A single autophosphorylation site confers oncogenicity to the Neu/ErbB-2 receptor and enables coupling to the MAP kinase pathway.
作者： R. Ben-Levy , H.F. Paterson , C.J. Marshall , Y. Yarden
DOI: 10.1002/J.1460-2075.1994.TB06632.X
关键词:
摘要: The transforming potential of the Neu/ErbB-2 receptor tyrosine kinase undergoes inactivation by deletion non-catalytic C-terminal tail, which contains five autophosphorylation sites. To determine site is essential for oncogenicity, we tailed C-terminally-deleted mutant with individual Complete restoration action in vitro and vivo was conferred a stretch 12 amino acids that contained most (Y1253). Reconstitution transformation specific to this acid sequence because none other sites, when grafted individually, caused transformation, replacement phenylalanine residue significantly reduced oncogenic both full-length proteins. When present alone enabled coupling biochemical pathway includes Ras, MAP transactivation Jun. These results indicate multiplicity sites on not transformability, implicate transduction signal Neu/ErbB-2.
sci-hub.se 参考文章(40)
M Liyanage, D Frith, S Stabel, K Vollmer, G Kour, O Sözeri, G E Mark rd, Activation of the c-Raf protein kinase by protein kinase C phosphorylation. Oncogene. ,vol. 7, pp. 2259- 2262 ,(1992)
E. Peles, R.B. Levy, E. Or, A. Ullrich, Y. Yarden, Oncogenic forms of the neu/HER2 tyrosine kinase are permanently coupled to phospholipase C gamma. The EMBO Journal. ,vol. 10, pp. 2077- 2086 ,(1991) , 10.1002/J.1460-2075.1991.TB07739.X
A. Honegger, T. J. Dull, F. Bellot, E. Van Obberghen, D. Szapary, A. Schmidt, A. Ullrich, J. Schlessinger, Biological activities of EGF-receptor mutants with individually altered autophosphorylation sites. The EMBO Journal. ,vol. 7, pp. 3045- 3052 ,(1988) , 10.1002/J.1460-2075.1988.TB03169.X
G M Walton, W S Chen, M G Rosenfeld, G N Gill, 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. Journal of Biological Chemistry. ,vol. 265, pp. 1750- 1754 ,(1990) , 10.1016/S0021-9258(19)40080-X
A. Ullrich, A. Zilberstein, M. Dombalagian, B. Margolis, J. Schlessinger, R. Hazan, Identification of autophosphorylation sites of HER2/neu. Cell Growth & Differentiation. ,vol. 1, pp. 3- 7 ,(1990)
A Sorkin, K Helin, C.M. Waters, G Carpenter, L Beguinot, 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. Journal of Biological Chemistry. ,vol. 267, pp. 8672- 8678 ,(1992) , 10.1016/S0021-9258(18)42495-7
E Peles, R Lamprecht, R Ben-Levy, E Tzahar, Y Yarden, Regulated coupling of the Neu receptor to phosphatidylinositol 3'-kinase and its release by oncogenic activation. Journal of Biological Chemistry. ,vol. 267, pp. 12266- 12274 ,(1992) , 10.1016/S0021-9258(19)49834-7
R Ben-Levy, E Peles, R Goldman-Michael, Y Yarden, An oncogenic point mutation confers high affinity ligand binding to the neu receptor. Implications for the generation of site heterogeneity. Journal of Biological Chemistry. ,vol. 267, pp. 17304- 17313 ,(1992) , 10.1016/S0021-9258(18)41926-6
D. Rotin, B. Margolis, M. Mohammadi, R.J. Daly, G. Daum, N. Li, E.H. Fischer, W.H. Burgess, A. Ullrich, J. Schlessinger, SH2 domains prevent tyrosine dephosphorylation of the EGF receptor: identification of Tyr992 as the high-affinity binding site for SH2 domains of phospholipase C gamma. The EMBO Journal. ,vol. 11, pp. 559- 567 ,(1992) , 10.1002/J.1460-2075.1992.TB05087.X
T Smeal, B Binetruy, D Mercola, A Grover-Bardwick, G Heidecker, U R Rapp, M Karin, Oncoprotein-mediated signalling cascade stimulates c-Jun activity by phosphorylation of serines 63 and 73. Molecular and Cellular Biology. ,vol. 12, pp. 3507- 3513 ,(1992) , 10.1128/MCB.12.8.3507