Association of CCT/TriC with other substrates during biosynthesis (unknown chaperone)

Stable Identifier
Homo sapiens
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A combination of proteomic and bioinformatics analyses of TRiC substrates has revealed that they have complex topologies that are slow folding and aggregation prone (Yam et al., 2008). These substrates are also enriched in proteins that belong to oligomeric assemblies suggesting that TRiC plays a role in promoting complex assembly (Yam et al., 2008). Two possible mechanisms describing the role of TriC have been suggested (Yam et al., 2008). The processes of TRiC-mediated folding and assembly could be directly coupled, or TRiC could fold monomeric subunits and hold them in an assembly-competent state until they associate with the appropriate partner subunits. The complete list of TriC subsrates is not yet known. Many of its substrates that are targeted during biosynthesis are conserved between mammals and yeast (Yam et al. 2008).

Literature References
PubMed ID Title Journal Year
25467444 Proteostatic control of telomerase function through TRiC-mediated folding of TCAB1

Venteicher, AS, Frydman, J, Veenstra, TD, Meng, Z, Artandi, SE, Freund, A, Zhong, FL

Cell 2014
21098288 Decreased glucocerebrosidase activity in Gaucher disease parallels quantitative enzyme loss due to abnormal interaction with TCP1 and c-Cbl

Zhuang, Z, Chen, M, Thompson, E, Lu, J, Xu, DS, Kaneski, CR, Iyer, RR, Hodes, RJ, Chiang, J, Lonser, RR, Brady, RO, Yang, C

Proc. Natl. Acad. Sci. U.S.A. 2010
24756126 Modulation of STAT3 folding and function by TRiC/CCT chaperonin

Tweardy, DJ, Frydman, J, Eckols, TK, Kasembeli, M, Chiu, W, Lau, WC, Roh, SH

PLoS Biol. 2014
23747015 Interaction of p53 with the CCT complex promotes protein folding and wild-type p53 activity

Trinidad, AG, Klejnot, M, Cuellar, J, Valpuesta, JM, Nobis, M, Vousden, KH, Muller, PA

Mol. Cell 2013
9819444 Maturation of human cyclin E requires the function of eukaryotic chaperonin CCT

Won, KA, Reed, SI, Farr, GW, Horwich, AL, Schumacher, RJ

Mol. Cell. Biol. 1998
25342745 The molecular chaperone TRiC/CCT binds to the Trp-Asp 40 (WD40) repeat protein WDR68 and promotes its folding, protein kinase DYRK1A binding, and nuclear accumulation

Aoshima, M, Shibata, T, Nishida, E, Miyata, Y, Tsubata, T

J. Biol. Chem. 2014
21995946 Chaperonin TRiC assists the refolding of sperm-specific glyceraldehyde-3-phosphate dehydrogenase

Muronetz, VI, Sevostyanova, IA, Schmalhausen, EV, Kuravsky, ML, Popova, KM, Eldarov, MA, Naletova, IN

Arch. Biochem. Biophys. 2011
12502735 Assembly of the SMRT-histone deacetylase 3 repression complex requires the TCP-1 ring complex

Yen, TJ, Guenther, MG, Kao, GD, Yu, J, Lazar, MA

Genes Dev. 2002
19011634 Defining the TRiC/CCT interactome links chaperonin function to stabilization of newly made proteins with complex topologies

Lin, HT, Burlingame, A, Frydman, J, Xia, Y, Gerstein, M, Yam, AY

Nat Struct Mol Biol 2008
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