Subunits of the chaperonin CCT interact with F-actin and influence cell shape and cytoskeletal assembly

被引：58

作者：

Brackley, Karen I. ^{[1
]}

Grantham, Julie ^{[1
]}

机构：

[1] Univ Gothenburg, Dept Cell & Mol Biol, S-40530 Gothenburg, Sweden

来源：

EXPERIMENTAL CELL RESEARCH | 2010年 / 316卷 / 04期

基金：

瑞典研究理事会;

关键词：

Molecular chaperone; Chaperonin; Cytoskeleton; Actin; MAMMALIAN NONMUSCLE CELLS; EUKARYOTIC CHAPERONIN; SACCHAROMYCES-CEREVISIAE; CYCLE PROGRESSION; IN-VITRO; ORGANIZATION; TUBULIN; COMPLEX; IDENTIFICATION; SUPPRESSOR;

D O I：

10.1016/j.yexcr.2009.11.003

中图分类号：

R73 [肿瘤学];

学科分类号：

100214 ;

摘要：

The integrity of the cytoskeleton is closely linked to the oligomeric chaperonin containing TCP-1 (CCT) via the folding requirements of actin and tubulin, but the role of CCT in cytoskeletal Organization remains unclear. We address this issue by analyzing the effects of targeting CCT subunits via siRNA and assessing their location/assembly state in cultured mammalian cells. Reducing levels of individual CCT subunits implicates CCT epsilon in influencing cell shape and reduced levels of this Subunit limit the cells' ability to recover from microfilament depolymerization. Conversely, cells displayed enhanced microtubule regrowth when CCT subunit levels were altered by siRNA. Some CCT subunits co-localize with F-actin, whilst all are predominantly monomeric in extracts enriched for the cytoskeleton. This provides compelling evidence that some CCT subunits as monomers can influence cytoskeletal organization/polymerization. Therefore the activity of CCT may well extend beyond the folding of newly synthesized polypeptides, representing a novel function for CCT Subunits distinct from their role in the CCT oligomer. (C) 2009 Elsevier Inc. All rights reserved.

引用

页码：543 / 553

页数：11

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