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

Fu Xin Yu; Paul A. Johnston; Thomas C. Südhof; Helen L. Yin

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

Fu Xin Yu, Paul A. Johnston, Thomas C. Südhof, Helen L. Yin

Research output: Contribution to journal › Article › peer-review

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

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.",

author = "Yu, {Fu Xin} and Johnston, {Paul A.} and S{\"u}dhof, {Thomas C.} and Yin, {Helen L.}",

year = "1990",

month = dec,

day = "7",

language = "English (US)",

volume = "250",

pages = "1413--1415",

journal = "Science",

issn = "0036-8075",

publisher = "American Association for the Advancement of Science",

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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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AN - SCOPUS:0025651999

SN - 0036-8075

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JF - Science

IS - 4986

ER -

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

Abstract

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