CCT2

Last update 08 May 2025

Basic Info

Synonyms

99D8.1, CCT-beta, CCT2

+ [4]

Introduction

Component of the chaperonin-containing T-complex (TRiC), a molecular chaperone complex that assists the folding of proteins upon ATP hydrolysis (PubMed:25467444). The TRiC complex mediates the folding of WRAP53/TCAB1, thereby regulating telomere maintenance (PubMed:25467444). As part of the TRiC complex may play a role in the assembly of BBSome, a complex involved in ciliogenesis regulating transports vesicles to the cilia (PubMed:20080638). The TRiC complex plays a role in the folding of actin and tubulin (Probable).

100 Clinical Results associated with CCT2

100 Translational Medicine associated with CCT2

0 Patents (Medical) associated with CCT2

127

Literatures (Medical) associated with CCT2

01 Jun 2025·Theriogenology

Comparative proteomic and transcriptomic analysis of testicular tissue of yaks with or without cryptorchidism

Article

Author: Yang, Dapeng ; Li, Haijun ; Lv, Jinhan ; Qi, Yumei ; Chen, Yulu ; Zeng, Jianlin ; Yuan, Ligang ; Ma, Long

Yak is a large plateau mammal with low reproduction rate, while cryptorchidism is a major reproductive disorder associated with infertility in highland yaks. To better understand the occurrence of cryptorchidism and its regulatory mechanisms in yaks, we conducted a multi-omic analysis, and screened a total of 4456 differentially expressed genes (DEGs) and 332 differentially expressed proteins (DEPs) between normal and unilateral cryptorchid testes of yaks using high-throughput transcriptome sequencing (RNA-seq) and Tandem Mass Tag (TMT)-based proteomics techniques, with testes from yaks with cryptorchidism as the target. Enrichment analysis revealed that the DEGs were associated with cell growth, sperm motility, immune regulation, and intercellular tight junctions, and were mainly enriched in pathways related to cell differentiation; amino acid, sugar, and lipid metabolism; cell adhesion, and hypoxia tolerance. The results of protein interactions network analyses indicated tight interactions between the differential proteins CCT2, CCT4, CCT5, FZR1, and PSMA8. In conclusion. This expression of these differential genes and proteins dysregulation may lead to the obstruction of the testicular descent process or the abnormal development of the testis, potentially leading to cryptorchidism. The results of this study laid a foundation for the screening of key candidate genes and proteins for cryptorchidism in yak, and also provided a theoretical basis for the research molecular mechanism of reproductive system diseases in yak and plateau animals.

01 Feb 2025·Neurochemical Research

Neuroprotective Effects of Chaperonin Containing TCP1 Subunit 2 (CCT2) on Motor Neurons Following Oxidative or Ischemic Stress

Article

Author: Yoo, Dae Young ; Hwang, In Koo ; Choi, Goang-Min ; Oh, Jae Keun ; Mun, Hyunwoong ; Kim, Dae Won ; Moon, Seung Myung ; Kwon, Hyun Jung

Chaperonin containing TCP1 (CCT) is an essential protein that controls proteostasis following spinal cord damage. In particular, CCT2 plays an important role in neuronal death in various neurological disorders; however, few studies have investigated the effects of CCT2 on ischemic damage in the spinal cord. In the present study, we synthesized a cell-permeable Tat-CCT2 fusion protein and observed its effects on H₂O₂-induced oxidative damage in NSC34 motoneuron-like cells and in the spinal cord after ischemic injury. Tat-CCT2, but not its control protein CCTs, was delivered into NSC34 cells in a concentration- and incubation time-dependent manner, and a clear cytosolic location of the delivered protein was observed. In addition, the delivered protein gradually degraded, and nearly control levels were observed 24 h after Tat-CCT2 treatment. Tat-CCT2 treatment significantly ameliorated 200 µM H₂O₂-induced neuronal damage in NSC34 cells at 8.0 µM protein treatment. Additionally, Tat-CCT2 significantly ameliorated H₂O₂-induced reactive oxygen species formation and DNA fragmentation. In the rabbit spinal cord, Tat-CCT2 was efficiently delivered into the spinal cord 4 h after 0.125 mg/kg protein treatment. In addition, treatment with Tat-CCT2 significantly improved the neurological scores based on the Tarlov criteria 24 and 72 h after ischemia/reperfusion. Moreover, the number of surviving neurons in the ventral horn of the spinal cord was significantly increased in the Tat-CCT2-treated group 3 and 7 days after ischemia compared to vehicle-treated group. Treatment with Tat-CCT2 alleviated the ischemia-induced oxidative stress and ferroptosis-related factor (malondialdehyde, 8-iso-prostaglandin F2α, and high mobility group box 1) and pro-inflammatory cytokine (interleukin-1β, interleukin-6, and tumor necrosis factor-α) releases in the ventral horn of the spinal cord 8 and 24 h after ischemia/reperfusion. In addition, Tat-CCT2 treatment significantly ameliorated ischemia-induced microglial activation in the ventral horn of spinal cord 24 h after reperfusion. These results suggest that Tat-CCT2 mitigates ischemia-induced neuronal damage in the spinal cord.

01 Jan 2025·QRB Discovery

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

Article

Author: Jin, Mingliang ; Wang, Huping ; Cong, Yao ; Zang, Yunxiang

AbstractThe 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 homeostasis. Despite our understanding of ATP-driven TRiC ring closing and substrate folding, the process and mechanisms underlying TRiC ring-opening and substrate release remain largely unexplored. In this study, by determining an ensemble of cryo-EM structures of yeast TRiC in the presence of ADP, including three intermediate transition states, we present a comprehensive picture of the TRiC ring-opening process. During this process, CCT3 detects the loss of γ-phosphate and initiates with the dynamics of its apical protrusion, and expands to the outward leaning of the consecutive CCT6/8/7/5 subunits. This is followed by significant movements of CCT2, CCT4, and especially CCT1 subunits, resulting in the opening of the TRiC rings. We also observed an unforeseen temporary separation between the two rings in the CCT2 side, coordinating the release of the originally locked CCT4 N-terminus, which potentially participates in the ring-opening process. Collectively, our study reveals a stepwise TRiC ring-opening mechanism, provides a comprehensive view of the TRiC conformational landscape, and sheds lights on its subunit specificity in sensing nucleotide status and substrate release. Our findings deepen our understanding of protein folding assisted by TRiC and may inspire new strategies for the diagnosis and treatment of related diseases.

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CCT2

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