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First published online October 11, 2005


Journal of Cell Science 118, 2002e (2005)
© The Company of Biologists Limited
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In this issue

Semaphorin' messages across the GAP


Semaphorins are conserved signalling molecules that control a wide range of biological activities, including axonal guidance and cell migration. Activation of plexins, high-affinity receptors for semaphorins, inhibits integrin-mediated adhesion and cytoskeletal remodelling. Luca Tamagnone and colleagues now report that p190 Rho-GTPase activating protein (p190-RhoGAP) associates with plexins and is required for semaphorin signalling (see p. 4689). The authors show first that RhoA-GTP levels transiently decrease upon plexin activation in adherent cells. Given that p190-RhoGAP is a major downregulator of RhoA, the authors next investigated semaphorin signalling in p190-RhoGAP-deficient fibroblasts. They found that the functional activities mediated by plexins, such as cell collapse and inhibition of integrin function, were blocked or impaired in these cells but could be rescued by expression of exogenous p190-RhoGAP. Knocking down p190-RhoGAP by RNAi also blocked semaphorin signalling in epithelial cells, primary endothelial cells and neuroblasts. The authors therefore conclude that p190RhoGAP mediates semaphorin signalling to the actin cytoskeleton and to integrin-mediated adhesions through its interaction with plexins.


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Related articles in JCS:

p190 Rho-GTPase activating protein associates with plexins and it is required for semaphorin signalling
Davide Barberis, Andrea Casazza, Raffaella Sordella, Simona Corso, Stefania Artigiani, Jeff Settleman, Paolo M. Comoglio, and Luca Tamagnone
JCS 2005 118: 4689-4700. [Abstract] [Full Text]  




This Article
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