p120 catenin and phosphorylation:: Mechanisms and traits of an unresolved issue

被引:69
作者
Alema, Stefano
Salvatore, Anna Maria [1 ]
机构
[1] CNR, Ist Biol Cellulare, I-00016 Monterotondo, Italy
[2] CNR, Ist Neurobiol & Med Mol, I-00143 Rome, Italy
来源
BIOCHIMICA ET BIOPHYSICA ACTA-MOLECULAR CELL RESEARCH | 2007年 / 1773卷 / 01期
关键词
p120ctn; E-cadherin; tyrosine kinase; protein tyrosine phosphatase; PKC; actin cytoskeleton; Rho GTPases;
D O I
10.1016/j.bbamcr.2006.06.001
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
p120 catenin is a scaffold protein that interacts with cadherin cytoplasmic domain and acts as a crucial component of the signalling that regulates the cycle of adherens junction fort-nation and disassembly. Here, we review the nature of stimuli that modulate p120cm function and are translated as serine/threonine and tyrosine phosphorylation events at this multisite substrate for a variety of protein kinases. We also highlight recent findings that tentatively link phosphorylation of p120cm to its role as a signal integrator capable to influence the state of the cadherin adhesive bond, the cytoskeleton and cell motility. (c) 2006 Elsevier B.V. All rights reserved.
引用
收藏
页码:47 / 58
页数:12
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