Abstract
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.
| Original language | English (US) |
|---|---|
| Pages (from-to) | 1413-1415 |
| Number of pages | 3 |
| Journal | Science |
| Volume | 250 |
| Issue number | 4986 |
| State | Published - Dec 7 1990 |
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gCap39, a calcium ion- and polyphosphoinositide-regulated actin capping protein. / Yu, Fu Xin; Johnston, Paul A.; Südhof, Thomas C.; Yin, Helen L.
In: Science, Vol. 250, No. 4986, 07.12.1990, p. 1413-1415.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - gCap39, a calcium ion- and polyphosphoinositide-regulated actin capping protein
AU - Yu, Fu Xin
AU - Johnston, Paul A.
AU - Südhof, Thomas C.
AU - Yin, Helen L.
PY - 1990/12/7
Y1 - 1990/12/7
N2 - 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.
AB - 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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UR - http://www.scopus.com/inward/citedby.url?scp=0025651999&partnerID=8YFLogxK
M3 - Article
C2 - 2255912
AN - SCOPUS:0025651999
VL - 250
SP - 1413
EP - 1415
JO - Science
JF - Science
SN - 0036-8075
IS - 4986
ER -