Coactosin interferes with the capping of actin filaments

FEBS Letters

Schleicher, Michael²  Röhrig, Ursula¹  Morozova, Ludmilla¹  Gerisch, Günther¹  Wegner, Albrecht³ 

[1] Max-Planck-Institut für Biochemie, 82152 Martinsried, Germany;Institut für Zellbiologie, Ludwig-Maximilians-Universität, Schillerstraβe 42, 80336 München, Germany;Institut für Physiologische Chemie, Ruhr-Universität, Universitätsstraβe 150, 44780 Bochum, Germany

关键词: Cytoskeleton;    Actin polymerization;    Coactosin;    F-actin capping protein;    cap32/34;    Severin;   

DOI  :  10.1016/0014-5793(95)01130-7

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Coactosin, a 16 kDa protein associated with the actin cytoskeleton from Dictyostelium discoideum, was purified by an improved method, in which other components of the cytoskeleton were removed. The highly purified coactosin had no effect on the time course of actin polymerization, but when added to actin in presence of capping proteins, coactosin counteracted the capping activity of these proteins. The capping proteins cap32/34 and severin domain 1 retarded actin polymerization, on addition of coactosin to samples containing one of these capping proteins the time course of actin polymerization became close to controls without capping proteins.

【 授权许可】

Unknown