Proteomics

Dataset Information

0

Proteomic analysis of integrin activation-state-dependent adhesion complexes


ABSTRACT: Proteomic analysis of integrin activation-state-dependent adhesion complexes. Adhesion complexes were isolated from K562 cells using activation-state-specific monoclonal antibodies coupled to magnetic beads.Tandem mass spectra were extracted using extract_msn (Thermo Fisher Scientific) executed in Mascot Daemon (version 2.2.2; Matrix Science). Peak list files were searched against the IPI Human database (version 3.70) modified to contain ten additional contaminants and reagent sequences of non-human origin. Searches were submitted to an in-house Mascot server (version 2.2.03; Matrix Science). Carbamidomethylation of cysteine was set as a fixed modification, and oxidation of methionine was allowed as a variable modification. Only tryptic peptides were considered, with up to one missed cleavage permitted. Monoisotopic precursor mass values were used, and only doubly and triply charged precursor ions were considered. Mass tolerances for precursor and fragment ions were 0.4 Da and 0.5 Da, respectively.

INSTRUMENT(S): LTQ Velos

ORGANISM(S): Homo Sapiens (human)

SUBMITTER: Adam Byron  

LAB HEAD: Adam Byron

PROVIDER: PXD000155 | Pride | 2015-01-26

REPOSITORIES: Pride

Dataset's files

Source:
Action DRS
20100604_mAbBBA1_JAA_1.raw Raw
20100604_mAbBBA1_JAA_10.raw Raw
20100604_mAbBBA1_JAA_11.raw Raw
20100604_mAbBBA1_JAA_12.raw Raw
20100604_mAbBBA1_JAA_13.raw Raw
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Publications

A proteomic approach reveals integrin activation state-dependent control of microtubule cortical targeting.

Byron Adam A   Askari Janet A JA   Humphries Jonathan D JD   Jacquemet Guillaume G   Koper Ewa J EJ   Warwood Stacey S   Choi Colin K CK   Stroud Matthew J MJ   Chen Christopher S CS   Knight David D   Humphries Martin J MJ  

Nature communications 20150122


Integrin activation, which is regulated by allosteric changes in receptor conformation, enables cellular responses to the chemical, mechanical and topological features of the extracellular microenvironment. A global view of how activation state converts the molecular composition of the region proximal to integrins into functional readouts is, however, lacking. Here, using conformation-specific monoclonal antibodies, we report the isolation of integrin activation state-dependent complexes and the  ...[more]

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