Characterization of structural domains of the human epidermal growth factor receptor obtained by partial proteolysis.
作者： M Chinkers , J S Brugge
DOI: 10.1016/S0021-9258(18)90895-1
关键词:
摘要: Partial cleavage with trypsin has been used to study the structure of epidermal growth factor (EGF) receptor purified from human carcinoma cells. Following affinity labeling 125I-EGF or ATP analogue 5'-p-fluorosulfonyl benzoyl[14C]adenosine, metabolic [35S]methionine, [3H]glucosamine, [32P]orthophosphate, in vitro autophosphorylation [gamma-32P]ATP, tryptic defines following three regions 180-kDa protein: 1) a 125-kDa trypsin-resistant domain which contains sites glycosylation, EGF binding, and an EGF-specific threonine phosphorylation site; 2) adjacent 40-kDa fragment serine is further cleaved 30-kDa domain; 3) terminal 15-kDa portion that tyrosine degraded small fragments presence trypsin. Both 125- appear be required for receptor-associated protein kinase activity since separation these by abolishes this activity, both are specifically labeled analogue, suggesting involved binding. Additional 63- 48-kDa phosphorylated generated upon treatment EGF-treated The potential usefulness partial studying possible biological function discussed.
sci-hub.st 参考文章(34)
G Carpenter, KJ Lembach, MM Morrison, S Cohen, Characterization of the binding of 125-I-labeled epidermal growth factor to human fibroblasts. Journal of Biological Chemistry. ,vol. 250, pp. 4297- 4304 ,(1975) , 10.1016/S0021-9258(19)41417-8
S A Buhrow, S Cohen, J V Staros, Affinity labeling of the protein kinase associated with the epidermal growth factor receptor in membrane vesicles from A431 cells. Journal of Biological Chemistry. ,vol. 257, pp. 4019- 4022 ,(1982) , 10.1016/S0021-9258(18)34676-3
L King, S Cohen, G Carpenter, Rapid enhancement of protein phosphorylation in A-431 cell membrane preparations by epidermal growth factor. Journal of Biological Chemistry. ,vol. 254, pp. 4884- 4891 ,(1979) , 10.1016/S0021-9258(17)30094-7
H. Ushiro, S. Cohen, Identification of phosphotyrosine as a product of epidermal growth factor-activated protein kinase in A-431 cell membranes. Journal of Biological Chemistry. ,vol. 255, pp. 8363- 8365 ,(1980) , 10.1016/S0021-9258(18)43497-7
S A Buhrow, S Cohen, D L Garbers, J V Staros, Characterization of the interaction of 5'-p-fluorosulfonylbenzoyl adenosine with the epidermal growth factor receptor/protein kinase in A431 cell membranes. Journal of Biological Chemistry. ,vol. 258, pp. 7824- 7827 ,(1983) , 10.1016/S0021-9258(18)32253-1
J S Brugge, D Darrow, Analysis of the catalytic domain of phosphotransferase activity of two avian sarcoma virus-transforming proteins. Journal of Biological Chemistry. ,vol. 259, pp. 4550- 4557 ,(1984) , 10.1016/S0021-9258(17)43081-X
S. Cohen, G. Carpenter, L. King, Epidermal growth factor-receptor-protein kinase interactions. Co-purification of receptor and epidermal growth factor-enhanced phosphorylation activity. Journal of Biological Chemistry. ,vol. 255, pp. 4834- 4842 ,(1980) , 10.1016/S0021-9258(19)85573-4
S. Cohen, H. Ushiro, C. Stoscheck, M. Chinkers, A native 170,000 epidermal growth factor receptor-kinase complex from shed plasma membrane vesicles. Journal of Biological Chemistry. ,vol. 257, pp. 1523- 1531 ,(1982) , 10.1016/S0021-9258(19)68224-4
Steven W. Kessler, Rapid isolation of antigens from cells with a staphylococcal protein A-antibody adsorbent: parameters of the interaction of antibody-antigen complexes with protein A. Journal of Immunology. ,vol. 115, pp. 1617- 1624 ,(1975)
P.G. Comens, R.L. Simmer, J.B. Baker, Direct linkage of 125I-EGF to cell surface receptors: a useful artifact of chloramine-T treatment Journal of Biological Chemistry. ,vol. 257, pp. 42- 45 ,(1982) , 10.1016/S0021-9258(19)68322-5