CHARACTERIZATION AND ANALYSIS OF PLATELET SETPINS

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This subproject is one of many research subprojects utilizing the resources provided by a Center grant funded by NIH/NCRR. The subproject and investigator (PI) may have received primary funding from another NIH source, and thus could be represented in other CRISP entries. The institution listed is for the Center, which is not necessarily the institution for the investigator. Septins are a family of proteins orginially identified in yeast as essential for budding. For years, the presence of septins in higher eukaryotic cells was dismissed since budding, asymmetric cell division, is a process unique to yeast. However, recent studies have demonstrated that septins do exist in higher eukaryotes and, in those cases examined, as associated with dynamic events involving membranes. Recent work form neurobiology laboratories has associated the septin SEPT5, with exocytic complex of neurons with implications that SEPT5 regulates transmitter release. In our Preliminary Studies, we demonstrate SEPT5 is part of a macromolecular complex containing a protein linked to platelet secretion, syntaxin 4. Defining the mechanisms that control platelet secretion is key to preventing the uncontrolled release of thrombogenic factors.