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Different integrin, different signal

The binding of ligands such as fibronectin to cell surface integrins produces a variety of intracellular signals. An attractive idea is that different integrin subtypes generate different signals, but strong evidence for this has been lacking. Shu Chien and co-workers now demonstrate that two integrin subtypes can indeed activate distinct signalling pathways (see p. 2199). They show that, when CHO cells are plated on fibronectin, integrin-ß1-expressing cells produce lamellipodia and activate Rac — a Rho-family GTPase implicated in induction of lamellipodia. By contrast, integrin-ß3-expressing cells generate actin stress fibres and activate Rho, which is thought to control stress fibre formation. Intriguingly, the authors found that expression of a chimeric construct in which one of the extracellular domains of integrin ß1 was replaced by the corresponding domain from integrin ß3 produced stress fibres and an increase in Rho activity. Their findings thus indicate not only that the two integrins signal differently in response to fibronectin but that differences in the extracellular region rather than the intracellular region are responsible.

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Differential regulation of Rho GTPases by ß1 and ß3 integrins: the role of an extracellular domain of integrin in intracellular signaling

Hui Miao, Song Li, Ying-Li Hu, Suli Yuan, Yihua Zhao, Benjamin P. C. Chen, Wilma Puzon-McLaughlin, Takehiko Tarui, John Y.-J. Shyy, Yoshikazu Takada, Shunichi Usami, and Shu Chien
JCS 2002 115: 2199-2206. [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?