作者: C Cenciarelli , R.J. Hohman , T.P. Atkinson , F Gusovsky , A.M. Weissman
DOI: 10.1016/S0021-9258(18)42068-6
关键词: Cell surface receptor 、 Biochemistry 、 Protein tyrosine phosphatase 、 Guanosine 、 Phosphorylation 、 GTP' 、 Biology 、 Tyrosine phosphorylation 、 Molecular biology 、 Receptor tyrosine kinase 、 Tyrosine kinase
摘要: The zeta subunit of the T cell receptor (TCR) is a prominent substrate for TCR-activated tyrosine kinase. Tyrosine phosphorylation in response to antibody-mediated cross-linking was synergized permeabilized cells by either two non-hydrolyzable GTP analogues, guanosine 5'-[gamma-thio]triphosphate (GTP gamma S) or 5'-[beta, gamma-imido]triphosphate Gpp(NH)p. ATP analogues did not significantly affect antibody-induced phosphorylation. Unlike GDP analogue 5'-[beta-thio]diphosphate (GDP beta enhance zeta. effect induced required TCR occupancy and independent protein kinase C. Taken together these observations implicate GTP-binding modulation TCR-induced