Severing of F-actin by yeast cofilin is pH-independent

被引:20
作者
Pavlov, Dmitry
Muhlrad, Andras
Cooper, John
Wear, Martin
Reisler, Emil [1 ]
机构
[1] Univ Calif Los Angeles, Inst Mol Biol, Los Angeles, CA 90095 USA
[2] Washington Univ, Sch Med, Dept Cell Biol & Physiol, St Louis, MO 63110 USA
[3] Hebrew Univ Jerusalem, Hadassah Sch Dent Med, Dept Oral Biol, IL-91010 Jerusalem, Israel
[4] Univ Calif Los Angeles, Dept Chem & Biochem, Los Angeles, CA 90095 USA
来源
CELL MOTILITY AND THE CYTOSKELETON | 2006年 / 63卷 / 09期
关键词
actin; severing; pH; cofilin;
D O I
10.1002/cm.20142
中图分类号
Q2 [细胞生物学];
学科分类号
071009 ; 090102 ;
摘要
Cofilin plays an important role in actin turnover in cells by severing actin filaments and accelerating their depolymerization. The role of pH in the severing by cofilin was examined using fluorescence microscopy. To facilitate the imaging of actin filaments and to avoid the use of rhodamine phalloidin, which competes with cofilin, alpha-actin was labeled with tetramethylrhodamine cadaverine (TRC) at Gln(41). The TRC-labeling inhibited actin treadmilling strongly, as measured by epsilon ATP release. Cofilin binding, detected via an increase in light scattering, and the subsequent conformational change in filament structure, as detected by TRC fluorescence decay, occurred 2-3 times faster at pH 6.8 than at pH 8.0. In contrast, actin filaments severing by cofilin was pH-independent. The pH-independent severing by cofilin was confirmed using actin labeled at Cys(374) with Oregon Green (R) 488 maleimide. The depolymerization of actin by cofilin was faster at high pH.
引用
收藏
页码:533 / 542
页数:10
相关论文
共 51 条
[1]   Putting a new twist on actin: ADF/cofilins modulate actin dynamics [J].
Bamburg, JR ;
McGough, A ;
Ono, S .
TRENDS IN CELL BIOLOGY, 1999, 9 (09) :364-370
[2]  
Bernstein BW, 2000, CELL MOTIL CYTOSKEL, V47, P319, DOI 10.1002/1097-0169(200012)47:4<319::AID-CM6>3.0.CO
[3]  
2-I
[4]   A structural basis for the pH-dependence of cofilin - F-actin interactions [J].
Blondin, L ;
Sapountzi, V ;
Maciver, SK ;
Lagarrigue, E ;
Benyamin, Y ;
Roustan, C .
EUROPEAN JOURNAL OF BIOCHEMISTRY, 2002, 269 (17) :4194-4201
[5]   Cooperative effects of cofilin (ADF) on actin structure suggest allosteric mechanism of cofilin function [J].
Bobkov, AA ;
Muhlrad, A ;
Pavlov, DA ;
Kokabi, K ;
Yilmaz, A ;
Reisler, E .
JOURNAL OF MOLECULAR BIOLOGY, 2006, 356 (02) :325-334
[6]   Cofilin (ADF) affects lateral contacts in F-actin [J].
Bobkov, AA ;
Muhlrad, A ;
Shvetsov, A ;
Benchaar, S ;
Scoville, D ;
Almo, SC ;
Reisler, E .
JOURNAL OF MOLECULAR BIOLOGY, 2004, 337 (01) :93-104
[7]   Structural effects of cofilin on longitudinal contacts in F-actin [J].
Bobkov, AA ;
Muhlrad, A ;
Kokabi, K ;
Vorobiev, S ;
Almo, SC ;
Reisler, E .
JOURNAL OF MOLECULAR BIOLOGY, 2002, 323 (04) :739-750
[8]   Rapid formation and high diffusibility of actin-cofilin cofilaments at low pH [J].
Bonet, C ;
Ternent, D ;
Maciver, SK ;
Mozo-Villarias, A .
EUROPEAN JOURNAL OF BIOCHEMISTRY, 2000, 267 (11) :3378-3384
[9]  
BRADFORD MM, 1976, ANAL BIOCHEM, V72, P248, DOI 10.1016/0003-2697(76)90527-3
[10]   Control of actin dynamics in cell motility - Role of ADF/cofilin [J].
Carlier, MF ;
Ressad, F ;
Pantaloni, D .
JOURNAL OF BIOLOGICAL CHEMISTRY, 1999, 274 (48) :33827-33830