Subcellular localization of talin is regulated by inter-domain interactions

Banno, Asoka and Goult, Benjamin T and Lee, HoSup and Bate, Neil and Critchley, David R and Ginsberg, Mark H (2012) Subcellular localization of talin is regulated by inter-domain interactions. The Journal of biological chemistry, 287 (17). pp. 13799-13812. ISSN 1083-351X. (doi:https://doi.org/10.1074/jbc.M112.341214) (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/10.1074/jbc.M112.341214

Abstract

Talin, which is composed of head (THD) and rod domains, plays an important role in cell adhesion events in diverse species including most metazoans and Dictyostelium discoideum. Talin is abundant in the cytosol; however, it mediates adhesion by associating with integrins in the plasma membrane where it forms a primary link between integrins and the actin cytoskeleton. Cells modulate the partitioning of talin between the plasma membrane and the cytosol to control cell adhesion. Here, we combine nuclear magnetic resonance spectroscopy (NMR) with subcellular fractionation to characterize two distinct THD-rod domain interactions that control the interaction of talin with the actin cytoskeleton or its localization to the plasma membrane. An interaction between a discrete vinculin-binding region of the rod (VBS1/2a; Tln1(482-787)), and the THD restrains talin from interacting with the plasma membrane. Furthermore, we show that vinculin binding to VBS1/2a results in talin recruitment to the plasma membrane. Thus, we have structurally defined specific inter-domain interactions between THD and the talin rod domain that regulate the subcellular localization of talin.

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 20:31 UTC
Last Modified: 30 Mar 2015 10:53 UTC
Resource URI: https://kar.kent.ac.uk/id/eprint/42114 (The current URI for this page, for reference purposes)
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