Capping of the barbed-ends of actin filaments is an important mechanism for control of the cytoskeleton. In platelets, a valuable model system, it has been thought that gelsolin was the major capping protein. We now report that platelets contain ~2 μM Cap Z, a calcium insensitive heterodimeric capping protein; two major and additional minor isoforms of both α and β subunits are present. In lysates from resting platelets 75-80% of the Cap Z sediments with the high speed pellet, but if the platelets are activated with thrombin for 10 s, about 15% of the Cap Z leaves the pellet fraction and is found in the high speed supernatant where it is not bound to actin. This translocation of Cap Z to the supernatant is also observed when resting platelets are lysed into buffer containing 50-100 μM GTPγS and 10 mM EGTA. Our results suggest that release of Cap Z from some actin filaments could generate free filament barbed-ends. An increase in free barbed-ends has been reported in platelet lysates prepared shortly after thrombin activation.
Nachmias, V. T., Golla, R., Casella, J. F., & Barron-Casella, E. (1996). Cap Z, a calcium insensitive capping protein in resting and activated platelets. FEBS Letters, 378(3), 258–262. https://doi.org/10.1016/0014-5793(95)01474-8