Talin-activated vinculin interacts with branched actin networks to initiate bundles.

Autor:	Boujemaa-Paterski R; Department of Biochemistry, University of Zurich, Zurich, Switzerland.; Université Grenoble Alpes, Grenoble, France., Martins B; Department of Biochemistry, University of Zurich, Zurich, Switzerland., Eibauer M; Department of Biochemistry, University of Zurich, Zurich, Switzerland., Beales CT; Department of Biochemistry, University of Zurich, Zurich, Switzerland., Geiger B; Department of Immunology, Weizmann Institute of Science, Rehovot, Israel., Medalia O; Department of Biochemistry, University of Zurich, Zurich, Switzerland.
Jazyk:	angličtina
Zdroj:	ELife [Elife] 2020 Nov 13; Vol. 9. Date of Electronic Publication: 2020 Nov 13.
DOI:	10.7554/eLife.53990
Abstrakt:	Vinculin plays a fundamental role in integrin-mediated cell adhesion. Activated by talin, it interacts with diverse adhesome components, enabling mechanical coupling between the actin cytoskeleton and the extracellular matrix. Here we studied the interactions of activated full-length vinculin with actin and the way it regulates the organization and dynamics of the Arp2/3 complex-mediated branched actin network. Through a combination of surface patterning and light microscopy experiments we show that vinculin can bundle dendritic actin networks through rapid binding and filament crosslinking. We show that vinculin promotes stable but flexible actin bundles having a mixed-polarity organization, as confirmed by cryo-electron tomography. Adhesion-like synthetic design of vinculin activation by surface-bound talin revealed that clustered vinculin can initiate and immobilize bundles from mobile Arp2/3-branched networks. Our results provide a molecular basis for coordinate actin bundle formation at nascent adhesions. Competing Interests: RB, BM, ME, CB, BG, OM No competing interests declared (© 2020, Boujemaa-Paterski et al.)
Databáze:	MEDLINE
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