Journal
NATURE CELL BIOLOGY
Volume 17, Issue 12, Pages 1577-1587Publisher
NATURE PUBLISHING GROUP
DOI: 10.1038/ncb3257
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Funding
- Wellcome Trust [092015]
- Wellcome Trust Institutional Strategic Support Fund [097820]
- Biotechnology and Biological Sciences Research Council studentship from the Systems Biology Doctoral Training Centre
- Biotechnology and Biological Sciences Research Council
- University of Manchester Strategic Fund
- Biotechnology and Biological Sciences Research Council [1087621] Funding Source: researchfish
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Integrin receptor activation initiates the formation of integrin adhesion complexes (IACs) at the cell membrane that transduce adhesion-dependent signals to control a multitude of cellular functions. Proteomic analyses of isolated IACs have revealed an unanticipated molecular complexity; however, a global view of the consensus composition and dynamics of IACs is lacking. Here, we have integrated several IAC proteomes and generated a 2,412-protein integrin adhesome. Analysis of this data set reveals the functional diversity of proteins in IACs and establishes a consensus adhesome of 60 proteins. The consensus adhesome is likely to represent a core cell adhesion machinery, centred around four axes comprising ILK PINCH kindlin, FAK paxillin, talin vinculin and alpha-actinin zyxin VASP, and includes underappreciated IAC components such as Rsu-1 and caldesmon. Proteomic quantification of IAC assembly and disassembly detailed the compositional dynamics of the core cell adhesion machinery. The definition of this consensus view of integrin adhesome components provides a resource for the research community.
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