Interactions between CAP70 and actinfilin are important for integrity of actin cytoskeleton structures in neurons

被引：11

作者：

Chen, Y

Li, M

机构：

[1] Johns Hopkins Univ, Sch Med, Dept Neurosci, Baltimore, MD 21205 USA

[2] Johns Hopkins Univ, Sch Med, High Throughput Biol Ctr, Baltimore, MD 21205 USA

来源：

NEUROPHARMACOLOGY | 2005年 / 49卷 / 07期

基金：

美国国家卫生研究院;

关键词：

protein interaction; PDZ domain; molecular organization; actin cytoskeleton; postsynaptic density;

D O I：

10.1016/j.neuropharm.2005.05.022

中图分类号：

Q189 [神经科学];

学科分类号：

071006 ;

摘要：

The integrity of dynamic actin structures is coupled to a variety of neurological processes. Actin-binding proteins play a critical role in regulating actin structure dynamics. A link between actin-binding proteins and receptor interacting scaffolding proteins may provide a conduit for transmitting signaling events to the cytoskeleton. Actinfilin is a brain-enriched actin-binding protein, though its functions are currently unknown. We report here that actinfilin interacts with the multi-PDZ domain protein CAP70. Recombinant expression of an actin-binding domain of actinfilin progressively causes marked changes of cellular morphology. The effect on cell morphology may be reduced by co-expression with CAP70. Mutation of actinfilin lacking the ability to interact with CAP70 abolished the effect by CAP70. The evidence suggests a role of actinfilin and possible regulation by scaffolding proteins. (c) 2005 Elsevier Ltd. All rights reserved.

引用

收藏

页码：1026 / 1041

页数：16

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