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First published online 28 March 2006
doi: 10.1242/jcs.02859

Journal of Cell Science 119, 1632-1644 (2006)
Published by The Company of Biologists 2006
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Research Article

Multiple factors contribute to integrin-talin interactions in vivo

Guy Tanentzapf, Maria D. Martin-Bermudo*, Marcus S. Hicks and Nicholas H. Brown{ddagger}

The Wellcome Trust/Cancer Research UK Gurdon Institute and Department of Anatomy, University of Cambridge, Tennis Court Road, Cambridge, CB2 1QN, UK

{ddagger} Author for correspondence (e-mail: nb117{at}cam.ac.uk)

Accepted 28 December 2005

The cytoplasmic protein talin is an essential part of the integrin-cytoskeleton link. We characterized the interaction between integrin and two conserved regions of talin, the N-terminal `head' domain and the C-terminus, which includes the I/LWEQ domain, within the living organism. Green-fluorescent-protein-tagged head and C-terminal domains were recruited to integrin adhesion sites. Both required integrins for recruitment, but the C-terminal domain also required endogenous talin, showing it was not recruited directly by integrins. We used chimeric transmembrane proteins containing the cytoplasmic domain of the integrin ß subunit to examine the integrin-talin head interaction. Monomeric chimeric proteins did not recruit talin head, whereas dimeric chimeras efficiently recruited it and caused a strong inhibition of integrin-mediated adhesion. These chimeras recruited surprisingly few integrin-associated proteins, indicating that recruitment of talin did not initiate a cascade of recruitment. Mutagenesis of the integrin cytoplasmic domain, within the chimera, showed the dominant-negative inhibition was not due to talin sequestration alone and that additional interactions are required.

Key words: Integrin, Cell adhesion, Cytoskeleton, Drosophila


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