Proteomics

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Proteomic analysis of integrin-associated adhesion complexes isolated from cells treated with DMSO or FAK inhibitor

ABSTRACT: Human foreskin fibroblast cells were spread on fibronectin (FN) for 1 h and treated with DMSO or FAK inhibitor (3 uM, AZ13256675 (termed AZ675 for short)) for 1 h. Integrin-associated adhesion complexes isolated from these cells were analysed by mass spectrometry to determine changes in adhesion complex composition upon FAK inhibition. As a negative control, complexes were also isolated from cells attached to transferrin (Tf), which allows integrin-independent adhesion via the transferrin receptor.

INSTRUMENT(S): LTQ Orbitrap Elite

ORGANISM(S): Homo Sapiens (ncbitaxon:9606)

SUBMITTER: Dr Martin J. Humphries 

PROVIDER: MSV000080089 | MassIVE | Tue Aug 23 00:31:00 BST 2016

SECONDARY ACCESSION(S): PXD002720

REPOSITORIES: MassIVE

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Publications

Modulation of FAK and Src adhesion signaling occurs independently of adhesion complex composition.

Horton Edward R ER   Humphries Jonathan D JD   Stutchbury Ben B   Jacquemet Guillaume G   Ballestrem Christoph C   Barry Simon T ST   Humphries Martin J MJ  

The Journal of cell biology 20160201 3

Integrin adhesion complexes (IACs) form mechanochemical connections between the extracellular matrix and actin cytoskeleton and mediate phenotypic responses via posttranslational modifications. Here, we investigate the modularity and robustness of the IAC network to pharmacological perturbation of the key IAC signaling components focal adhesion kinase (FAK) and Src. FAK inhibition using AZ13256675 blocked FAK(Y397) phosphorylation but did not alter IAC composition, as reported by mass spectromet  ...[more]