Human small heat shock proteins: Protein interactomes of homo- and hetero-oligomeric complexes: An update

被引:103
|
作者
Arrigo, Andre-Patrick [1 ]
机构
[1] Univ Lyon 1, Apoptosis Canc & Dev Lab, Lyon Canc Res Ctr, INSERM CNRS UMR5286 U1052, F-69365 Lyon, France
关键词
Human small Hsps; Protein interactome; Hetero-oligomeric complexe; G6PD; ALPHA-B-CRYSTALLIN; CHAPERONE-LIKE ACTIVITY; MOLECULAR CHAPERONE; ACTIN CYTOSKELETON; PROSTATE-CANCER; STRESS-PROTEIN; INTERACTION NETWORK; PROTECTIVE ACTIVITY; MISFOLDED PROTEINS; ANDROGEN ABLATION;
D O I
10.1016/j.febslet.2013.05.011
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
Small heat shock proteins (sHsps) regulate a large number of fundamental cellular processes and are involved in many pathological diseases. They share complex oligomerization and phosphorylation properties allowing them to interact and modulate the activity of many client proteins. Here, the up-to date protein interactome of the ten human sHsps is presented as an illustration of their multiple cellular functions. In addition of forming homo-oligomers, some of these proteins interact whith each other and form hetero-oligomeric complexes that could bear new protein targets recognition abilities. Here, novel informations are presented on how the formation of HspB1/HspB5 complex can stimulate the activity of the oxidoresistance promoting enzyme glucose 6-phosphate dehydrogenase through its interaction with newly formed highly phosphorylated HspB1 homo-oligomers. (C) 2013 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
引用
收藏
页码:1959 / 1969
页数:11
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