TY - JOUR TI - Myosin II isoforms play distinct roles in adherens junction biogenesis AU - Heuzé, Mélina L AU - Sankara Narayana, Gautham Hari Narayana AU - D'Alessandro, Joseph AU - Cellerin, Victor AU - Dang, Tien AU - Williams, David S AU - Van Hest, Jan CM AU - Marcq, Philippe AU - Mège, René-Marc AU - Ladoux, Benoit A2 - Akhmanova, Anna A2 - Weis, William I A2 - Discher, Dennis VL - 8 PY - 2019 DA - 2019/09/05 SP - e46599 C1 - eLife 2019;8:e46599 DO - 10.7554/eLife.46599 UR - https://doi.org/10.7554/eLife.46599 AB - Adherens junction (AJ) assembly under force is essential for many biological processes like epithelial monolayer bending, collective cell migration, cell extrusion and wound healing. The acto-myosin cytoskeleton acts as a major force-generator during the de novo formation and remodeling of AJ. Here, we investigated the role of non-muscle myosin II isoforms (NMIIA and NMIIB) in epithelial junction assembly. NMIIA and NMIIB differentially regulate biogenesis of AJ through association with distinct actin networks. Analysis of junction dynamics, actin organization, and mechanical forces of control and knockdown cells for myosins revealed that NMIIA provides the mechanical tugging force necessary for cell-cell junction reinforcement and maintenance. NMIIB is involved in E-cadherin clustering, maintenance of a branched actin layer connecting E-cadherin complexes and perijunctional actin fibres leading to the building-up of anisotropic stress. These data reveal unanticipated complementary functions of NMIIA and NMIIB in the biogenesis and integrity of AJ. KW - mechanobiology KW - epithelial cells KW - cytoskeleton KW - adherens junctions KW - myosin JF - eLife SN - 2050-084X PB - eLife Sciences Publications, Ltd ER -