SHIP1 Controls Internal Platelet Contraction and α_IIbβ₃ Integrin Dynamics in Early Platelet Activation.

ABSTRACT: The Src homology 2 domain-containing inositol 5-phosphatase 1 (SHIP1) is known to dephosphorylate PtdIns(3,4,5)P₃ into PtdIns(3,4)P₂ and to interact with several signaling proteins though its docking functions. It has been shown to negatively regulate platelet adhesion and spreading on a fibrinogen surface and to positively regulate thrombus growth. In the present study, we have investigated its role during the early phase of platelet activation. Using confocal-based morphometric analysis, we found that SHIP1 is involved in the regulation of cytoskeletal organization and internal contractile activity in thrombin-activated platelets. The absence of SHIP1 has no significant impact on thrombin-induced Akt or Erk1/2 activation, but it selectively affects the RhoA/Rho-kina

SUBMITTER: Severin S 

PROVIDER: S-EPMC9860818 | biostudies-literature | 2023 Jan

REPOSITORIES: biostudies-literature