Crk interacts with tyrosine-phosphorylated p116 upon T cell activation

S. Sawasdikosol, K. S. Ravichandran, Kay Lee Kyungah Kay Lee, J. H. Chang, S. J. Burakoff

Research output: Contribution to journalArticlepeer-review

74 Scopus citations

Abstract

Products of the crk oncogene are expressed in all tissues. Crk proteins are composed exclusively of Src homology 2 (SH2) and Src homology 3 (SH3) domains, and they have been implicated in intracellular signaling. For example, they participate as mediators of Ras activation during nerve growth factor stimulation of PC12 pheochromocytoma cells. We examined the role of Crk proteins during T cell receptor-mediated signaling and observed that Crk proteins specifically interact, via their SH2 domains, with a tyrosine- phosphorylated 116-kDa protein upon T cell activation. p116 may be related to the recently cloned fibroblast p130(cas) and/or p120-Cb1. In addition, we observed that GST-Crk fusion proteins and Crk-L bind, most likely via their SH3 domain, to C3G, a Ras guanine nucleotide exchange factor. Thus, the interaction of Crk with p116 and C3G strongly implicates Crk as a mediator of T cell receptor signaling, possibly involved in Ras activation.

Original languageEnglish
Pages (from-to)2893-2896
Number of pages4
JournalJournal of Biological Chemistry
Volume270
Issue number7
DOIs
StatePublished - 1995

Fingerprint

Dive into the research topics of 'Crk interacts with tyrosine-phosphorylated p116 upon T cell activation'. Together they form a unique fingerprint.

Cite this