Redirecting lipoic acid ligase for cell surface protein labeling with small-molecule probes (original) (raw)
References
Debant, A., Ponzio, G., Clauser, E., Contreres, J.O. & Rossi, B. Receptor cross-linking restores an insulin metabolic effect altered by mutation on tyrosine 1162 and tyrosine 1163. Biochemistry28, 14–17 (1989). ArticleCAS Google Scholar
Weiss, A. & Littman, D.R. Signal transduction by lymphocyte antigen receptors. Cell76, 263–274 (1994). ArticleCAS Google Scholar
Anderson, R.G., Brown, M.S., Beisiegel, U. & Goldstein, J.L. Surface distribution and recycling of the low density lipoprotein receptor as visualized with antireceptor antibodies. J. Cell Biol.93, 523–531 (1982). ArticleCAS Google Scholar
Barak, L.S. & Webb, W.W. Fluorescent low density lipoprotein for observation of dynamics of individual receptor complexes on cultured human fibroblasts. J. Cell Biol.90, 595–604 (1981). ArticleCAS Google Scholar
Green, D.E., Morris, T.W., Green, J., Cronan, J.E., Jr. & Guest, J.R. Purification and properties of the lipoate protein ligase of Escherichia coli. Biochem. J.309, 853–862 (1995). ArticleCAS Google Scholar
Agard, N.J., Baskin, J.M., Prescher, J.A., Lo, A. & Bertozzi, C.R. A comparative study of bioorthogonal reactions with azides. ACS Chem. Biol.1, 644–648 (2006). ArticleCAS Google Scholar
Howarth, M., Takao, K., Hayashi, Y. & Ting, A.Y. Targeting quantum dots to surface proteins in living cells with biotin ligase. Proc. Natl. Acad. Sci. USA102, 7583–7588 (2005). ArticleCAS Google Scholar
Howarth, M. et al. A monovalent streptavidin with a single femtomolar biotin binding site. Nat. Methods3, 267–273 (2006). ArticleCAS Google Scholar
Marks, K.M. & Nolan, G.P. Chemical labeling strategies for cell biology. Nat. Methods3, 591–596 (2006). ArticleCAS Google Scholar
Prescher, J.A. & Bertozzi, C.R. Chemistry in living systems. Nat. Chem. Biol.1, 13–21 (2005). ArticleCAS Google Scholar
Ali, S.T. & Guest, J.R. Isolation and characterization of lipoylated and unlipoylated domains of the E2p subunit of the pyruvate dehydrogenase complex of Escherichia coli. Biochem. J.271, 139–145 (1990). ArticleCAS Google Scholar
Fujiwara, K. et al. Crystal structure of lipoate-protein ligase A from Escherichia coli. Determination of the lipoic acid-binding site. J. Biol. Chem.280, 33645–33651 (2005). ArticleCAS Google Scholar
Green, J.D., Laue, E.D., Perham, R.N., Ali, S.T. & Guest, J.R. Three-dimensional structure of a lipoyl domain from the dihydrolipoyl acetyltransferase component of the pyruvate dehydrogenase multienzyme complex of Escherichia coli. J. Mol. Biol.248, 328–343 (1995). CASPubMed Google Scholar
Kiick, K.L., Saxon, E., Tirrell, D.A. & Bertozzi, C.R. Incorporation of azides into recombinant proteins for chemoselective modification by the Staudinger ligation. Proc. Natl. Acad. Sci. USA99, 19–24 (2002). ArticleCAS Google Scholar
Griffin, R.J. The medicinal chemistry of the azido group. Prog. Med. Chem.31, 121–232 (1994). ArticleCAS Google Scholar
Chen, I., Howarth, M., Lin, W. & Ting, A.Y. Site-specific labeling of cell surface proteins with biophysical probes using biotin ligase. Nat. Methods2, 99–104 (2005). ArticleCAS Google Scholar
Lin, C.W. & Ting, A.Y. Transglutaminase-catalyzed site-specific conjugation of small-molecule probes to proteins in vitro and on the surface of living cells. J. Am. Chem. Soc.128, 4542–4543 (2006). ArticleCAS Google Scholar
Adams, S.R. et al. New biarsenical ligands and tetracysteine motifs for protein labeling in vitro and in vivo: synthesis and biological applications. J. Am. Chem. Soc.124, 6063–6076 (2002). ArticleCAS Google Scholar
Willnow, T.E. The low-density lipoprotein receptor gene family: multiple roles in lipid metabolism. J. Mol. Med.77, 306–315 (1999). ArticleCAS Google Scholar
Reche, P. & Perham, R.N. Structure and selectivity in post-translational modification: attaching the biotinyl-lysine and lipoyl-lysine swinging arms in multifunctional enzymes. EMBO J.18, 2673–2682 (1999). ArticleCAS Google Scholar
Pasquale, E.B. Eph receptor signalling casts a wide net on cell behaviour. Nat. Rev. Mol. Cell Biol.6, 462–475 (2005). ArticleCAS Google Scholar
Singh, A.B. & Harris, R.C. Autocrine, paracrine and juxtacrine signaling by EGFR ligands. Cell. Signal.17, 1183–1193 (2005). ArticleCAS Google Scholar
Tuli, S.S. et al. Immunohistochemical localization of EGF, TGF-alpha, TGF-beta, and their receptors in rat corneas during healing of excimer laser ablation. Curr. Eye Res.31, 709–719 (2006). ArticleCAS Google Scholar
Flanagan, J.G. & Vanderhaeghen, P. The ephrins and Eph receptors in neural development. Annu. Rev. Neurosci.21, 309–345 (1998). ArticleCAS Google Scholar
Wimmer-Kleikamp, S.H. & Lackmann, M. Eph-modulated cell morphology, adhesion and motility in carcinogenesis. IUBMB Life57, 421–431 (2005). ArticleCAS Google Scholar
George, N., Pick, H., Vogel, H., Johnsson, N. & Johnsson, K. Specific labeling of cell surface proteins with chemically diverse compounds. J. Am. Chem. Soc.126, 8896–8897 (2004). ArticleCAS Google Scholar
Griffin, B.A., Adams, S.R. & Tsien, R.Y. Specific covalent labeling of recombinant protein molecules inside live cells. Science281, 269–272 (1998). ArticleCAS Google Scholar
Brock, R., Hamelers, I.H. & Jovin, T.M. Comparison of fixation protocols for adherent cultured cells applied to a GFP fusion protein of the epidermal growth factor receptor. Cytometry35, 353–362 (1999). ArticleCAS Google Scholar
McLean, A.J. & Milligan, G. Ligand regulation of green fluorescent protein-tagged forms of the human beta(1)- and beta(2)-adrenoceptors; comparisons with the unmodified receptors. Br. J. Pharmacol.130, 1825–1832 (2000). ArticleCAS Google Scholar
Zhou, Z. et al. Genetically encoded short peptide tags for orthogonal protein labeling by Sfp and AcpS phosphopantetheinyl transferases. ACS Chem. Biol.2, 337–346 (2007). ArticleCAS Google Scholar