Please use this identifier to cite or link to this item: https://doi.org/10.1016/j.semcdb.2019.11.016
Title: Mechanical regulation of formin-dependent actin polymerization
Authors: LE SHIMIN 
YU MIAO 
YAN JIE 
BERSHADSKY,ALEXANDER 
Keywords: Formins, Actin, E-Cadherin, Adherens Junctions, Collective migration
Actin polymerization
Force
Torque
Single-molecule technologies
Issue Date: 5-Dec-2019
Publisher: London : Academic Press
Citation: LE SHIMIN, YU MIAO, YAN JIE, BERSHADSKY,ALEXANDER (2019-12-05). Mechanical regulation of formin-dependent actin polymerization. Seminars in Cell & Developmental Biology 102 : 73-80. ScholarBank@NUS Repository. https://doi.org/10.1016/j.semcdb.2019.11.016
Abstract: The actomyosin cytoskeleton network plays a key role in a variety of fundamental cellular processes such as cell division, migration, and cell adhesion. The functions of cytoskeleton rely on its capability to receive, generate, respond to and transmit mechanical signals throughout the cytoskeleton network within the cells and throughout the tissue via cell-extracellular matrix and cell-cell adhesions. Crucial to the cytoskeleton’s functions is actin polymerization that is regulated by many cellular factors. Among these factors, the formin family proteins, which bind the barbed end of an actin filament (F-actin), are known to be a major actin polymerization promoting factor. Mounting evidence from single-molecule mechanical manipulation experiments have suggested that formin-dependent actin polymerization is sensitively regulated by the force and torque applied to the F-actin, making the formin family an emerging mechanosensing factor that selectively promotes elongation of the F-actin under tensile forces. In this review, we will focus on the current understanding of the mechanical regulation of formin-mediated actin polymerization, the key technologies that have enabled quantification of formin-mediated actin polymerization under mechanical constraints, and future perspectives and studies on molecular mechanisms involved in the mechanosensing of actin dynamics.
Source Title: Seminars in Cell & Developmental Biology
URI: https://scholarbank.nus.edu.sg/handle/10635/170840
ISSN: 1084-9521
DOI: 10.1016/j.semcdb.2019.11.016
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