ArticleCell death discovery2022
Disruption of actin dynamics induces autophagy of the eukaryotic chaperonin TRiC/CCT.
Article in Cell death discovery, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
10 citing papers in PubMed, 7 citations in OpenAlex.
- Knockdown of CCT2 inhibits the malignant progression of hepatocellular carcinoma cells by impairing STAT3 activation.Oncology reports · 2026Article
- Review
- Chaperonin in health and disease.Molecular biomedicine · 2026Review
- Mapping the chaperonin TRiC/CCT interactome in mouse photoreceptors reveals functional significance for energy metabolism.PloS one · 2026Article
- Lassa virus Z protein hijacks the autophagy machinery for efficient transportation by interrupting CCT2-mediated cytoskeleton network formation.Autophagy · 2024Article
- Review
- The N-acetylglucosaminyltransferase Radical fringe contributes to defects in JAG1-dependent turnover and signaling of NOTCH3 CADASIL mutants.The Journal of biological chemistry · 2024Article
- Effect of natural products on host cell autophagy induced by Influenza A virus infection.Frontiers in cellular and infection microbiology · 2024Review
- The TRiCky Business of Protein Folding in Health and Disease.Frontiers in cell and developmental biology · 2022Review
- The malaria parasite chaperonin containing TCP-1 (CCT) complex: Data integration with other CCT proteomes.Frontiers in molecular biosciences · 2022Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Autophagy plays important role in the intracellular protein quality control system by degrading abnormal organelles and proteins, including large protein complexes such as ribosomes. The eukaryotic chaperonin tailless complex polypeptide 1 (TCP1) ring complex (TRiC), also called chaperonin-containing TCP1 (CCT), is a 1-MDa hetero-oligomer complex comprising 16 subunits that facilitates the folding of ~10% of the cellular proteome that contains actin. However, the quality control mechanism of TRiC remains unclear. To monitor the autophagic degradation of TRiC, we generated TCP1α-RFP-GFP knock-in HeLa cells using a CRISPR/Cas9-knock-in system with an RFP-GFP donor vector. We analyzed the autophagic degradation of TRiC under several stress conditions and found that treatment with actin (de)polymerization inhibitors increased the lysosomal degradation of TRiC, which was localized in lysosomes and suppressed by deficiency of autophagy-related genes. Furthermore, we found that treatment with actin (de)polymerization inhibitors increased the association between TRiC and unfolded actin, suggesting that TRiC was inactivated. Moreover, unfolded actin mutants were degraded by autophagy. Taken together, our results indicate that autophagy eliminates inactivated TRiC, serving as a quality control system.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.