Vinculin anchors contractile actin to the cardiomyocyte adherens junction.

Autor:	Merkel CD; Department of Cell Biology, School of Medicine, University of Pittsburgh, Pittsburgh, PA 15261., Li Y; Department of Cell Biology, School of Medicine, University of Pittsburgh, Pittsburgh, PA 15261., Raza Q; Department of Cell Biology, School of Medicine, University of Pittsburgh, Pittsburgh, PA 15261., Stolz DB; Department of Cell Biology, School of Medicine, University of Pittsburgh, Pittsburgh, PA 15261., Kwiatkowski AV; Department of Cell Biology, School of Medicine, University of Pittsburgh, Pittsburgh, PA 15261.
Jazyk:	angličtina
Zdroj:	Molecular biology of the cell [Mol Biol Cell] 2019 Oct 01; Vol. 30 (21), pp. 2639-2650. Date of Electronic Publication: 2019 Sep 04.
DOI:	10.1091/mbc.E19-04-0216
Abstrakt:	The adherens junction (AJ) couples the actin cytoskeletons of neighboring cells to allow mechanical integration and tissue organization. The physiological demands of intercellular adhesion require that the AJ be responsive to dynamic changes in force while maintaining mechanical load. These demands are tested in the heart, where cardiomyocyte AJs must withstand repeated cycles of actomyosin-mediated contractile force. Here we show that force-responsive cardiomyocyte AJs recruit actin-binding ligands to selectively couple actin networks. We employed a panel of N-cadherin-αE-catenin fusion proteins to rebuild AJs with specific actin linkages in N-cadherin-null cardiomyocytes. In this system, vinculin recruitment was required to rescue myofibril integration at nascent contacts. In contrast, loss of vinculin from the AJ disrupted junction morphology and blocked myofibril integration at cell-cell contacts. Our results identify vinculin as a critical link to contractile actomyosin and offer insight to how actin integration at the AJ is regulated to provide stability under mechanical load.
Databáze:	MEDLINE
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