The WASH-complex subunit Strumpellin regulates integrin αIIbβ3 trafficking in murine platelets.

ABSTRACT: The platelet specific integrin αIIbβ3 mediates platelet adhesion, aggregation and plays a central role in thrombosis and hemostasis. In resting platelets, αIIbβ3 is expressed on the membrane surface and in intracellular compartments. Upon activation, the number of surface-expressed αIIbβ3 is increased by the translocation of internal granule pools to the plasma membrane. The WASH complex is the major endosomal actin polymerization-promoting complex and has been implicated in the generation of actin networks involved in endocytic trafficking of integrins in other cell types. The role of the WASH complex and its subunit Strumpellin in platelet function is still unknown. Here, we report that Strumpellin-deficient murine platelets display an approximately 20% reduction in integrin αIIbβ3 surfa

SUBMITTER: Schurr Y 

PROVIDER: S-EPMC10260982 | biostudies-literature | 2023 Jun

REPOSITORIES: biostudies-literature