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Science 7 December 1990:
Vol. 250. no. 4986, pp. 1413 - 1415
DOI: 10.1126/science.2255912
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Articles

Science, Vol 250, Issue 4986, 1413-1415
Copyright © 1990 by American Association for the Advancement of Science

articles

gCap39, a calcium ion- and polyphosphoinositide-regulated actin capping protein

FX Yu, PA Johnston, TC Sudhof, and HL Yin

Department of Physiology, University of Texas Southwestern Medical Center, Dallas 75235-9040.

The polymerization of actin filaments is involved in growth, movement, and cell division. It has been shown that actin polymerization is controlled by gelsolin, whose interactions with actin are activated by calcium ion (Ca2+) and inhibited by membrane polyphosphoinositides (PPI). A smaller Ca2(+)- and PPI-regulated protein, gCap39, which has 49% sequence identity with gelsolin, has been identified by cDNA cloning and protein purification. Like gelsolin, gCap39 binds to the fast-growing (+) end of actin filaments. However, gCap39 does not sever actin filaments and can respond to Ca2+ and PPI transients independently, under conditions in which gelsolin is ineffective. The coexistence of gCap39 with gelsolin should allow precise regulation of actin assembly at the leading edge of the cell.


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