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The Structure of the talin head reveals a novel extended conformation of the FERM domain

Elliott, Paul R, Goult, Benjamin T, Kopp, Petra M, Bate, Neil, Grossmann, J Günter, Roberts, Gordon C K, Critchley, David R, Barsukov, Igor L (2010) The Structure of the talin head reveals a novel extended conformation of the FERM domain. Structure, 18 (10). pp. 1289-1299. ISSN 1878-4186. (doi:10.1016/j.str.2010.07.011) (KAR id:42120)

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FERM domains are found in a diverse superfamily of signaling and adaptor proteins at membrane interfaces. They typically consist of three separately folded domains (F1, F2, F3) in a compact cloverleaf structure. The crystal structure of the N-terminal head of the integrin-associated cytoskeletal protein talin reported here reveals a novel FERM domain with a linear domain arrangement, plus an additional domain F0 packed against F1. While F3 binds beta-integrin tails, basic residues in F1 and F2 are required for membrane association and for integrin activation. We show that these same residues are also required for cell spreading and focal adhesion assembly in cells. We suggest that the extended conformation of the talin head allows simultaneous binding to integrins via F3 and to PtdIns(4,5)P2-enriched microdomains via basic residues distributed along one surface of the talin head, and that these multiple interactions are required to stabilize integrins in the activated state.

Item Type: Article
DOI/Identification number: 10.1016/j.str.2010.07.011
Subjects: Q Science > QH Natural history > QH301 Biology
Divisions: Divisions > Division of Natural Sciences > Biosciences
Depositing User: Ben Goult
Date Deposited: 07 Aug 2014 20:15 UTC
Last Modified: 16 Nov 2021 10:16 UTC
Resource URI: (The current URI for this page, for reference purposes)
Goult, Benjamin T:
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