The interaction network of the chaperonin CCT

被引：163

作者：

Dekker, Carien ^{[1
]}

Stirling, Peter C. ^{[2
]}

McCormack, Elizabeth A. ^{[1
]}

Filmore, Heather ^{[1
]}

Paul, Angela ^{[1
]}

Brost, Renee L. ^{[3
]}

Costanzo, Michael ^{[3
]}

Boone, Charles ^{[3
]}

Leroux, Michel R. ^{[2
]}

Willison, Keith R. ^{[1
]}

机构：

[1] Inst Canc Res, Canc Res UK Ctr Cell & Mol Biol, Chester Beatty Labs, London SW3 6JB, England

[2] Simon Fraser Univ, Dept Mol Biol & Biochem, Burnaby, BC V5A 1S6, Canada

[3] Univ Toronto, Banting & Best Dept Med Res, Terrence Donnelly Ctr Cellular & Biomol Res, Toronto, ON, Canada

来源：

EMBO JOURNAL | 2008年 / 27卷 / 13期

关键词：

CCT; chaperone; proteomics; septin; SGA;

D O I：

10.1038/emboj.2008.108

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：

The eukaryotic cytosolic chaperonin containing TCP-1 (CCT) has an important function in maintaining cellular homoeostasis by assisting the folding of many proteins, including the cytoskeletal components actin and tubulin. Yet the nature of the proteins and cellular pathways dependent on CCT function has not been established globally. Here, we use proteomic and genomic approaches to define CCT interaction networks involving 136 proteins/genes that include links to the nuclear pore complex, chromatin remodelling, and protein degradation. Our study also identifies a third eukaryotic cytoskeletal system connected with CCT: the septin ring complex, which is essential for cytokinesis. CCT interactions with septins are ATP dependent, and disrupting the function of the chaperonin in yeast leads to loss of CCT-septin interaction and aberrant septin ring assembly. Our results therefore provide a rich framework for understanding the function of CCT in several essential cellular processes, including epigenetics and cell division.

引用

页码：1827 / 1839

页数：13

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