Abstract
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 α-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.
Original language | English |
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Pages (from-to) | 1577–1587 |
Number of pages | 11 |
Journal | Nature Cell Biology |
Volume | 17 |
Issue number | 12 |
DOIs | |
Publication status | Published - 19 Oct 2015 |
Keywords
- Actinin
- Animals
- Cell Adhesion
- Cell Line, Tumor
- Cells, Cultured
- Cluster Analysis
- Focal Adhesions
- Humans
- Immunoblotting
- Integrins
- K562 Cells
- Kinetics
- Mass Spectrometry
- Mice
- Microscopy, Fluorescence
- Nocodazole
- Paxillin
- Protein Interaction Maps
- Proteome
- Proteomics
- Talin
- Tubulin Modulators
- Vinculin
- Zyxin