The inner life of integrin adhesion sites: From single molecules to functional macromolecular complexes.

Thomas Orré, Olivier Rossier, Grégory Giannone
Experimental Cell Research. 2019-06-01; 379(2): 235-244
DOI: 10.1016/j.yexcr.2019.03.036

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Cells are mechanical living machines that remodel their microenvironment by
adhering and generating forces on the extracellular matrix (ECM) using
integrin-dependent adhesion sites (IAS). In return, the biochemical and physical
nature of the ECM determines cellular behavior and morphology during
proliferation, differentiation and migration. IAS come in different shapes and
forms. They have specific compositions, morphologies, mechanical and biochemical
signaling activities, which serve different cellular functions. Proteomic studies
showed that IAS are composed of a large repertoire of proteins that could be
linked to different functional activities, including signaling,
force-transmission and force-sensing. Thanks to recent technological advances in
microscopy and protein engineering, it is now possible to localize single
proteins in three dimensions inside IAS, determine their diffusive behaviors,
orientations, and how much mechanical force is transmitted across individual
components. Here, we review how researchers have used those tools to investigate
how IAS components assemble and dynamically interact to produce diverse functions
of adhesive structures.

Copyright © 2019. Published by Elsevier Inc.

DOI: 10.1016/j.yexcr.2019.03.036
PMID: 30943383

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