Analyzing the Anatomy of Integrin Adhesions

Adam Byron^*

The author is a postdoctoral research associate at the Wellcome Trust Centre for Cell-Matrix Research, Faculty of Life Sciences, University of Manchester, Manchester M13 9PT, UK.

Abstract: Cell adhesion to the extracellular matrix (ECM) is necessary for fundamental cellular processes such as survival, migration, and differentiation. Adhesion is mediated by integrin receptors, which recruit multiprotein adhesion complexes to sites of attachment to the ECM. Adhesion complexes provide a structural connection between the ECM and cytoskeleton, transmit mechanical force, and act as signaling hubs to control cell behavior. Recent high-resolution imaging studies of adhesion sites reveal some aspects of their spatial organization and provide insights into their function at the molecular level.

* E-mail, adam.byron{at}manchester.ac.uk

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In Science Signaling

EDITORIAL GUIDES
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Wei Wong (26 April 2011)
Sci. Signal. 4 (170), eg4. [DOI: 10.1126/scisignal.2002100]
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PERSPECTIVES
Cell Biology
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Sci. Signal. 2 (89), pe58. [DOI: 10.1126/scisignal.289pe58]
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RESEARCH ARTICLES
Cell Biology
Proteomic Analysis of Integrin-Associated Complexes Identifies RCC2 as a Dual Regulator of Rac1 and Arf6

Jonathan D. Humphries, Adam Byron, Mark D. Bass, Sue E. Craig, John W. Pinney, David Knight, and Martin J. Humphries (8 September 2009)
Sci. Signal. 2 (87), ra51. [DOI: 10.1126/scisignal.2000396]
 |  Editor's Summary »  |  Abstract »  |  Full Text »  |  PDF »  |  Supplementary Materials »