Interactions of drebrin and gephyrin with profilin

被引：117

作者：

Mammoto, A

Sasaki, T

Asakura, T

Hotta, I

Imamura, H

Takahashi, K

Matsuura, Y

Shirao, T

Takai, Y

机构：

[1] Osaka Univ, Sch Med, Dept Mol Biol & Biochem, Suita, Osaka 565, Japan

[2] Natl Inst Infect Dis, Dept Virol 2, Tokyo 162, Japan

[3] Gunma Univ, Sch Med, Dept Neurobiol & Behav, Maebashi, Gumma 371, Japan

来源：

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 1998年 / 243卷 / 01期

关键词：

D O I：

10.1006/bbrc.1997.8068

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：

Profilin is an ac tin monomer-binding protein which stimulates actin polymerization. Recent studies have revealed that profilin interacts with VASP, Mena, Bni1p, Bnr1p, and mDia, all of which have the proline-rich domain. Here, we isolated three profilin-binding proteins from rat brain cytosol by glutathione S-transferase-profilin affinity column chromatography and identified them as Mena, drebrin, and gephyrin. These proteins had a proline-rich domain and directly interacted with profilin. (C) 1998 Academic Press.

引用

页码：86 / 89

页数：4

共 27 条

[1]

BRADFORD MM, 1976, ANAL BIOCHEM, V72, P248, DOI 10.1016/0003-2697(76)90527-3

[2] Bni1p, a yeast formin linking Cdc42p and the actin cytoskeleton during polarized morphogenesis [J].