Inhibition and activation of c-Src: the head and tail of a coin

被引:11
|
作者
Fukami, Y [1 ]
Nagao, T
Iwasaki, T
Sato, K
机构
[1] Kobe Univ, Fac Sci, Dept Biol, Nada Ku, Kobe, Hyogo 6578501, Japan
[2] Kobe Univ, Grad Sch Sci & Technol, Nada Ku, Kobe, Hyogo 6578501, Japan
[3] Kobe Univ, Res Ctr Environm Genom, Nada Ku, Kobe, Hyogo 6578501, Japan
关键词
protein-tyrosine kinase; c-Src; protein-protein interaction; IDA (Inter-DFG-APE) regions; activation segment;
D O I
10.1016/S0163-7258(02)00195-X
中图分类号
R9 [药学];
学科分类号
1007 ;
摘要
Protein-tyro sine kinases (PTKs) play pivotal roles in many cell systems. The Src family kinases (SFKs) are the most characterized PTKs shown to be coupled with various cell surface receptors. However, their mode of activation and regulating partners are largely unknown, Here we describe a novel mechanism of inhibition and activation of c-Src, a representative of the SFKs. Both directions of regulation take place at the same site in the catalytic domain of c-Src via a peptide- or protein-protein interaction. Our results highlight a novel and general mode of kinase regulation that may be applied not only to SFKs, but to other PTKs and Ser/Thr kinases as well. (C) 2002 Elsevier Science Inc. All rights reserved.
引用
收藏
页码:263 / 270
页数:8
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