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Wardenburg JB , Pappu R , Bu JY , Mayer B , Chernoff J , Straus D , Chan AC
Regulation of PAK activation and the T cell cytoskeleton by the linker protein SLP-76
Immunity. 1998 Nov;9(5) :607-616
AbstractTyrosine phosphorylation of linker proteins enables the T cell antigen receptor (TCR)-associated protein tyrosine kinases to phosphorylate and regulate effector molecules that generate second messengers. We demonstrate here that the SLP-76 linker protein interacts with both nck, an adaptor protein, and Vav, a guanine nucleotide exchange factor for Rho-family GTPases. The assembly of this tri-molecular complex permits the activated Rho-family GTPases to regulate target effecters that interact through nck. In turn, assembly of this complex mediates the enzymatic activation of the p21-activated protein kinase 1 and facilitates actin polymerization. Hence, phosphorylation of linker proteins not only bridges the TCR-associated PTK, ZAP- 70, with downstream effector proteins, but also provides a scaffold to integrate distinct signaling complexes to regulate T cell function.
NotesTimes Cited: 66 English Article 144DK IMMUNITY