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EMBO Rep. 2011 Mar;12(3):259-66. doi: 10.1038/embor.2011.5. Epub 2011 Feb 11.

Quantitative proteomics of the integrin adhesome show a myosin II-dependent recruitment of LIM domain proteins.

Author information

1
Department of Molecular Medicine, Max-Planck Institute of Biochemistry, Am Klopferspitz 18, Martinsried 82152, Germany.

Abstract

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.

PMID:
21311561
PMCID:
PMC3059911
DOI:
10.1038/embor.2011.5
[Indexed for MEDLINE]
Free PMC Article

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