Structural studies on full-length talin1 reveal a compact auto-inhibited dimer: implications for talin activation

Goult, Benjamin T and Xu, Xiao-Ping and Gingras, Alexandre R and Swift, Mark and Patel, Bipin and Bate, Neil and Kopp, Petra M and Barsukov, Igor L and Critchley, David R and Volkmann, Niels and Hanein, Dorit (2013) Structural studies on full-length talin1 reveal a compact auto-inhibited dimer: implications for talin activation. Journal of structural biology, 184 (1). pp. 21-32. ISSN 1095-8657. (doi:https://doi.org/10.1016/j.jsb.2013.05.014) (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/10.1016/j.jsb.2013.05.014

Abstract

Talin is a large adaptor protein that activates integrins and couples them to cytoskeletal actin. Talin contains an N-terminal FERM (band 4.1, ezrin, radixin, moesin) domain (the head) linked to a flexible rod comprised of 13 amphipathic helical bundles (R1-R13) that terminate in a C-terminal helix (DD) that forms an anti-parallel dimer. We derived a three-dimensional structural model of full-length talin at a resolution of approximately 2.5nm using EM reconstruction of full-length talin and the known shapes of the individual domains and inter-domain angles as derived from small angle X-ray scattering. Talin adopts a compact conformation consistent with a dimer in which the two talin rods form a donut-shaped structure, with the two talin heads packed side by side occupying the hole at the center of this donut. In this configuration, the integrin binding site in the head domain and the actin-binding site at the carboxy-terminus of the rod are masked, implying that talin must unravel before it can support integrin activation and engage the actin cytoskeleton.

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 20:26 UTC
Last Modified: 25 Mar 2015 16:14 UTC
Resource URI: https://kar.kent.ac.uk/id/eprint/42110 (The current URI for this page, for reference purposes)
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