ArticleMolecular biology of the cell2015
A novel function of the monomeric CCTε subunit connects the serum response factor pathway to chaperone-mediated actin folding.
Article in Molecular biology of the cell, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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Who cites it
20 citing papers in PubMed, 37 citations in OpenAlex.
- Integration of CCT/TRiC assembly, degradation and function: Chaperonin complexity in a cellular context.Cell stress & chaperones · 2026Review
- The CCT chaperonin and actin modulate the ER and RNA-binding protein condensation during oogenesis and maintain translational repression of maternal mRNA and oocyte quality.Molecular biology of the cell · 2024Article
- Enterovirus-A71 exploits RAB11 to recruit chaperones for virus morphogenesis.Journal of biomedical science · 2024Article
- A hierarchical assembly pathway directs the unique subunit arrangement of TRiC/CCT.Molecular cell · 2023Article
- Chaperonin TRiC/CCT Participates in Mammarenavirus Multiplication in Human Cells via Interaction with the Viral Nucleoprotein.Journal of virology · 2023Article
- Structural and Dynamic Disturbances Revealed by Molecular Dynamics Simulations Predict the Impact on Function of CCT5 Chaperonin Mutations Associated with Rare Severe Distal Neuropathies.International journal of molecular sciences · 2023Article
- The TRiCky Business of Protein Folding in Health and Disease.Frontiers in cell and developmental biology · 2022Review
- Native mass spectrometry analyses of chaperonin complex TRiC/CCT reveal subunit N-terminal processing and re-association patterns.Scientific reports · 2021Article
- Human Papillomavirus infection requires the CCT Chaperonin Complex.Journal of virology · 2021Article
- Correlated fluorescence microscopy and multi-ion beam secondary ion mass spectrometry imaging reveals phosphatidylethanolamine increases in the membrane of cancer cells over-expressing the molecular chaperone subunit CCTδ.Analytical and bioanalytical chemistry · 2021Article
- Molecular and Clinical Characterization of CCT2 Expression and PrognosisFrontiers in oncology · 2021Article
- CCTs as new biomarkers for the prognosis of head and neck squamous cancer.Open medicine (Warsaw, Poland) · 2020Article
- The Molecular Chaperone CCT/TRiC: An Essential Component of Proteostasis and a Potential Modulator of Protein Aggregation.Frontiers in genetics · 2020Review
- Co-expression of CCT subunits hints at TRiC assembly.Cell stress & chaperones · 2019Article
- Overexpression of chaperonin containing T-complex polypeptide subunit zeta 2 (CCT6b) suppresses the functions of active fibroblasts in a rat model of joint contracture.Journal of orthopaedic surgery and research · 2019Article
- The role of the molecular chaperone CCT in protein folding and mediation of cytoskeleton-associated processes: implications for cancer cell biology.Cell stress & chaperones · 2019Review
- Identification of the PAK4 interactome reveals PAK4 phosphorylation of N-WASP and promotion of Arp2/3-dependent actin polymerization.Oncotarget · 2017Article
- The chaperonin TRiC forms an oligomeric complex in the malaria parasite cytosol.Cellular microbiology · 2017Article
- Chaperonin Containing TCP-1 Protein Level in Breast Cancer Cells Predicts Therapeutic Application of a Cytotoxic Peptide.Clinical cancer research : an official journal of the American Association for Cancer Research · 2016Article
- The molecular chaperone CCT modulates the activity of the actin filament severing and capping protein gelsolin in vitro.Cell stress & chaperones · 2016Article
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Correct protein folding is fundamental for maintaining protein homeostasis and avoiding the formation of potentially cytotoxic protein aggregates. Although some proteins appear to fold unaided, actin requires assistance from the oligomeric molecular chaperone CCT. Here we report an additional connection between CCT and actin by identifying one of the CCT subunits, CCTε, as a component of the myocardin-related cotranscription factor-A (MRTF-A)/serum response factor (SRF) pathway. The SRF pathway registers changes in G-actin levels, leading to the transcriptional up-regulation of a large number of genes after actin polymerization. These genes encode numerous actin-binding proteins as well as actin. We show that depletion of the CCTε subunit by siRNA enhances SRF signaling in cultured mammalian cells by an actin assembly-independent mechanism. Overexpression of CCTε in its monomeric form revealed that CCTε binds via its substrate-binding domain to the C-terminal region of MRTF-A and that CCTε is able to alter the nuclear accumulation of MRTF-A after stimulation by serum addition. Given that the levels of monomeric CCTε conversely reflect the levels of CCT oligomer, our results suggest that CCTε provides a connection between the actin-folding capacity of the cell and actin expression.
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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.