Cited by 225Heat shock proteins researchMicrotubule and mitosis dynamicsUbiquitin and proteasome pathways

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The interaction network of the chaperonin CCT

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Dekker, Carien, Stirling, Peter C, McCormack, Elizabeth A, Filmore, Heather, Paul, Angela, Brost, Renee L, Costanzo, Michael, Boone, Charles, Leroux, Michel R, Willison, Keith R·2008·The EMBO Journal

DOI 10.1038/emboj.2008.108PMC PMC2486426

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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.

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Authors: Dekker, C., Stirling, P. C., McCormack, E. A., Filmore, H., Paul, A., Brost, R. L., Costanzo, M., Boone, C., Leroux, M. R., & Willison, K. R.
Affiliations: Institute of Cancer Research (GB)
Simon Fraser University (CA)
University of Toronto (CA)
ORCID: Stirling, Peter C
Costanzo, Michael
Boone, Charles
Leroux, Michel R
Willison, Keith R
Venue: The EMBO Journal
Publisher: Springer Science and Business Media LLC
Published: 2008-05-29
Volume: 27
Issue: 13
Pages: 1827-1839
ISSN: 0261-4189 (ISSN-L)
1460-2075
DOI: 10.1038/emboj.2008.108
PMC: PMC2486426
OpenAlex: W2039639602
Cited by: 220
References: 59
Citations by year: 2026: 9 · 2025: 8 · 2024: 10 · 2023: 2 · 2022: 7 · 2021: 9 · 2020: 9 · 2019: 12 · 2018: 18 · 2017: 13 · 2016: 10 · 2015: 15 · 2014: 10 · 2013: 13 · 2012: 15
FWCI: 8.22
Type: journal article
Language: en
Open access: bronze
doi.org
Licence: www.springernature.com/gp/researchers/text-and-data-mining (tdm)
www.springernature.com/gp/researchers/text-and-data-mining (vor)
Locations: The EMBO Journal (publishedVersion)
PubMed Central (publishedVersion)
PubMed (publishedVersion)
Funders: Genome Canada
Michael Smith Health Research BC
Cancer Research UK
Canadian Institutes of Health Research
Natural Sciences and Engineering Research Council of Canada
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Heat shock proteins research
Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Microtubule and mitosis dynamics
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Ubiquitin and proteasome pathways
Keywords: chaperonin CCT, TCP1, protein folding, protein-protein interaction network, nuclear pore complex, chromatin remodeling, protein degradation, septins, cytokinesis, actin folding, tubulin folding, epigenetics, cell division, yeast
MeSH terms: Saccharomyces cerevisiae, Chaperonins, Genomics, Saccharomyces cerevisiae Proteins, Proteomics, Multiprotein Complexes, Cytokinesis, Chaperonin Containing TCP-1

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The interaction network of the chaperonin CCT

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