Article
- The EMBO Journal (2008) 27, 1827 - 1839
- doi:10.1038/emboj.2008.108
Published online: 29 May 2008
Subject Categories:
The interaction network of the chaperonin CCT
Carien Dekker1,a, Peter C Stirling2,ab, Elizabeth A McCormack1, Heather Filmore1, Angela Paul1, Renee L Brost3, Michael Costanzo3, Charles Boone3, Michel R Leroux2 and Keith R Willison1
- Cancer Research UK Centre for Cell and Molecular Biology, Chester Beatty Laboratories, Institute of Cancer Research, London, UK
- Department of Molecular Biology and Biochemistry, Simon Fraser University, Burnaby, British Columbia, Canada
- Banting and Best Department of Medical Research, Terrence Donnelly Centre for Cellular and Biomolecular Research, University of Toronto, Toronto, Ontario, Canada
Correspondence to:
Keith R Willison, Cancer Research UK Centre for Cell and Molecular Biology, Chester Beatty Laboratories, Institute of Cancer Research, Institute of Cancer Research, 237 Fulham Road, London SW3 6JB, UK. Tel.: +44 20 7878 3855; Fax: +44 20 7351 3325; E-mail: keith.willison@icr.ac.uk
Michel R Leroux, Department of Molecular Biology and Biochemistry, Simon Fraser University, Burnaby, British Columbia, Canada. Tel.: +1 778 782 6683; Fax: +1 778 782 5583; E-mail: leroux@sfu.ca
aThese authors contributed equally to this work
bPresent address: Department of Molecular and Cell Biology, University of California at Berkeley, Berkeley, CA 94720, USA
Received 20 March 2008; Accepted 8 May 2008
Abstract
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.
Keywords:
- CCT,
- chaperone,
- proteomics,
- septin,
- SGA
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