Pinpointing phosphotyrosine-dependent interactions downstream of the collagen receptor DDR1

被引：40

作者：

Koo, DHH ^{[1
]}

McFadden, C ^{[1
]}

Huang, Y ^{[1
]}

Abdulhussein, R ^{[1
]}

Friese-Hamim, M ^{[1
]}

Vogel, WF ^{[1
]}

机构：

[1] Univ Toronto, Dept Lab Med & Pathobiol, Toronto, ON M5S 1A8, Canada

来源：

FEBS LETTERS | 2006年 / 580卷 / 01期

关键词：

collagen receptor tyrosine kinase; phosphotyrosine; discoidin domain; SH2-domain ITIM motif;

D O I：

10.1016/j.febslet.2005.11.035

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：

Activation of the receptor tyrosine kinase DDR1 by collagen results in robust and sustained phosphorylation, however little is known about its downstream mediators. Using phosphopeptide mapping and site-directed mutagenesis, we here identified multiple tyrosine phosphorylation sites within DDR1. We found that Nck2 and Shp-2, two SH2 domain-containing proteins, bind to DDR1 in a collagen-dependent manner. The binding site of Shp-2 was mapped to tyrosine-740 of DDR1 within an ITIM-consensus sequence. Lastly, ablation of DDR1 in the mouse mammary gland resulted in delocalized expression of Nck2, suggesting that defects observed during alveologenesis are caused by the lack of the DDR1-Nck2 interaction. (c) 2005 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.

引用

页码：15 / 22

页数：8

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