Conformational changes accompany phosphorylation of the epidermal growth factor receptor C-terminal domain

Protein Science

Volumn 14, Issue 11, 2005, Pages 2793-2803

  Lee, Nam Y ^a   Koland, John G ^a  

^a UNIVERSITY OF IOWA   (United States)

Author keywords

ErbB; FRET; HER; Protein tyrosine kinase

Indexed keywords

EPIDERMAL GROWTH FACTOR RECEPTOR;

ARTICLE; BINDING AFFINITY; BINDING SITE; CARBOXY TERMINAL SEQUENCE; CHEMICAL INTERACTION; ENERGY TRANSFER; ENERGY YIELD; ENZYME ACTIVITY; FLUORESCENCE RESONANCE ENERGY TRANSFER; GEOMETRY; NONHUMAN; PHOSPHORYLATION; PRIORITY JOURNAL; PROTEIN FOLDING;

ADENOSINE TRIPHOSPHATE; CATALYTIC DOMAIN; FLUORESCENCE RESONANCE ENERGY TRANSFER; FLUORESCENT DYES; LIGHT; LUMINESCENT PROTEINS; PHOSPHORYLATION; PROTEIN STRUCTURE, TERTIARY; RECEPTOR, EPIDERMAL GROWTH FACTOR; SCATTERING, RADIATION;

EID: 27644550586     PISSN: 09618368     EISSN: 1469896X     Source Type: Journal    
DOI: 10.1110/ps.051630305     Document Type: Article

References (21)

1. Bertics, P.J. and Gill, G.N. 1985. Self-phosphorylation enhances the protein-tyrosine kinase activity of the epidermal growth factor receptor. J. Biol. Chem. 260: 14642-14647.
2. Bertics, P.J., Chen, W.S., Hubler, L., Lazar, C.S., Rosenfeld, M.G., and Gill, G.N. 1988. Alteration of epidermal growth factor receptor activity by mutation of its primary carboxyl-terminal site of tyrosine self-phosphorylation. J. Biol. Chem. 263: 3610-3617.
3. Burgess, A.W., Cho, H.S., Eigenbrot, C., Ferguson, K.M., Garrett, T.P., Leahy, D.J., Lemmon, M.A., Sliwkowski, M.X., Ward, C.W., and Yokoyama, S. 2003. An open-and-shut case? Recent insights into the activation of EGF/ErbB receptors. Mol. Cell 12: 541-552.
4. Cadena, D.L., Chan, C.L., and Gill, G.N. 1994. The intracellular tyrosine kinase domain of the epidermal growth factor receptor undergoes a conformational change upon autophosphorylation. J. Biol. Chem. 269: 260-265.
5. Cheng, K. and Koland, J.G. 1996. Nucleotide binding by the epidermal growth factor receptor protein-tyrosine kinase: Trinitrophenyl-ATP as a spectroscopic probe. J. Biol. Chem. 271: 311-318.
6. Dancey, J.E. 2004. Predictive factors for epidermal growth factor receptor inhibitors: The bull's-eye hits the arrow. Cancer Cell 5: 411-415.
7. Honegger, A., Dull, T.J., Szapary, D., Komoriya, A., Kris, R., Ullrich, A., and Schlessinger, J. 1988. Kinetic parameters of the protein tyrosine kinase activity of EGF-receptor mutants with individually altered autophosphorylation sites. EMBO J. 7: 3053-3060.
8. Landau, M., Fleishman, S.J., and Ben-Tal, N. 2004. A putative mechanism for downregulation of the catalytic activity of the EGF receptor via direct contact between its kinase and C-terminal domains. Structure (Camb.) 12: 2265-2275.
9. Margolis, B.L., Lax, I., Kris, R., Dombalagian, M., Honegger, A.M., Howk, R., Givol, D., Ullrich, A., and Schlessinger, J. 1989. All autophosphorylation sites of epidermal growth factor receptor and HER2/neu are located in their carboxyl-terminal tails: Identification of a novel site in EGF receptor. J. Biol. Chem. 264: 10667-10671.
10. Patterson, G., Day, R.N., and Piston, D. 2001. Fluorescent protein spectra. J. Cell Sci. 114: 837-838.
11. Pawson, T. 1994. Signal transduction: Look at a tyrosine kinase. Nature 372: 726-727.
12. _. 1995. Protein-tyrosine kinases: Getting down to specifics. Nature 373: 477-478.
13. Posner, I., Engel, M., and Levitzki, A. 1992. Kinetic model of the epidermal growth factor (EGF) receptor tyrosine kinase and a possible mechanism of its activation by EGF. J. Biol. Chem. 267: 20638-20647.
14. Posner, I., Engel, M., Gazit, A., and Levitzki, A. 1994. Kinetics of inhibition by tyrphostins of the tyrosine kinase activity of the epidermal growth factor receptor and analysis by a new computer program. Mol. Pharmacol. 45: 673-683.
15. Schlessinger, J. 2000. Cell signaling by receptor tyrosine kinases. Cell 103: 211-225.
16. _. 2002. Ligand-induced, receptor-mediated dimerization and activation of EGF receptor. Cell 110: 669-672.
17. Stamos, J., Sliwkowski, M.X., and Eigenbrot, C. 2002. Structure of the epidermal growth factor receptor kinase domain alone and in complex with a 4-anilinoquinazoline inhibitor. J. Biol. Chem. 277: 46265-46272.
18. Walton, G.M., Chen, W.S., Rosenfeld, M.G., and Gill, G.N. 1990. Analysis of deletions of the carboxyl terminus of the epidermal growth factor receptor reveals self-phosphorylation at tyrosine 992 and enhanced in vivo tyrosine phosphorylation of cell substrates. J. Biol. Chem. 265: 1750-1754.
19. Wedegaertner, P.B. and Gill, G.N. 1992. Effect of carboxyl terminal truncation on the tyrosine kinase activity of the epidermal growth factor receptor. Arch. Biochem. Biophys. 292: 273-280.
20. Wood, E.R., Truesdale, A.T., McDonald, O.B., Yuan, D., Hassell, A., Dickerson, S.H., Ellis, B., Pennisi, C., Horne, E., Lackey, K., et al. 2004. A unique structure for epidermal growth factor receptor bound to GW572016 (Lapatinib): Relationships among protein conformation, inhibitor off-rate, and receptor activity in tumor cells. Cancer Res. 64: 6652-6659.
21. Yu, X., Sharma, K.D., Takahashi, T., Iwamoto, R., and Mekada, E. 2002. Ligand-independent dimer formation of epidermal growth factor receptor (EGFR) is a step separable from ligand-induced EGFR signaling. Mol. Biol. Cell 13: 2547-2557.