期刊
INTERNATIONAL JOURNAL OF BIOCHEMISTRY & CELL BIOLOGY
卷 45, 期 2, 页码 344-346出版社
PERGAMON-ELSEVIER SCIENCE LTD
DOI: 10.1016/j.biocel.2012.11.011
关键词
Small heat shock proteins; Phosphorylation; Cytoskeleton; Actin filaments
资金
- Russian Foundation for Basic Science
The recently published paper by Wettstein et al. (2012) reviews the data of literature dealing with participation of small heat shock proteins (sHsp) in cytoskeleton regulation. Analyzing the effect of sHsp on microfilaments, the authors come to conclusion that depending on phosphorylation HspB1 can function as barbed-end-capping protein and can prevent aggregation of F-actin under stress conditions. The modern data do not confirm all these suggestions. We propose that stabilization effect of HspB1 on microfilaments is due to HspB1 interaction with partially unfolded actin or with genuine actin-binding proteins. In addition, HspB1 can exert its stabilizing effect on F-actin by modulating other elements of the cytoskeleton (intermediate filaments and microtubules) or by controlling homeostasis (for instance, redox state). Without being genuine actin-binding proteins, HspB1 and HspB6 predominantly protect microfilaments via an indirect mechanism that is yet to be characterized. (C) 2012 Elsevier Ltd. All rights reserved.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据