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The interaction network of the chaperonin CCT
Author(s) -
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
Publication year - 2008
Publication title -
the embo journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 7.484
H-Index - 392
eISSN - 1460-2075
pISSN - 0261-4189
DOI - 10.1038/emboj.2008.108
Subject(s) - septin , chaperonin , biology , cytokinesis , microbiology and biotechnology , cytoskeleton , function (biology) , actin , cell division , cytosol , protein folding , genetics , biochemistry , cell , enzyme
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.