Proteomic analysis of integrin adhesion complexes

Adam Byron, Jonathan D Humphries, Mark D Bass, David Knight, Martin J Humphries

Research output: Contribution to journalArticle

Abstract / Description of output

Integrin receptors regulate cell fate by coupling the binding of extracellular adhesion proteins to the assembly of intracellular cytoskeletal and signaling complexes. A detailed, integrative view of adhesion complexes will provide insight into the molecular mechanisms that control cell morphology, survival, movement, and differentiation. To date, membrane receptor-associated signaling complexes have been refractory to proteomic analysis because of their inherent lability and inaccessibility. We developed a methodology to isolate ligand-induced integrin adhesion complexes, and we used this technique to analyze the composition of complexes associated with multiple receptor-ligand pairs and define core and receptor-specific subnetworks. In particular, we identified regulator of chromosome condensation-2 (RCC2) as a component of fibronectin-activated signaling pathways that regulate directional cell movement. The development of this proteomics pipeline provides the means to investigate the molecular composition and function of various adhesion complexes.

Original languageEnglish
Pages (from-to)pt2
JournalScience Signaling
Issue number167
Early online date5 Apr 2011
Publication statusPublished - 2011
Externally publishedYes

Keywords / Materials (for Non-textual outputs)

  • Cell Adhesion
  • Cell Adhesion Molecules
  • Cell Movement
  • Chromosomal Proteins, Non-Histone
  • Cluster Analysis
  • Guanine Nucleotide Exchange Factors
  • Integrins
  • Multiprotein Complexes
  • Proteomics
  • Signal Transduction


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