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Subcellular Localization of Talin Is Regulated by Inter-domain Interactions

Department of Medicine, University of California, San Diego, La Jolla, California 92093-0726, USA.
Journal of Biological Chemistry (Impact Factor: 4.57). 02/2012; 287(17):13799-812. DOI: 10.1074/jbc.M112.341214
Source: PubMed

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.

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Available from: Ben Goult, Nov 11, 2015