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Molecular Tuning of Filamin A Activities in the Context of Adhesion and Migration

Authors
  • Lamsoul, Isabelle
  • Dupré, Loïc
  • Lutz, Pierre
Publication Date
Nov 20, 2020
Identifiers
DOI: 10.3389/fcell.2020.591323
OAI: oai:HAL:hal-03021277v1
Source
HAL-INRIA
Keywords
Language
English
License
Unknown
External links

Abstract

The dynamic organization of actin cytoskeleton meshworks relies on multiple actinbinding proteins endowed with distinct actin-remodeling activities. Filamin A is a large multi-domain scaffolding protein that cross-links actin filaments with orthogonal orientation in response to various stimuli. As such it plays key roles in the modulation of cell shape, cell motility, and differentiation throughout development and adult life. The essentiality and complexity of Filamin A is highlighted by mutations that lead to a variety of severe human disorders affecting multiple organs. One of the most conserved activity of Filamin A is to bridge the actin cytoskeleton to integrins, thereby maintaining the later in an inactive state. We here review the numerous mechanisms cells have developed to adjust Filamin A content and activity and focus on the function of Filamin A as a gatekeeper to integrin activation and associated adhesion and motility.

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