Protein interactions with the platelet integrin alpha(IIb) regulatory motif

Raab, Markus, Daxecker, Heide, Edwards, Richard J., Treumann, Achim, Murphy, Derek and Moran, Niamh (2010) Protein interactions with the platelet integrin alpha(IIb) regulatory motif. Proteomics, 9999 (999A). (doi:10.1002/pmic.200900621).

Abstract

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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