TRiC/CCT chaperonin: structure and function

M Jin, C Liu, W Han, Y Cong - Macromolecular Protein Complexes II …, 2019 - Springer
The eukaryotic group II chaperonin TRiC/CCT assists the folding of 10% of cytosolic proteins
including many key structural and regulatory proteins. TRiC plays an essential role in …

Function and regulation of cytosolic molecular chaperone CCT

H Kubota - 2002 - Elsevier
Molecular chaperones are a group of proteins that assists in the folding of newly synthesized
proteins or in the refolding of denatured proteins. The cytosolic chaperonin-containing t …

Cytosolic chaperonin is up-regulated during cell growth: Preferential expression and binding to tubulin at G1/S transition through early S phase

S Yokota, H Yanagi, T Yura, H Kubota - Journal of Biological Chemistry, 1999 - ASBMB
The chaperonin containing t-complex polypeptide 1 (CCT) is a heterooligomeric molecular
chaperone assisting in the folding of actin, tubulin, and other cytosolic proteins. The …

The Parkin co-regulated gene product, PACRG, is an evolutionarily conserved axonemal protein that functions in outer-doublet microtubule morphogenesis

HR Dawe, H Farr, N Portman… - Journal of cell …, 2005 - journals.biologists.com
Eukaryotic cilia and flagella are highly conserved structures composed of a canonical 9+ 2
microtubule axoneme. Comparative genomics of flagellated and non-flagellated eukaryotes …

The structure and evolution of eukaryotic chaperonin-containing TCP-1 and its mechanism that folds actin into a protein spring

KR Willison - Biochemical Journal, 2018 - portlandpress.com
Actin is folded to its native state in eukaryotic cytosol by the sequential allosteric mechanism
of the chaperonin-containing TCP-1 (CCT). The CCT machine is a double-ring ATPase built …

Cloning, characterization and sub-cellular localization of gamma subunit of T-complex protein-1 (chaperonin) from Leishmania donovani

N Kumari, N Goyal - Biochemical and Biophysical Research …, 2012 - Elsevier
T-complex protein-1 (TCP1) complex, a chaperonin class of protein, ubiquitous in all genera
of life, is involved in intracellular assembly and folding of various proteins. The gamma …

Subunits of the eukaryotic cytosolic chaperonin CCT do not always behave as components of a uniform hetero-oligomeric particle

A Roobol, MJ Carden - European journal of cell biology, 1999 - Elsevier
The chaperonin CCT is an hetero-oligomeric molecular chaperone complex. Stndies in
yeast suggest each of its eight gene products are required for its major identified functions in …

CCTα and CCTδ Chaperonin Subunits Are Essential and Required for Cilia Assembly and Maintenance in Tetrahymena

C Seixas, T Cruto, A Tavares, J Gaertig, H Soares - PloS one, 2010 - journals.plos.org
Background The eukaryotic cytosolic chaperonin CCT is a hetero-oligomeric complex
formed by two rings connected back-to-back, each composed of eight distinct subunits …

Chaperonin containing T-complex polypeptide subunit eta (CCT-eta) is a specific regulator of fibroblast motility and contractility

L Satish, S Johnson, JHC Wang, JC Post, GD Ehrlich… - PLoS …, 2010 - journals.plos.org
Integumentary wounds in mammalian fetuses heal without scar; this scarless wound healing
is intrinsic to fetal tissues and is notable for absence of the contraction seen in postnatal …

Molecular chaperones in cilia and flagella: implications for protein turnover

RE Stephens, NA Lemieux - Cell motility and the cytoskeleton, 1999 - Wiley Online Library
The mechanisms of protein incorporation and turnover in 9+ 2 ciliary axonemes are not
known. Previous reports of an HSP70‐related protein, first in Chlamydomonas flagella and …