Title : Selective interaction of LAT (linker of activated T cells) with the open-active form of Lck in lipid rafts reveals a new mechanism for the regulation of Lck in T cells.

Pub. Date : 2003 May 1

PMID : 12570875






5 Functional Relationships(s)
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1 In T cells, the lipid raft-associated Lck is strongly tyrosine phosphorylated and has reduced enzymic activity in contrast with the detergent-soluble pool, which has substantial activity. Tyrosine LCK proto-oncogene, Src family tyrosine kinase Homo sapiens
2 In the LAT(linker of activated T cells)-deficient J.CaM2 cells, Tyr(505) phosphorylation of raft-associated Lck was reduced whereas its enzymic activity was elevated. Tyrosine LCK proto-oncogene, Src family tyrosine kinase Homo sapiens
3 Increased tyrosine phosphorylation of Lck was restored in LAT-reconstituted J.CaM2 cells suggesting that LAT negatively regulates Lck activity in lipid rafts. Tyrosine LCK proto-oncogene, Src family tyrosine kinase Homo sapiens
4 Increased tyrosine phosphorylation of Lck was restored in LAT-reconstituted J.CaM2 cells suggesting that LAT negatively regulates Lck activity in lipid rafts. Tyrosine LCK proto-oncogene, Src family tyrosine kinase Homo sapiens
5 Co-immunoprecipitation experiments from Tyr(505) --> Phe/V5-His-expressing cells revealed that LAT preferentially interacts with the "open" form of Lck in T cell raft domains. Tyrosine LCK proto-oncogene, Src family tyrosine kinase Homo sapiens