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(Arteriosclerosis, Thrombosis, and Vascular Biology. 2008;28:1326.)
© 2008 American Heart Association, Inc.

Cell Biology and Signaling

Platelet Protein Interactions

Map, Signaling Components, and Phosphorylation Groundstate

Marcus Dittrich; Ingvild Birschmann; Silke Mietner; Albert Sickmann; Ulrich Walter; Thomas Dandekar

From the Department of Bioinformatics (M.D., T.D.), Biocenter, University of Würzburg; the Institut fuer Klinische Biochemie & Pathobiochemie (M.D., I.B., S.M., U.W.), Würzburg; Rudolf Virchow Center (A.S.), Würzburg; and EMBL (T.D.), Heidelberg, Germany.

Correspondence to Thomas Dandekar, Department of Bioinformatics, Biocenter, University of Würzburg, Am Hubland, Würzburg, D-97074 Germany. E-mail dandekar{at}biozentrum.uni-wuerzburg.de

Abstract

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.

Key Words: platelet • interactome • network • signaling pathway • phosphoproteome

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Arterioscler. Thromb. Vasc. Biol. 2008 28: 1214-1215. [Full Text] [PDF]