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Research Article |
1 Department of Bioengineering and The Whitaker Institute of Biomedical
Engineering, University of California, San Diego, La Jolla CA 92093-0427,
USA
2 Department of Vascular Biology VB-1, The Scripps Research Institute, La Jolla,
CA 92037, USA
* Present address: Department of Bioengineering, University of California,
Berkeley, Berkeley, CA, USA
Present address: Department of Biomedical Sciences, University of California,
Riverside, Riverside, CA, USA
Present address: Lawrence Berkeley National Laboratory, One Cyclotron Road, MS
74-157, Berkeley, CA, USA
¶ Author for correspondence (e-mail: shuchien{at}ucsd.edu )
Accepted 25 February 2002
Integrins mediate cell adhesion and signal transduction at focal adhesions. Here we investigate the roles of integrin ß subunits in the regulation of actin cytoskeletal structure and the activities of Rho and Rac. The overexpression of ß3 integrin in Chinese hamster ovary cells enhances Rho activity and stress fiber formation, whereas the overexpression of ß1 integrin increases Rac activity and lamellipodia formation. The overexpression of a mutant ß1-3-1 integrin, in which the extracellular I-domain-like sequence of ß1 integrin has been replaced with the corresponding sequence of ß3 integrin, also enhances Rho activity and the formation of stress fibers. Our results demonstrate that ß1 and ß3 integrins differentially regulate the activities of Rho family GTPases and that the extracellular domains of integrin ß subunits play a critical role in transducing the extracellular ligand-binding information into specific intracellular signaling events.
Key words: Integrin, Extracellular domain, Small GTPase, Signal transduction
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