Abstract
Subcellular distribution of heterotrimeric GTP-binding proteins during thrombin receptor-mediated platelet activation was examined, revealing two phases of translocation to the cytoskeleton. A part of Gi2α and Gsα shows first phase translocation to the low-speed pellet (15000 × g pellet) within 1 min after activation, suggesting involvement in platelet shape change or granule secretion. In the second phase, Gi2α, Gsα, Gqα, and Gβ translocate to the low-speed pellet, depending on platelet aggregation. These translocation correlated with the reorganization of the actin-cytoskeleton and were inhibited by cytochalasin D. Reconstitution experiments also revealed that G proteins are associated with the actin-cytoskeleton during platelet activation.
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