Results 21 to 30 of about 37,307 (249)

DCAF12 Ubiquitin Ligase Promotes Lung Cancer Metastasis by Modulating the TRiC/CCT Chaperonin Complex. [PDF]

Adv Sci (Weinh)
This study elucidates how DCAF12 facilitates non‐degradative ubiquitination to stabilize TRiC/CCT, thereby enhancing the folding capacity of chaperonins. This mechanism promotes the maturation of cytoskeletal proteins and activates key oncogenic drivers, including YAP, STAT3, and mTOR, ultimately driving metastatic progression in lung cancer.
Wang Z, Huang H, Huang K, Cui X, Wu L, Lin R, Zhao Z, Chen H, Zheng C, Jin W, Chen S, Chen J, Xu Y, Wei D.   +13 more
europepmc   +2 more sources

Emerging Roles of the Unique Molecular Chaperone Cosmc in the Regulation of Health and Disease

Biomolecules, 2022
The core-1 β1-3galactosyltransferase-specific chaperone 1 (Cosmc) is a unique molecular chaperone of core-1 β1-3galactosyltransferase(C1GALT1), which typically functions inside the endoplasmic reticulum (ER).
Ting Xiang, Muchuan Qiao, Jiangbo Xie, Zheng Li, Hailong Xie   +4 more
doaj   +1 more source

The malaria parasite chaperonin containing TCP-1 (CCT) complex: Data integration with other CCT proteomes

Frontiers in Molecular Biosciences, 2022
The multi-subunit chaperonin containing TCP-1 (CCT) is an essential molecular chaperone that functions in the folding of key cellular proteins. This paper reviews the interactome of the eukaryotic chaperonin CCT and its primary clients, the ubiquitous ...
Mark D. Wilkinson, Josie L. Ferreira, Morgan Beeby, Jake Baum, Jake Baum, Keith R. Willison   +5 more
doaj   +1 more source

Polycomb Requires Chaperonin Containing TCP-1 Subunit 7 for Maintaining Gene Silencing in Drosophila

Frontiers in Cell and Developmental Biology, 2021
In metazoans, heritable states of cell type-specific gene expression patterns linked with specialization of various cell types constitute transcriptional cellular memory.
Najma Shaheen, Jawad Akhtar, Zain Umer, Muhammad Haider Farooq Khan, Mahnoor Hussain Bakhtiari, Murtaza Saleem, Amir Faisal, Muhammad Tariq   +7 more
doaj   +1 more source

Evaluation and Characterization of the Insecticidal Activity and Synergistic Effects of Different GroEL Proteins from Bacteria Associated with Entomopathogenic Nematodes on Galleria mellonella

Toxins, 2023
GroEL is a chaperonin that helps other proteins fold correctly. However, alternative activities, such as acting as an insect toxin, have also been discovered.
Abraham Rivera-Ramírez, Rosalba Salgado-Morales, Janette Onofre-Lemus, Blanca I. García-Gómez, Humberto Lanz-Mendoza, Edgar Dantán-González   +5 more
doaj   +1 more source

Investigating Chaperonin-Containing TCP-1 subunit 2 as an essential component of the chaperonin complex for tumorigenesis

Scientific Reports, 2020
Chaperonin-containing TCP-1 (CCT or TRiC) is a multi-subunit complex that folds many of the proteins essential for cancer development. CCT is expressed in diverse cancers and could be an ideal therapeutic target if not for the fact that the complex is ...
Anne E. Showalter, A. Martini, Daniel Nierenberg, Kristen Hosang, N. Fahmi, P. Gopalan, A. Khaled, Wei Zhang, A. Khaled   +8 more
semanticscholar   +1 more source

Chaperonin genes on the rise: new divergent classes and intense duplication in human and other vertebrate genomes

BMC Evolutionary Biology, 2010
Background Chaperonin proteins are well known for the critical role they play in protein folding and in disease. However, the recent identification of three diverged chaperonin paralogs associated with the human Bardet-Biedl and McKusick-Kaufman ...
Macario Alberto JL, Conway de Macario Everly, Mukherjee Krishanu, Brocchieri Luciano   +3 more
doaj   +1 more source

Myelin pathology: Involvement of molecular chaperones and the promise of chaperonotherapy [PDF]

, 2019
The process of axon myelination involves various proteins including molecular chaperones. Myelin alteration is a common feature in neurological diseases due to structural and functional abnormalities of one or more myelin proteins.
Cappello F., Conway De Macario E., Macario A. J. L., Marino Gammazza A., Scalia F.   +4 more
core   +1 more source

Hsp60 Post-translational Modifications: Functional and Pathological Consequences

Frontiers in Molecular Biosciences, 2020
Hsp60 is a chaperone belonging to the Chaperonins of Group I and typically functions inside mitochondria in which, together with the co-chaperonin Hsp10, maintains protein homeostasis.
Celeste Caruso Bavisotto, Celeste Caruso Bavisotto, Giusi Alberti, Alessandra Maria Vitale, Letizia Paladino, Claudia Campanella, Francesca Rappa, Magdalena Gorska, Everly Conway de Macario, Everly Conway de Macario, Francesco Cappello, Francesco Cappello, Alberto J. L. Macario, Alberto J. L. Macario, Antonella Marino Gammazza   +14 more
doaj   +1 more source

Structural basis for active single and double ring complexes in human mitochondrial Hsp60-Hsp10 chaperonin

Nature Communications, 2020
mHsp60-mHsp10 assists the folding of mitochondrial matrix proteins without the negative ATP binding inter-ring cooperativity of GroEL-GroES. Here we report the crystal structure of an ATP (ADP:BeF 3 -bound) ground-state mimic double-ring mHsp60 14 ...
Y. Gómez-Llorente, F. Jebara, M. Patra, R. Malik, S. Nisemblat, Orna Chomsky-Hecht, A. Parnas, A. Azem, J. Hirsch, I. Ubarretxena-Belandia   +9 more
semanticscholar   +1 more source