Journal
EMBO REPORTS
Volume 12, Issue 3, Pages 259-266Publisher
WILEY
DOI: 10.1038/embor.2011.5
Keywords
integrin adhesome; quantitative proteomics; focal adhesion; myosin-II; LIM domain
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Funding
- European Molecular Biology Organisation (EMBO)
- Max Planck Society
- German Funding Agency [SFB 863]
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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.
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