. J Biol Chem 267: 9065–9070, 1992 PubMed Google Scholar
Argetsinger LS, Shafer JA: The reversible and irreversible autophosphorylations of insulin receptor kinase. J Biol Chem 267: 22095–22101, 1992 PubMed Google Scholar
Akiyama T, Matsuda S, Namba Y, Saito T, Toyoshima K, Yamamoto T: The transforming potential of c-erbB-2 protein is regulated by its autophosphorylation at the carboxyl-terminal domain. Mol Cell Biol 11: 833–842, 1991 PubMed Google Scholar
Downward J, Parker P, Waterfield MD: Autophosphorylation sites on the epidermal growth factor receptor. Nature 311: 483–485, 1984 PubMed Google Scholar
Hsuan JJ, Totty N, Waterfield MD: Identification of a novel autophosphorylation site (P4) on the epidermal growth factor receptor. Biochem J 262: 659–663, 1989 PubMed Google Scholar
Margolis BL, Lax I, Kris R, Dombalagian M, Honegger AM, Howk R, Givol D, Ulrich A, Schlessinger J: All autophosphorylation sites of epidermal growth factor (EGF) receptor and HER/neu are located in their carboxyl-terminal tails: identification of a novel site in EGF receptor. J Biol Chem 264: 10667–10671, 1989 PubMed Google Scholar
Sorkin A, Waters C, Overholser KA, Carpenter G: Multiple autophosphorylation site mutations of the epidermal growth factor receptor: analysis of kinase activity and endocytosis. J Biol Chem 266: 8355–8362, 1991 PubMed Google Scholar
Helin K, Beguinot L: Internalization and down-regulation of the human epidermal growth factor receptor are regulated by the carboxyl-terminal tyrosines. J Biol Chem 266: 8363–8368, 1991 PubMed Google Scholar
Sorkin A, Helin K, Waters CM, Carpenter G, Beginot L: Multiple autophosphorylation sites of the epidermal growth factor receptor are essential for receptor kinase activity and internalization: contrasting significance of tyrosine 992 in the native and truncated receptors. J Biol Chem 267: 8672–8678, 1992 PubMed Google Scholar
Coughlin SR, Escobedo JA, Williams LT: Role of phosphatidylinositol kinase in PDGF receptor signal transduction. Science 243: 1191–1194, 1989 PubMed Google Scholar
Kaplan DR, Morrison DK, Wong G, McCormick F, Williams LT: PDGF β-receptor stimulates tyrosine phosphorylation of GAP and association of GAP with a signaling complex. Cell 61: 125–133, 1990 PubMed Google Scholar
Kashishian A, Kazlauskas A, Cooper JA: Phosphorylation sites in the PDGF receptor with different specificities for binding GAP and PI3 kinase_in vivo_. EMBO J 11: 1373–1382, 1992 PubMed Google Scholar
Courtneidge SA, Kypta RM, Cooper JA, Kazlauskas A: Plateletderived growth factor receptor sequences important for binding of_src_ family tyrosine kinases. Cell Growth Diff 2: 483–486, 1991 PubMed Google Scholar
Rönnstrand L, Mori S, Arridsson A-K, Eriksson A, Wernstedt C, Hellman U, Claesson-Welsh L, Heldin C-H: Identification of two C-terminal autophosphorylation sites in the PDGF β-receptor: involvement in the interaction with phospholipase C-γ. EMBO J 11: 3911–3919, 1992 PubMed Google Scholar
Koch CA, Anderson D, Moran MF, Ellis C, Pawson T: SH2 and SH3 domains: elements that control interactions of cytoplasmic signaling proteins. Science 252: 668–674, 1991 PubMed Google Scholar
Bardelli A, Maina F, Gout I, Fry MJ, Waterfield MD, Comoglio PM, Ponzetta C: Autophosphorylation promotes complex formation of recombinant hepatocyte growth factor receptor with cytoplasmic effectors containing SH2 domains. Oncogene 7: 1973–1978, 1992 PubMed Google Scholar
Lee BA, Donoghue DJ: Membrane-anchored form of v-SIS/PDGFR-B induces mitogenesis without detectable PDGF receptor autophosphorylation. J Cell Biol 113: 361–370, 1991 PubMed Google Scholar
Quiñones MA, Mundschau LJ, Rake JB, Faller DV: Dissociation of platelet-derived growth factor (PDGF) receptor autophosphorylation from other PDGF-mediated second messenger events. J Biol Chem 266: 14055–14063, 1991 PubMed Google Scholar
Selva E, Raden DL, Davis RJ: Mitogen-activated protein kinase stimulation by tyrosine kinase-negative epidermal growth factor receptor. J Biol Chem 268: 2250–2254, 1993 PubMed Google Scholar
Veillette A, Bolen JB: Src-related protein kinases. In: C Benz, E Liu (eds) Oncogenes. Kluwer Academic Publishers, Norwell, Mass, 1989, pp 121–142 Google Scholar
Purchio AF: Evidence that pp60_src_, the product of the Rous sarcoma virus_src_ gene, undergoes autophosphorylation. J Virol 41: 1–7, 1982 PubMed Google Scholar
Sugimoto Y, Erikson E, Graziani Y, Erikson RL: Inter- and intramolecular interactions of highly purified Rous sarcoma virus-transforming protein, pp60v-src. J Biol Chem 260: 13838–13843, 1985 PubMed Google Scholar
Jove R, Kornbluth S, Hanafusa H: Enzymatically inactive p60c-src mutant with altered ATP-binding site is fully phosphorylated in its carboxy-terminal regulatory region. Cell 50: 937–943, 1987 PubMed Google Scholar
Courtneidge SA: Activation of the pp60c-src kinase by middle T antigen binding or by dephosphorylation. EMBO J 4: 1471–1477, 1985 PubMed Google Scholar
Cooper JA, King CS: Dephosphorylation or antibody binding to the carboxy terminus stimulates pp60c-src. Mol Cell Biol 6: 4467–4477, 1986 PubMed Google Scholar
Hunter T: A tail to two_src_'s: mutatis mutandis. Cell 49: 1–4, 1987 PubMed Google Scholar
Piwnica-Worms H, Saunders KB, Roberts TM, Smith AE, Cheng SH: Tyrosine phosphorylation regulates the biochemical and biological properties of pp60c-src. Cell 49: 75–82, 1987 PubMed Google Scholar
Kmiecik TE, Shalloway D: Activation and suppression of pp60c-src transforming ability by mutation of its primary sites of tyrosine phosphorylation. Cell 49: 65–73, 1987 PubMed Google Scholar
Tanaka A, Fujita DJ: Expression of molecularly cloned human c-src oncogene by using a replication-competent retroviral vector. Mol Cell Biol 6: 3900–3909, 1986 PubMed Google Scholar
Jove R, Hanafusa H: Cell transformation by the viral_src_ oncogene. Annu Rev Cell Biol 3: 31–56, 1987 PubMed Google Scholar
Smart JE, Oppermann H, Czernilofsky AP, Purchio AF, Erikson RL, Bishop JM: Characterization of sites for tyrosine phosphorylation in the transforming protein of Rous sarcoma virus (pp60v-src) and its normal cellular homologue (pp60c-src). Proc Natl Acad Sci USA 78: 6013–6017, 1981 PubMed Google Scholar
Snyder MA, Bishop JM, Colby WW, Levinson AD: Phosphorylation of tyrosine-416 is not required for the transforming properties and kinase activity of pp60v-src. Cell 32: 891–901, 1983 PubMed Google Scholar
Kmiecik TE, Johnson PJ, Shalloway D: Regulation by the autophosphorylation site in overexpressed pp60c-src. Mol Cell Biol 8: 4541–4546, 1988 PubMed Google Scholar
Cantley LC, Auger KR, Carpenter C, Duckworth B, Graziani A, Kapeller R, Soltoff S: Oncogenes and signal transduction. Cell 64: 281–302, 1991 PubMed Google Scholar
Rousell RR, Brodeur SR, Shalloway D, Laudano AP: Selective binding of activated pp60c-src by an immobilized synthetic phosphopeptide modeled on the carboxyl terminus of pp60c-src. Proc Natl Acad Sci USA 88: 10696–10700, 1991 PubMed Google Scholar
Fukami Y, Sato K-I, Ikeda K, Kamisango K, Koizumi K, Matsuno T: Evidence for autoinhibitory regulation of the c-src gene product: a possible interaction between the src homology 2 domain and autophosphorylation. J Biol Chem 268: 1132–1140, 1993 PubMed Google Scholar
Sato K-I, Miki S, Tachibana H, Hayashi F, Akiyama T, Fukami Y: A synthetic peptide corresponding to residues 137 to 157 of p60v-src inhibits tyrosine-specific protein kinases. Biochem Biophys Res Commun 171: 1152–1159, 1990 PubMed Google Scholar
Rudd CE, Trevillyan JM, Dasgupta JD, Wong LL, Schlossman SF: The CD4 receptor is complexed in detergent lysates to a protein-tyrosine kinase (pp58) from human T lymphocytes. Proc Natl Acad Sci USA 85: 5190–5194, 1988 PubMed Google Scholar
Veillette A, Bookman MA, Horak EM, Bolen JB: The CD4 and CD8 T cell surface antigens are associated with the internal membrane tyrosine-protein kinase p56_lck_. Cell 55: 301–308, 1988 PubMed Google Scholar
Amrein K, Sefton BM: Mutation of a site of tyrosine phosphorylation in the lymphocyte-specific tyrosine protein kinase, p56_lck_, reveals its oncogenic potential in fibroblasts. Proc Natl Acad Sci USA 85: 4247–4251, 1988 PubMed Google Scholar
Marth JD, Cooper JA, King CS, Ziegler SF, Tinker DA, Overell RW, Krebs EG, Perlmutter RM: Neoplastic transformation induced by an activated lymphocyte-specific protein tyrosine kinase (pp56_lck_). Mol Cell Biol 8: 540–550, 1988 PubMed Google Scholar
Veillette A, Fournal M: The CD4 associated tyrosine protein kinase p56lck is positively regulated through its site of autophosphorylation. Oncogene 5: 1455–1462, 1991 Google Scholar
Robinson-Steiner AM, Corbin JD: Protein phosphorylation in the heart. In: HA Fozzard (ed.) The Heart and Cardiovascular System. Raven Press, New York, 1986, pp 887–910 Google Scholar