Structure of a double ubiquitin-like domain in the talin head: a role in integrin activation.

Goult, Benjamin T and Bouaouina, Mohamed and Elliott, Paul R and Bate, Neil and Patel, Bipin and Gingras, Alexandre R and Grossmann, J Günter and Roberts, Gordon C K and Calderwood, David A and Critchley, David R and Barsukov, Igor L (2010) Structure of a double ubiquitin-like domain in the talin head: a role in integrin activation. The EMBO journal, 29 (6). pp. 1069-1080. ISSN 1460-2075. (doi:https://doi.org/10.1038/emboj.2010.4) (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.2010.4

Abstract

Talin is a 270-kDa protein that activates integrins and couples them to cytoskeletal actin. Talin contains an N-terminal FERM domain comprised of F1, F2 and F3 domains, but it is atypical in that F1 contains a large insert and is preceded by an extra domain F0. Although F3 contains the binding site for beta-integrin tails, F0 and F1 are also required for activation of beta1-integrins. Here, we report the solution structures of F0, F1 and of the F0F1 double domain. Both F0 and F1 have ubiquitin-like folds joined in a novel fixed orientation by an extensive charged interface. The F1 insert forms a loop with helical propensity, and basic residues predicted to reside on one surface of the helix are required for binding to acidic phospholipids and for talin-mediated activation of beta1-integrins. This and the fact that basic residues on F2 and F3 are also essential for integrin activation suggest that extensive interactions between the talin FERM domain and acidic membrane phospholipids are required to orientate the FERM domain such that it can activate integrins.

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 15:54 UTC
Last Modified: 07 May 2015 08:56 UTC
Resource URI: https://kar.kent.ac.uk/id/eprint/42126 (The current URI for this page, for reference purposes)
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