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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) 9:607-616.
Abstract
Tyrosine 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.
Note
Publication Date: 1998-11-01.
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