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Quantitative proteomics of the integrin adhesome show a myosin II‐dependent recruitment of LIM domain proteins
Author(s) -
Schiller Herbert B,
Friedel Caroline C,
Boulegue Cyril,
Fässler Reinhard
Publication year - 2011
Publication title -
embo reports
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 4.584
H-Index - 184
eISSN - 1469-3178
pISSN - 1469-221X
DOI - 10.1038/embor.2011.5
Subject(s) - focal adhesion , integrin , myosin , lim domain , adhesion , microbiology and biotechnology , chemistry , cell adhesion , proteomics , biology , zinc finger , biochemistry , signal transduction , receptor , organic chemistry , gene , transcription factor
A characteristic of integrins is their ability to transfer chemical and mechanical signals across the plasma membrane. Force generated by myosin II makes cells able to sense substrate stiffness and induce maturation of nascent adhesions into focal adhesions. In this paper, we present a comprehensive proteomic analysis of nascent and mature adhesions. The purification of integrin adhesion complexes combined with quantitative mass spectrometry enabled the identification and quantification of known and new adhesion‐associated proteins. Furthermore, blocking adhesion maturation with the myosin II inhibitor blebbistatin markedly impaired the recruitment of LIM domain proteins to integrin adhesion sites. This suggests a common recruitment mechanism for a whole class of adhesion‐associated proteins, involving myosin II and the zinc‐finger‐type LIM domain.