Key result
In silico assembly of a comprehensive proteome and transcriptome database provided a first view of the human platelet interactome, phosphorylation, and kinome.
May inform platelet signaling research; leaves open experimental validation before any clinical translation.
OBJECTIVE: Assembly of a comprehensive proteome and transcriptome database of human platelets, derivation of a model of the platelet-specific interactome, and generation of a functional interaction map of platelet phosphorylations and kinases. METHODS AND RESULTS: Interactions are derived from literature-curated data from HPRD and yeast two hybrid (Y2H) and mapped to platelet-specific expression data (SAGE or proteome). From this a cell-type specific model of platelet proteins and protein-protein interactions is derived. The obtained inventory of platelet-specific proteins includes key domains, protein GO annotations, and receptors. Collected interactions point to new platelet signaling components, actin remodeling processes, and pharmacological targets and offer incentives for further studies (eg, on the IPP complex). Integration of platelet-specific phosphoproteins and the characterization of the platelet kinase repertoire sketch a first outline of kinase signaling in human platelets. CONCLUSIONS: A first view of the platelet interactome, platelet phosphorylation, and platelet kinome is available from the in silico data.
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Dittrich et al. (2008) studied Human platelets. In silico database assembly and interaction mapping was evaluated on Derivation of a model of the platelet-specific interactome and functional interaction map. In silico assembly of a comprehensive proteome and transcriptome database provided a first view of the human platelet interactome, phosphorylation, and kinome.
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