Defining the phospho-adhesome through the phosphoproteomic analysis of integrin signalling

• DOI: 10.1038/ncomms7265
• Publication Date: 2015-02-13T09:22:55Z
• Authors: Joseph Robertson; Guillaume Jacquemet; Adam Byron; Matthew C. Jones; Stacey Warwood; Julian N. Selley; David Knight; Jonathan D. Humph...; Martin J. Humphries
• Keywords: Signalling

Cell-extracellular matrix (ECM) adhesion is a fundamental requirement for multicellular existence due to roles in positioning, proliferation and differentiation. Phosphorylation plays major role signalling; however, full understanding of the phosphorylation events that occur at sites lacking. Here we report proteomic phosphoproteomic analysis complexes isolated from cells spread on fibronectin. We identify 1,174 proteins, 499 which are phosphorylated (1,109 sites), including both well-characterized novel adhesion-regulated events. Immunoblotting suggests two classes residues found sites-those induced by those constitutively but recruited response adhesion. Kinase prediction identifies kinases with putative signalling CDK1, inhibition reduces complex formation. This phospho-adhesome data set constitutes valuable resource improve our mechanisms through cell-ECM interactions control cell behaviour.