In situ analysis reveals the TRiC duty cycle and PDCD5 as an open-state cofactor

H Xing, RRE Rosenkranz, P Rodriguez-Aliaga, TT Lee… - Nature, 2024 - nature.com
The ring-shaped chaperonin T-complex protein ring complex (TRiC; also known as
chaperonin containing TCP-1, CCT) is an ATP-driven protein-folding machine that is …

Identification of a Non-canonical Function of Prefoldin Subunit 5 in Proteasome Assembly

SS Ghahe, K Drabikowski, M Stasiak, U Topf - Journal of Molecular Biology, 2024 - Elsevier
The prefoldin complex is a heterohexameric, evolutionarily conserved co-chaperone that
assists in folding of polypeptides downstream of the protein translation machinery. Loss of …

[HTML][HTML] Protocol to study CCT-mediated folding of Gβ5 by single-particle cryo-EM

MI Sass, S Wang, D Mack, SL Cottam, PS Shen… - STAR protocols, 2024 - Elsevier
The chaperonin CCT mediates folding of many cytosolic proteins, including G protein β
subunits (Gβs). Here, we present a protocol for isolating Gβ 5 bound to CCT and its co …

A role of Arabidopsis Phosducin-like2 (AtPhLP2) in regulation of plant growth and development

V Poláková - 2024 - dspace.cuni.cz
Recently, we identified Phosducin-like2 (AtPhLP2) in Arabidopsis as a possible regulator of
growth and development that could be involved in the non-transcriptional auxin response in …

The conformational landscape of TRiC ring-opening and its underlining stepwise mechanism revealed by cryo-EM

M Jin, Y Zang, H Wang, Y Cong - QRB Discovery - cambridge.org
The TRiC/CCT complex assists in the folding of approximately 10% of cytosolic proteins
through an ATP-driven conformational cycle, playing a crucial role in maintaining protein …

The Role of Cytosolic Chaperonin CCT and its Co-Chaperone PhLP1 in Folding and Assembly of Signaling Complexes

Y Kwon - 2023 - scholarsarchive.byu.edu
Abstract CCT, a large (1 MDa) protein-folding machine, is a eukaryotic group II chaperonin
that is essential for folding many cellular proteins and is the most complex of all chaperonins …