Journal
JOURNAL OF STRUCTURAL BIOLOGY
Volume 135, Issue 2, Pages 176-184Publisher
ACADEMIC PRESS INC ELSEVIER SCIENCE
DOI: 10.1006/jsbi.2001.4380
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Funding
- NIGMS NIH HHS [GM56433] Funding Source: Medline
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The TCP-1 ring complex (TRiC; also called CCT, for chaperonin containing TCP-1) is a large (similar to 900 kDa) multisubunit complex that mediates protein folding in the eukaryotic cytosol. The physiological substrate spectrum of TRiC is still poorly defined. Genetic and biochemical data show that it is required for the folding of the cytoskeletal proteins actin and tubulin. Recent years have witnessed a steady stream of reports that describe other proteins that require TRiC for proper folding. Furthermore, analysis of the transit of newly synthesized proteins through TRiC in intact cells suggests that the chaperonin contributes to the folding of a distinct subset of cellular proteins. Here we review the current understanding of a role for TRiC in the folding of newly synthesized polypeptides, with a focus on some of the individual proteins that require TRiC. (C) 2001 Aademic Press.
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