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J Cell Sci. 2014 Sep 1;127(Pt 17):3768-81. doi: 10.1242/jcs.149518. Epub 2014 Jul 2.

An EMMPRIN-γ-catenin-Nm23 complex drives ATP production and actomyosin contractility at endothelial junctions.

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Centro Nacional de Investigaciones Cardiovasculares (CNIC), 28029 Madrid, Spain.
University of Pennsylvania, Philadelphia, PA 19104, USA.
Instituto de Investigación Sanitaria Princesa. Universidad Autónoma de Madrid, 28006 Madrid, Spain.
FIRC Institute of Molecular Oncology, University of Milan, 20139 Milan, Italy.
Nagoya University, Nagoya, 464-8601, Japan.
Centro Nacional de Investigaciones Cardiovasculares (CNIC), 28029 Madrid, Spain


Cell-cell adhesions are important sites through which cells experience and resist forces. In endothelial cells, these forces regulate junction dynamics and determine endothelial barrier strength. We identify the Ig superfamily member EMMPRIN (also known as basigin) as a coordinator of forces at endothelial junctions. EMMPRIN localization at junctions correlates with endothelial junction strength in different mouse vascular beds. Accordingly, EMMPRIN-deficient mice show altered junctions and increased junction permeability. Lack of EMMPRIN alters the localization and function of VE-cadherin (also known as cadherin-5) by decreasing both actomyosin contractility and tugging forces at endothelial cell junctions. EMMPRIN ensures proper actomyosin-driven maturation of competent endothelial junctions by forming a molecular complex with γ-catenin (also known as junction plakoglobin) and Nm23 (also known as NME1), a nucleoside diphosphate kinase, thereby locally providing ATP to fuel the actomyosin machinery. These results provide a novel mechanism for the regulation of actomyosin contractility at endothelial junctions and might have broader implications in biological contexts such as angiogenesis, collective migration and tissue morphogenesis by coupling compartmentalized energy production to junction assembly.


ATP; Actomyosin contractility; EMMPRIN; Endothelial junctions; NDPK; Nm23; Nucleoside diphosphate kinase; Vascular integrity; γ-catenin

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