The structure of an integrin/talin complex reveals the basis of inside-out signal transduction.

Anthis, Nicholas J and Wegener, Kate L and Ye, Feng and Kim, Chungho and Goult, Benjamin T and Lowe, Edward D and Vakonakis, Ioannis and Bate, Neil and Critchley, David R and Ginsberg, Mark H and Campbell, Iain D (2009) The structure of an integrin/talin complex reveals the basis of inside-out signal transduction. The EMBO journal, 28 (22). pp. 3623-3632. ISSN 1460-2075. (doi:https://doi.org/10.1038/emboj.2009.287) (The full text of this publication is not currently available from this repository. You may be able to access a copy if URLs are provided)

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Official URL
http://dx.doi.org/10.1038/emboj.2009.287

Abstract

Fundamental to cell adhesion and migration, integrins are large heterodimeric membrane proteins that uniquely mediate inside-out signal transduction, whereby adhesion to the extracellular matrix is activated from within the cell by direct binding of talin to the cytoplasmic tail of the beta integrin subunit. Here, we report the first structure of talin bound to an authentic full-length beta integrin tail. Using biophysical and whole cell measurements, we show that a specific ionic interaction between the talin F3 domain and the membrane-proximal helix of the beta tail disrupts an integrin alpha/beta salt bridge that helps maintain the integrin inactive state. Second, we identify a positively charged surface on the talin F2 domain that precisely orients talin to disrupt the heterodimeric integrin transmembrane (TM) complex. These results show key structural features that explain the ability of talin to mediate inside-out TM signalling.

Item Type: Article
Subjects: Q Science > QH Natural history > QH301 Biology
Divisions: Faculties > Sciences > School of Biosciences
Depositing User: Ben Goult
Date Deposited: 07 Aug 2014 16:01 UTC
Last Modified: 07 May 2015 09:04 UTC
Resource URI: https://kar.kent.ac.uk/id/eprint/42128 (The current URI for this page, for reference purposes)
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