Cellubrevin/vesicle-associated membrane protein-3-mediated endocytosis and trafficking regulate platelet functions.

ABSTRACT: Endocytosis is key to fibrinogen (Fg) uptake, trafficking of integrins (αIIbβ₃, α_vβ₃), and purinergic receptors (P2Y₁, P2Y₁₂), and thus normal platelet function. However, the molecular machinery required and possible trafficking routes are still ill-defined. To further identify elements of the platelet endocytic machinery, we examined the role of a vesicle-residing, soluble N-ethylmaleimide factor attachment protein receptor (v-SNARE) called cellubrevin/vesicle-associated membrane protein-3 (VAMP-3) in platelet function. Although not required for normal platelet exocytosis or hemostasis, VAMP-3^-/- mice had less platelet-associated Fg, indicating a defect in Fg uptake/storage. Other granule markers were unaffected. Dir

SUBMITTER: Banerjee M 

PROVIDER: S-EPMC5746669 | biostudies-literature | 2017 Dec

REPOSITORIES: biostudies-literature