QUICK SEARCH:   [advanced] Author: Keyword(s):
Home     Help     Feedback     Subscriptions     Archive     Search     Table of Contents

First published online June 4, 2008

This Article Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Services Email this article to a friend Related articles in JCS Similar articles in this journal Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via Google Scholar Google Scholar Search for Related Content Social Bookmarking                         What's this?

p190A and p190B: not created equal

Members of the Rho family of small GTPases, which facilitate cell migration, are negatively regulated by RhoGAP proteins, which include the closely related proteins p190A and p190B. These two proteins are ubiquitously expressed, share several binding partners and, in neurons, have partially overlapping functions – but do they have distinct roles in endothelial-cell migration? To address this question, Violaine Moreau and colleagues (p. 2054) use RNAi to knock down p190A and p190B individually in human umbilical vein endothelial cells (HUVECs). The authors show that, when p190B is absent, the total expression and cell-surface localisation of the matrix metalloproteinase MT1-MMP is decreased (although it is increased when p190A is knocked down), and that MMP2 – which is usually activated by MT1-MMP – is less active. Because both MMP proteins are associated with podosome-mediated degradation of the extracellular matrix, the authors induce the formation of podosomes and show that the number of podosomes per cell, as well as the amount of matrix degradation, increases in the absence of p190A. By contrast, knocking down p190B decreases podosome function. Thus, p190A and p190B have distinct, and possibly antagonistic, functions in endothelial-cell biology.

CiteULike    Complore    Connotea    Del.icio.us    Digg    Reddit    Technorati    Twitter    What's this?

Related articles in JCS:

p190B RhoGAP regulates endothelial-cell-associated proteolysis through MT1-MMP and MMP2

Fabien Guegan, Florence Tatin, Thierry Leste-Lasserre, Guillaume Drutel, Elisabeth Genot, and Violaine Moreau
JCS 2008 121: 2054-2061. [Abstract] [Full Text]  

This Article Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Services Email this article to a friend Related articles in JCS Similar articles in this journal Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via Google Scholar Google Scholar Search for Related Content Social Bookmarking                         What's this?