Literature summary for 3.6.4.B10 extracted from

Gestaut, D.; Roh, S.H.; Ma, B.; Pintilie, G.; Joachimiak, L.A.; Leitner, A.; Walzthoeni, T.; Aebersold, R.; Chiu, W.; Frydman, J.
The chaperonin TRiC/CCT associates with prefoldin through a conserved electrostatic interface essential for cellular proteostasis (2019), Cell, 177, 751-765.e15 .

Search for more literature for 3.6.4.B10

Cloned(Commentary)

Cloned (Comment)	Organism
genes CCT1-8, recombinant expression of GFP-tagged subunits CCT-alpha, CCT-beta, CCT-gamma, CCT-delta, CCT-epsilon, CCT-zeta-1, CCT-eta, and CCT-theta in insect cells, method overview. Examination if recombinant hTRiC and or hTRiC-GFP are assembled into the correct and evolutionarily conserved subunit arrangement using disuccinimidyl suberate (DSS) XL-MS	Homo sapiens

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Mg2+	required	Homo sapiens

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
ATP + H2O	Homo sapiens	-	ADP + phosphate	-	?

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	P17987 AND P78371 AND P49368 AND P50991 AND P48643 AND P40227 AND Q99832 AND P50990	genes CCT1-8 encoding subunits CCT-alpha, CCT-beta, CCT-gamma, CCT-delta, CCT-epsilon, CCT-zeta-1, CCT-eta, and CCT-theta	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
ATP + H2O	-	Homo sapiens	ADP + phosphate	-	?
additional information	functional cooperation of TRiC and PFD in actin folding. In the absence of PFD, TRiC mediates actin folding with biphasic kinetics. Upon ATP addition, a burst of folding activity (about 4 min) is followed by a much slower and inefficient folding phase that extended up to 60 min. Following ATP addition, PFD enhances the yield of actin folding and disfavored actin aggregation. Substrate folding and PFD interactions, detailed overview. PFD is not merely capturing actin that is released from TRiC due to ATP cycling. Instead, it appears that transfer is mediated by a ternary TRiC-actin-PFD complex, from which actin partitions between TRiC and PFD. Dynamic TRiC-PFD interaction	Homo sapiens	?	-	-

Subunits

Subunits	Comment	Organism
octamer	-	Homo sapiens

Synonyms

Synonyms	Comment	Organism
chaperonin TRiC/CCT	-	Homo sapiens
TriC	-	Homo sapiens

Cofactor

Cofactor	Comment	Organism	Structure
prefoldin	PFD, is required for protein substrate folding, PFD pivots around a conserved electrostatic interface with TRiC/CCT, PFD acts on TRiC/CCT-substrate complex to enhance the rate of the folding reaction. PFD alternates between an open latched conformation and a closed engaged conformation that aligns the PFD-TRiC substrate binding chambers. PFD can act after TRiC binds its substrates to enhance the rate and yield of the folding reaction, suppressing non-productive reaction cycles. Disrupting the TRiC-PFD interaction in vivo is strongly deleterious, leading to accumulation of amyloid aggregates	Homo sapiens

General Information

General Information	Comment	Organism
malfunction	disrupting the TRiC-PFD interaction in vivo is strongly deleterious, leading to accumulation of amyloid aggregates	Homo sapiens
physiological function	direct interactions between two chaperonins allow them to feed folding substrates bi-directionally between active sites, preventing aggregation and promoting proteostasis. The essential ring-shaped chaperonin TRiC/CCT cooperates with the chaperone prefoldin/GIMc (PFD). These hetero-oligomeric chaperones associate in a defined architecture, through a conserved interface of electrostatic contacts that serves as a pivot point for a TRiC-PFD conformational cycle. PFD pivots around a conserved electrostatic interface with TRiC/CCT PFD acts on TRiC/CCT-substrate complex to enhance the rate of the folding reaction, overview. The suprachaperone assembly formed by PFD and TRiC is essential to prevent toxic conformations and ensure effective cellular proteostasis	Homo sapiens

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Release 2023.1 (January 2023)