TALIN BINDS TO ACTIN AND PROMOTES FILAMENT NUCLEATION

被引：74

作者：

KAUFMANN, S ^{[1
]}

PIEKENBROCK, T ^{[1
]}

GOLDMANN, WH ^{[1
]}

BARMANN, M ^{[1
]}

ISENBERG, G ^{[1
]}

机构：

[1] TECH UNIV MUNICH,DEPT BIOPHYS E22,W-8046 GARCHING,GERMANY

来源：

FEBS LETTERS | 1991年 / 284卷 / 02期

关键词：

TALIN; PLATELET; ACTIN POLYMERIZATION;

D O I：

10.1016/0014-5793(91)80681-R

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Platelet talin binds to actin in vitro and hence is an actin binding protein. By four different non-interfering assay conditions (fluorescence, fluorescence recovery after photobleaching, (FRAP), dynamic light scattering and DNase-I inhibition) we show that talin promotes filament nucleation, raises the filament number concentration and increases the net rate of actin polymerization but has no inhibitory effect on filament elongation. Binding of talin to actin occurs at a maximal molar ratio of 1:3 as determined by fluorescencetitration under G-buffer conditions. The overall binding constant was almost-equal-to 0.25-mu-M.

引用

页码：187 / 191

页数：5

共 18 条

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