Raab, Markus, Daxecker, Heide, Edwards, Richard J., Treumann, Achim, Murphy, Derek and Moran, Niamh
Protein interactions with the platelet integrin alpha(IIb) regulatory motif
Proteomics, 9999, (999A) (doi:10.1002/pmic.200900621).
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Integrins are transmembrane proteins regulating cellular shape, mobility and the cell cycle. A highly-conserved signature motif in the cytoplasmic tail of the integrin -subunit, KXGFFKR, plays a critical role in regulating integrin function. To date, six proteins have been identified that target this motif of the platelet-specific integrin IIb3.
We employ peptide-affinity chromatography followed-up with LC-MS/MS analysis as well as protein chips to identify new potential regulators of integrin function in platelets and put them into their biological context using information from protein:protein interaction (PPI) databases. 44 platelet proteins bind with high affinity to an immobilized LAMWKVGFFKR-peptide. Of these, seven have been reported in the PPI literature as interactors with integrin -subunits. 68 recombinant human proteins expressed on the protein chip specifically bind with high affinity to biotin-tagged -integrin cytoplasmic peptides. Two of these proteins are also identified in the peptide-affinity experiments, one is also found in the PPI databases and a further one is present in the data to all three approaches. Finally, novel short linear interaction motifs are common to a number of proteins identified.
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