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Updated: Aug 15, 2026

Static Adhesion Assay for the Study of Integrin Activation in T Lymphocytes
Published on: June 13, 2014
An unraveling tale of how integrins are activated from within
Mark A Travis1, Jonathan D Humphries, Martin J Humphries
1Wellcome Trust Centre for Cell-Matrix Research, School of Biological Sciences, University of Manchester, 2.205 Stopford Building, Oxford Road, Manchester M13 9PT, UK.
Abstract:
Integrin cytoplasmic tail domains are short, but are essential for normal receptor function because of their key role in relaying bidirectional signals across the plasma membrane. Although it is well established that the cytoplasmic tails both initiate signalling pathways inside the cell and control the transition of integrins from a resting to a ligand-binding competent state, until recently the structural basis of these changes has been unclear. In the past year, however, a series of structural studies has revealed certain features of cytoplasmic domain function, and in this review we focus on how these advances have enlightened our understanding of integrin tail structure and function.
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