Platelet protein interactions: map, signaling components, and phosphorylation groundstate. Arterioscler. Thromb. Vasc. Biol 2008;28:1326–1331. [PubMed: 18451328] 5 ••. Woulfe D, Jiang H, Morgans A, et al. Defects in secretion, aggregation, and thrombus fo

Objectives—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. (Arterioscler Thromb Vasc Biol. 2008;28:1326-1331) Key Words: platelet interactome network signaling pathway phosphoproteome The small anuclear platelets are central for hemostasis andinvolved in the pathophysiology of several cardiovascular diseases as well as inflammatory processes and metastasis. Data on the platelet and its proteome are accumulating at an unprec