4.8 Article

Definition of a consensus integrin adhesome and its dynamics during adhesion complex assembly and disassembly

Journal

NATURE CELL BIOLOGY
Volume 17, Issue 12, Pages 1577-1587

Publisher

NATURE PUBLISHING GROUP
DOI: 10.1038/ncb3257

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Funding

  1. Wellcome Trust [092015]
  2. Wellcome Trust Institutional Strategic Support Fund [097820]
  3. Biotechnology and Biological Sciences Research Council studentship from the Systems Biology Doctoral Training Centre
  4. Biotechnology and Biological Sciences Research Council
  5. University of Manchester Strategic Fund
  6. 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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