A NOVEL LIGAND FOR SH3 DOMAINS

被引：46

作者：

CHOU, MM ^{[1
]}

HANAFUSA, H ^{[1
]}

机构：

[1] ROCKEFELLER UNIV,MOLEC ONCOL LAB,NEW YORK,NY 10021

来源：

JOURNAL OF BIOLOGICAL CHEMISTRY | 1995年 / 270卷 / 13期

关键词：

D O I：

10.1074/jbc.270.13.7359

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

We have previously shown that overexpression of the SH2- and SH3-containing Nck adaptor protein causes transformation of mammalian fibroblasts. To elucidate the mechanism by which it deregulates growth, we have sought to identify potential effecters for Nck. We report that a serine/threonine kinase, which we term NAK (for Nck-associated kinase), associates with Nck in vivo and in vitro. Using glutathione S-transferase fusion proteins generated with isolated domains of Nck, we demonstrate that NAK binds specifically to the second of Nck's three SH3 domains. NAK is complexed with Nck in a wide variety of cell types, including NIH3T3, A431, PC12, and HeLa cells.

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页码：7359 / 7364

页数：6

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