Title : The amino-terminal Src homology 2 domain of phospholipase C gamma 1 is essential for TCR-induced tyrosine phosphorylation of phospholipase C gamma 1.

Pub. Date : 1998 Feb 1

PMID : 9570517






7 Functional Relationships(s)
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Compound Name
Protein Name
Organism
1 The amino-terminal Src homology 2 domain of phospholipase C gamma 1 is essential for TCR-induced tyrosine phosphorylation of phospholipase C gamma 1. Tyrosine phospholipase C gamma 1 Homo sapiens
2 The amino-terminal Src homology 2 domain of phospholipase C gamma 1 is essential for TCR-induced tyrosine phosphorylation of phospholipase C gamma 1. Tyrosine phospholipase C gamma 1 Homo sapiens
3 TCR engagement activates phospholipase C gamma 1 (PLC gamma 1) via a tyrosine phosphorylation-dependent mechanism. Tyrosine phospholipase C gamma 1 Homo sapiens
4 TCR engagement activates phospholipase C gamma 1 (PLC gamma 1) via a tyrosine phosphorylation-dependent mechanism. Tyrosine phospholipase C gamma 1 Homo sapiens
5 PLC gamma 1 contains a pair of Src homology 2 (SH2) domains whose function is that of promoting protein interactions by binding phosphorylated tyrosine and adjacent amino acids. Tyrosine phospholipase C gamma 1 Homo sapiens
6 Mutation of the amino-terminal SH2 domain (SH2(N) domain) resulted in defective tyrosine phosphorylation of PLC gamma 1 in response to TCR/CD3 perturbation. Tyrosine phospholipase C gamma 1 Homo sapiens
7 In contrast to TCR/CD3 ligation, treatment of cells with pervanadate induced tyrosine phosphorylation of either PLC gamma 1 SH2(N) or SH2(C) domain mutants to a level comparable with that of the wild-type protein, indicating that pervanadate treatment induces an alternate mechanism of PLC gamma 1 phosphorylation. Tyrosine phospholipase C gamma 1 Homo sapiens