Organization of functional domains in the docking protein p130Cas

被引：12

作者：

Nasertorabi, F ^{[1
]}

Garcia-Guzman, M ^{[1
]}

Briknarová, K ^{[1
]}

Larsen, E ^{[1
]}

Havert, ML ^{[1
]}

Vuori, K ^{[1
]}

Ely, KR ^{[1
]}

机构：

[1] Burnham Inst, Ctr Canc, La Jolla, CA 92037 USA

来源：

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 2004年 / 324卷 / 03期

关键词：

Cas family proteins; protein phosphorylation; protein design; integrin signaling; Src family kinases; 14-3-3; protein;

D O I：

10.1016/j.bbrc.2004.09.148

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：

The docking protein p 1 30Cas becomes phosphorylated upon cell adhesion to extracellular matrix proteins, and is thought to play an essential role in cell transformation. Cas transmits signals through interactions with the Src-hornology 3 (SH3) and Src-homology 2 domains of FAK or v-Crk signaling molecules, or with 14-3-3 protein, as well as phosphatases PTP1B and PTP-PEST. The large (130 kDa), multi-domain Cas molecule contains an SH3 domain, a Src-binding domain, a serine-rich protein interaction region, and a C-terminal region that participates in protein interactions implicated in antiestrogen resistance in breast cancer. In this study, as part of a long-term goal to examine the protein interactions of Cas by X-ray crystallography and nuclear magnetic resonance spectroscopy, molecular constructs were designed to express two adjacent domains, the serine-rich domain and the Src-binding domain, that each participate in intermolecular contacts dependent on protein phosphorylation. The protein products are soluble, homogeneous, monodisperse, and highly suitable for structural studies to define the role of Cas in integrin-mediated cell signaling. (C) 2004 Elsevier Inc. All rights reserved.

引用

页码：993 / 998

页数：6

共 21 条

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