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The interaction network of the chaperonin CCT

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Date
2008-07-09
ICR Author
Paul, Angela
Mccormack, Elizabeth Anne
Willison, Keith
Dekker, Carien
Author
Dekker, C
Stirling, PC
McCormack, EA
Filmore, H
Paul, A
Brost, RL
Costanzo, M
Boone, C
Leroux, MR
Willison, KR
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Type
Journal Article
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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.
URI
https://repository.icr.ac.uk/handle/internal/2437
DOI
https://doi.org/10.1038/emboj.2008.108
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Research team
Chromatin Regulation
Wigley Group
Language
eng
License start date
2008-07-09
Citation
EMBO JOURNAL, 2008, 27 pp. 1827 - 1839
Publisher
NATURE PUBLISHING GROUP

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