Thromb Haemost 1993; 70(06): 0884-0893
DOI: 10.1055/s-0038-1649694
Review Article
Schattauer GmbH Stuttgart

The Platelet Cytoskeleton

Joan E B Fox
The Children’s Hospital Oakland Research Institute, Oakland, CA, USA
› Author Affiliations
Further Information

Publication History

Received 01 June 1993

Accepted after revision 30 July 1993

Publication Date:
06 July 2018 (online)

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Summary

The platelet cytoskeleton contains two actin filament-based components. One is the cytoplasmic actin filaments which fill the cytoplasm and mediate contractile events. The other is the membrane skeleton, which coats the plasma membrane and regulates properties of the membrane such as its contours and stability. In the unstimulated platelet, only 30-40% of the actin is polymerized into filaments; the rest is thought to be prevented from polymerizing by the association of thymosin β4 with monomeric actin and by the association of gelsolin with the barbed ends of pre-existing actin filaments. When platelets are activated, there is a rapid increase in actin polymerization; new filaments fill the extending filopodia and form a network at the periphery of the platelet. As a result of activation, myosin binds to cytoplasmic actin filaments, causing them to move towards the center of the platelet. As platelets aggregate, additional cytoskeletal reorganizations occur: GP Ilb-IIIa associates with adhesive ligand in a platelet aggregate; this results in the association of GP Ilb-IIIa, membrane skeleton proteins, and signaling molecules with cytoplasmic actin. Future studies should help to elucidate the significance of the cytoskeleton in regulating signal transduction events in platelets.