The leukocyte common antigen (CD45): a putative receptor-linked protein tyrosine phosphatase. (original) (raw)
Proc Natl Acad Sci U S A. 1988 Oct; 85(19): 7182–7186.
Department of Biochemistry, University of Washington, Seattle 98195.
Abstract
A major protein tyrosine phosphatase (PTPase 1B) has been isolated in essentially homogeneous form from the soluble and particulate fractions of human placenta. Unexpectedly, partial amino acid sequences displayed no homology with the primary structures of the protein Ser/Thr phosphatases deduced from cDNA clones. However, the sequence is strikingly similar to the tandem C-terminal homologous domains of the leukocyte common antigen (CD45). A 157-residue segment of PTPase 1B displayed 40% and 33% sequence identity with corresponding regions from cytoplasmic domains I and II of human CD45. Similar degrees of identity have been observed among the catalytic domains of families of regulatory proteins such as protein kinases and cyclic nucleotide phosphodiesterases. On this basis, it is proposed that the CD45 family has protein tyrosine phosphatase activity and may represent a set of cell-surface receptors involved in signal transduction. This suggests that the repertoire of signal transduction mechanisms may include the direct control of an intracellular protein tyrosine phosphatase, offering the possibility of a regulatory balance with those protein tyrosine kinases that act at the internal surface of the membrane.
Full text
Full text is available as a scanned copy of the original print version. Get a printable copy (PDF file) of the complete article (1.1M), or click on a page image below to browse page by page. Links to PubMed are also available for Selected References.
Images in this article
Click on the image to see a larger version.
Selected References
These references are in PubMed. This may not be the complete list of references from this article.
- Carpenter G. Receptors for epidermal growth factor and other polypeptide mitogens. Annu Rev Biochem. 1987;56:881–914. [PubMed] [Google Scholar]
- White MF, Shoelson SE, Keutmann H, Kahn CR. A cascade of tyrosine autophosphorylation in the beta-subunit activates the phosphotransferase of the insulin receptor. J Biol Chem. 1988 Feb 25;263(6):2969–2980. [PubMed] [Google Scholar]
- Chou CK, Dull TJ, Russell DS, Gherzi R, Lebwohl D, Ullrich A, Rosen OM. Human insulin receptors mutated at the ATP-binding site lack protein tyrosine kinase activity and fail to mediate postreceptor effects of insulin. J Biol Chem. 1987 Feb 5;262(4):1842–1847. [PubMed] [Google Scholar]
- Ebina Y, Araki E, Taira M, Shimada F, Mori M, Craik CS, Siddle K, Pierce SB, Roth RA, Rutter WJ. Replacement of lysine residue 1030 in the putative ATP-binding region of the insulin receptor abolishes insulin- and antibody-stimulated glucose uptake and receptor kinase activity. Proc Natl Acad Sci U S A. 1987 Feb;84(3):704–708. [PMC free article] [PubMed] [Google Scholar]
- Chen WS, Lazar CS, Poenie M, Tsien RY, Gill GN, Rosenfeld MG. Requirement for intrinsic protein tyrosine kinase in the immediate and late actions of the EGF receptor. Nature. 328(6133):820–823. [PubMed] [Google Scholar]
- Moolenaar WH, Bierman AJ, Tilly BC, Verlaan I, Defize LH, Honegger AM, Ullrich A, Schlessinger J. A point mutation at the ATP-binding site of the EGF-receptor abolishes signal transduction. EMBO J. 1988 Mar;7(3):707–710. [PMC free article] [PubMed] [Google Scholar]
- Snyder MA, Bishop JM, McGrath JP, Levinson AD. A mutation at the ATP-binding site of pp60v-src abolishes kinase activity, transformation, and tumorigenicity. Mol Cell Biol. 1985 Jul;5(7):1772–1779. [PMC free article] [PubMed] [Google Scholar]
- Hannink M, Donoghue DJ. Lysine residue 121 in the proposed ATP-binding site of the v-mos protein is required for transformation. Proc Natl Acad Sci U S A. 1985 Dec;82(23):7894–7898. [PMC free article] [PubMed] [Google Scholar]
- Weinmaster G, Zoller MJ, Pawson T. A lysine in the ATP-binding site of P130gag-fps is essential for protein-tyrosine kinase activity. EMBO J. 1986 Jan;5(1):69–76. [PMC free article] [PubMed] [Google Scholar]
- Tonks NK, Diltz CD, Fischer EH. Purification of the major protein-tyrosine-phosphatases of human placenta. J Biol Chem. 1988 May 15;263(14):6722–6730. [PubMed] [Google Scholar]
- Tonks NK, Diltz CD, Fischer EH. Characterization of the major protein-tyrosine-phosphatases of human placenta. J Biol Chem. 1988 May 15;263(14):6731–6737. [PubMed] [Google Scholar]
- Ingebritsen TS, Cohen P. The protein phosphatases involved in cellular regulation. 1. Classification and substrate specificities. Eur J Biochem. 1983 May 2;132(2):255–261. [PubMed] [Google Scholar]
- Thomas M, Shackelford D, Ralph S, Trowbridge I. Structural studies of T200 glycoprotein and the IL-2 receptor. J Recept Res. 1987;7(1-4):133–155. [PubMed] [Google Scholar]
- Friedman M, Krull LH, Cavins JF. The chromatographic determination of cystine and cysteine residues in proteins as s-beta-(4-pyridylethyl)cysteine. J Biol Chem. 1970 Aug 10;245(15):3868–3871. [PubMed] [Google Scholar]
- Charbonneau H, Walsh KA, McCann RO, Prendergast FG, Cormier MJ, Vanaman TC. Amino acid sequence of the calcium-dependent photoprotein aequorin. Biochemistry. 1985 Nov 19;24(24):6762–6771. [PubMed] [Google Scholar]
- Inglis AS. Cleavage at aspartic acid. Methods Enzymol. 1983;91:324–332. [PubMed] [Google Scholar]
- Bidlingmeyer BA, Cohen SA, Tarvin TL. Rapid analysis of amino acids using pre-column derivatization. J Chromatogr. 1984 Dec 7;336(1):93–104. [PubMed] [Google Scholar]
- Dayhoff MO, Barker WC, Hunt LT. Establishing homologies in protein sequences. Methods Enzymol. 1983;91:524–545. [PubMed] [Google Scholar]
- Ralph SJ, Thomas ML, Morton CC, Trowbridge IS. Structural variants of human T200 glycoprotein (leukocyte-common antigen). EMBO J. 1987 May;6(5):1251–1257. [PMC free article] [PubMed] [Google Scholar]
- Thomas ML, Barclay AN, Gagnon J, Williams AF. Evidence from cDNA clones that the rat leukocyte-common antigen (T200) spans the lipid bilayer and contains a cytoplasmic domain of 80,000 Mr. Cell. 1985 May;41(1):83–93. [PubMed] [Google Scholar]
- Thomas ML, Reynolds PJ, Chain A, Ben-Neriah Y, Trowbridge IS. B-cell variant of mouse T200 (Ly-5): evidence for alternative mRNA splicing. Proc Natl Acad Sci U S A. 1987 Aug;84(15):5360–5363. [PMC free article] [PubMed] [Google Scholar]
- Berndt N, Campbell DG, Caudwell FB, Cohen P, da Cruz e Silva EF, da Cruz e Silva OB, Cohen PT. Isolation and sequence analysis of a cDNA clone encoding a type-1 protein phosphatase catalytic subunit: homology with protein phosphatase 2A. FEBS Lett. 1987 Nov 2;223(2):340–346. [PubMed] [Google Scholar]
- Green DD, Yang SI, Mumby MC. Molecular cloning and sequence analysis of the catalytic subunit of bovine type 2A protein phosphatase. Proc Natl Acad Sci U S A. 1987 Jul;84(14):4880–4884. [PMC free article] [PubMed] [Google Scholar]
- Stone SR, Hofsteenge J, Hemmings BA. Molecular cloning of cDNAs encoding two isoforms of the catalytic subunit of protein phosphatase 2A. Biochemistry. 1987 Nov 17;26(23):7215–7220. [PubMed] [Google Scholar]
- Saga Y, Tung JS, Shen FW, Boyse EA. Sequences of Ly-5 cDNA: isoform-related diversity of Ly-5 mRNA. Proc Natl Acad Sci U S A. 1986 Sep;83(18):6940–6944. [PMC free article] [PubMed] [Google Scholar]
- Barclay AN, Jackson DI, Willis AC, Williams AF. Lymphocyte specific heterogeneity in the rat leucocyte common antigen (T200) is due to differences in polypeptide sequences near the NH2-terminus. EMBO J. 1987 May;6(5):1259–1264. [PMC free article] [PubMed] [Google Scholar]
- Streuli M, Hall LR, Saga Y, Schlossman SF, Saito H. Differential usage of three exons generates at least five different mRNAs encoding human leukocyte common antigens. J Exp Med. 1987 Nov 1;166(5):1548–1566. [PMC free article] [PubMed] [Google Scholar]
- Hunter T. A thousand and one protein kinases. Cell. 1987 Sep 11;50(6):823–829. [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. 1984 Aug 28;23(18):4207–4218. [PubMed] [Google Scholar]
- Charbonneau H, Beier N, Walsh KA, Beavo JA. Identification of a conserved domain among cyclic nucleotide phosphodiesterases from diverse species. Proc Natl Acad Sci U S A. 1986 Dec;83(24):9308–9312. [PMC free article] [PubMed] [Google Scholar]
- Shackelford DA, Trowbridge IS. Identification of lymphocyte integral membrane proteins as substrates for protein kinase C. Phosphorylation of the interleukin-2 receptor, class I HLA antigens, and T200 glycoprotein. J Biol Chem. 1986 Jun 25;261(18):8334–8341. [PubMed] [Google Scholar]
- Autero M, Gahmberg CG. Phorbol diesters increase the phosphorylation of the leukocyte common antigen CD45 in human T cells. Eur J Immunol. 1987 Oct;17(10):1503–1506. [PubMed] [Google Scholar]
- Jones SW, Erikson E, Blenis J, Maller JL, Erikson RL. A Xenopus ribosomal protein S6 kinase has two apparent kinase domains that are each similar to distinct protein kinases. Proc Natl Acad Sci U S A. 1988 May;85(10):3377–3381. [PMC free article] [PubMed] [Google Scholar]
- Klausner RD, O'Shea JJ, Luong H, Ross P, Bluestone JA, Samelson LE. T cell receptor tyrosine phosphorylation. Variable coupling for different activating ligands. J Biol Chem. 1987 Sep 15;262(26):12654–12659. [PubMed] [Google Scholar]
Articles from Proceedings of the National Academy of Sciences of the United States of America are provided here courtesy of National Academy of Sciences