Proteomic Analysis of Integrin Adhesion Complexes

Sci. Signal., 5 April 2011
Vol. 4, Issue 167, p. pt2
DOI: 10.1126/scisignal.2001827

Proteomic Analysis of Integrin Adhesion Complexes

  1. Adam Byron1,2,*,
  2. Jonathan D. Humphries1,2,
  3. Mark D. Bass1,2,,
  4. David Knight2, and
  5. Martin J. Humphries1,2,
  1. 1Wellcome Trust Centre for Cell-Matrix Research, University of Manchester, Manchester M13 9PT, UK.
  2. 2Faculty of Life Sciences, University of Manchester, Manchester M13 9PT, UK.
  3. *Presenter.
  4. Current address: Department of Biochemistry, University of Bristol, Bristol BS8 1TD, UK.
  1. Corresponding author. E-mail: martin.humphries{at}
A presentation from the 6th British Society for Proteome Research (BSPR)–European Bioinformatics Institute (EBI) Meeting “Multiscale Proteomics: From Cells to Organisms” at the Wellcome Trust Conference Centre, Cambridge, UK, 14 to 16 July 2009. The Presentation also complements the Science Signaling Research Article by Humphries et al. published 8 September 2009.


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.


A. Byron, J. D. Humphries, M. D. Bass, D. Knight, and M. J. Humphries, Proteomic Analysis of Integrin Adhesion Complexes. Sci. Signal. 4, pt2 (2011).

Symmetric exchange of multi-protein building blocks between stationary focal adhesions and the cytosol
J.-E. Hoffmann, Y. Fermin, R. L. Stricker, K. Ickstadt, and E. Zamir
elife 3, e02257-e02257 (1 January 2014)

The role of integrin-linked kinase in the molecular architecture of focal adhesions
N. Elad, T. Volberg, I. Patla, V. Hirschfeld-Warneken, C. Grashoff, J. P. Spatz, R. Fassler, B. Geiger, and O. Medalia
J. Cell Sci. 126, 4099-4107 (15 September 2013)

Comparative Proteomic Analysis of Supportive and Unsupportive Extracellular Matrix Substrates for Human Embryonic Stem Cell Maintenance
D. Soteriou, B. Iskender, A. Byron, J. D. Humphries, S. Borg-Bartolo, M.-C. Haddock, M. A. Baxter, D. Knight, M. J. Humphries, S. J. Kimber et al.
J Biol Chem 288, 18716-18731 (28 June 2013)

Two modes of integrin activation form a binary molecular switch in adhesion maturation
H.-S. Lee, P. Anekal, C. J. Lim, C.-C. Liu, and M. H. Ginsberg
Mol. Biol. Cell 24, 1354-1362 (1 May 2013)

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