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Publication Detail
A role for Rab10 in von Willebrand factor release discovered by an AP-1 interactor screen in C. elegans.
  • Publication Type:
    Journal article
  • Publication Sub Type:
    Journal Article
  • Authors:
    Michaux G, Dyer CE, Nightingale TD, Gallaud E, Nurrish S, Cutler DF
  • Publication date:
  • Pagination:
    392, 401
  • Journal:
    J Thromb Haemost
  • Volume:
  • Issue:
  • Country:
  • Language:
  • Keywords:
    Animals, Caenorhabditis elegans, Cell Line, Endothelium, Vascular, Humans, Polymerase Chain Reaction, RNA Interference, Transcription Factor AP-1, rab GTP-Binding Proteins, von Willebrand Factor
Endothelial von Willebrand factor (VWF) mediates platelet adhesion and acts as a protective chaperone to clotting factor VIII. Rapid release of highly multimerized VWF is particularly effective in promoting hemostasis. To produce this protein, an elaborate biogenesis is required, culminating at the trans-Golgi network (TGN) in storage within secretory granules called Weibel-Palade bodies (WPB). Failure to correctly form these organelles can lead to uncontrolled secretion of low-molecular-weight multimers of VWF. The TGN-associated adaptor AP-1 and its interactors clathrin, aftiphilin and γ-synergin are essential to initial WPB formation at the Golgi apparatus, and thus to VWF storage and secretion.
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