一种新型的SH3结构域配体。Nck衔接蛋白通过一个SH3结构域与一种丝氨酸/苏氨酸激酶结合。
A novel ligand for SH3 domains. The Nck adaptor protein binds to a serine/threonine kinase via an SH3 domain.
作者信息
Chou M M, Hanafusa H
机构信息
Laboratory of Molecular Oncology, Rockefeller University, New York, New York 10021, USA.
出版信息
J Biol Chem. 1995 Mar 31;270(13):7359-64. doi: 10.1074/jbc.270.13.7359.
We have previously shown that overexpression of the SH2- and SH3-containing Nck adaptor protein causes transformation of mammalian fibroblast. To elucidate the mechanism by which it deregulates growth, we have sought to identify potential effectors 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.
我们之前已经表明，含SH2和SH3结构域的Nck衔接蛋白的过表达会导致哺乳动物成纤维细胞发生转化。为了阐明其失调生长的机制，我们试图鉴定Nck的潜在效应分子。我们报告称，一种丝氨酸/苏氨酸激酶，我们将其命名为NAK（Nck相关激酶），在体内和体外均与Nck相关联。利用用Nck的分离结构域产生的谷胱甘肽S-转移酶融合蛋白，我们证明NAK特异性结合到Nck三个SH3结构域中的第二个。NAK在多种细胞类型中与Nck形成复合物，包括NIH3T3、A431、PC12和Hela细胞。
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