ArticleCell stress & chaperones2011
Interactions between the actin filament capping and severing protein gelsolin and the molecular chaperone CCT: evidence for nonclassical substrate interactions.
Article in Cell stress & chaperones, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
What it found
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Who cites it
14 citing papers in PubMed, 28 citations in OpenAlex.
- TRiC/CCT chaperonin governs RNA polymerase II activity in the nucleus to support RNA homeostasis.Molecular cell · 2026Article
- Loss of the E3 ubiquitin ligase TRIM67 alters the post-synaptic density proteome.bioRxiv : the preprint server for biology · 2024Article
- Loss of the E3 ubiquitin ligase TRIM67 alters the post-synaptic density proteome.microPublication biology · 2024Article
- CCT6A knockdown suppresses osteosarcoma cell growth and Akt pathway activation in vitro.PloS one · 2022Article
- The TRiCky Business of Protein Folding in Health and Disease.Frontiers in cell and developmental biology · 2022Review
- Proteomic Changes Associated With Sperm Fertilizing Ability in Meat-Type Roosters.Frontiers in cell and developmental biology · 2021Article
- Article
- The Molecular Chaperone CCT/TRiC: An Essential Component of Proteostasis and a Potential Modulator of Protein Aggregation.Frontiers in genetics · 2020Review
- Suppression of CCT3 inhibits the proliferation and migration in breast cancer cells.Cancer cell international · 2020Article
- 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
- The molecular chaperone CCT modulates the activity of the actin filament severing and capping protein gelsolin in vitro.Cell stress & chaperones · 2016Article
- A novel function of the monomeric CCTε subunit connects the serum response factor pathway to chaperone-mediated actin folding.Molecular biology of the cell · 2015Article
- Controlling the cortical actin motor.Protoplasma · 2012Review
- Management of cytoskeleton architecture by molecular chaperones and immunophilins.Cellular signalling · 2011Review
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
CCT is a member of the chaperonin family of molecular chaperones and consists of eight distinct subunit species which occupy fixed positions within the chaperonin rings. The activity of CCT is closely linked to the integrity of the cytoskeleton as newly synthesized actin and tubulin monomers are dependent upon CCT to reach their native conformations. Furthermore, an additional role for CCT involving interactions with assembling/assembled microfilaments and microtubules is emerging. CCT is also known to interact with other proteins, only some of which will be genuine folding substrates. Here, we identify the actin filament remodeling protein gelsolin as a CCT-binding partner, and although it does not behave as a classical folding substrate, gelsolin binds to CCT with a degree of specificity. In cultured cells, the levels of CCT monomers affect levels of gelsolin, suggesting an additional link between CCT and the actin cytoskeleton that is mediated via the actin filament severing and capping protein gelsolin.
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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.