ArticlePloS one2010
CCTalpha and CCTdelta chaperonin subunits are essential and required for cilia assembly and maintenance in Tetrahymena.
Article in PloS one, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed, 33 citations in OpenAlex.
- The Molecular Chaperone TCP1 Affects Carcinogenicity and Is a Potential Therapeutic Target for Acute Myeloid Leukemia.Pharmaceutics · 2025Article
- An amino acid-resolution interactome for motile cilia identifies the structure and function of ciliopathy protein complexes.Developmental cell · 2025Article
- Peptide Fraction fromAntioxidants (Basel, Switzerland) · 2025Article
- Identification and bioinformatics analysis of cilia-associated gene families inFrontiers in microbiology · 2025Article
- Article
- Usher syndrome proteins ADGRV1 (USH2C) and CIB2 (USH1J) interact and share a common interactome containing TRiC/CCT-BBS chaperonins.Frontiers in cell and developmental biology · 2023Article
- Spatial constraints on chromosomes are instrumental to meiotic pairing.Journal of cell science · 2020Article
- Review
- Bardet-Biedl Syndrome as a Chaperonopathy: Dissecting the Major Role of Chaperonin-Like BBS Proteins (BBS6-BBS10-BBS12).Frontiers in molecular biosciences · 2017Review
- Article
- Essential role of the chaperonin CCT in rod outer segment biogenesis.Investigative ophthalmology & visual science · 2014Article
- The nucleotide-binding proteins Nubp1 and Nubp2 are negative regulators of ciliogenesis.Cellular and molecular life sciences : CMLS · 2014Article
- Proteomic analysis of apoptotic and oncotic pancreatic acinar AR42J cells treated with caerulein.Molecular and cellular biochemistry · 2013Article
- DYX1C1 is required for axonemal dynein assembly and ciliary motility.Nature genetics · 2013Article
- Ancient Origin of Chaperonin Gene Paralogs Involved in Ciliopathies.Journal of phylogenetics & evolutionary biology · 2013Article
Corrections and comments
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Authors and funding
5 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
backgroundThe eukaryotic cytosolic chaperonin CCT is a hetero-oligomeric complex formed by two rings connected back-to-back, each composed of eight distinct subunits (CCTalpha to CCTzeta). CCT complex mediates the folding, of a wide range of newly synthesised proteins including tubulin (alpha, beta and gamma) and actin, as quantitatively major substrates. METHODOLOGY/PRINCIPAL
findingsWe disrupted the genes encoding CCTalpha and CCTdelta subunits in the ciliate Tetrahymena. Cells lacking the zygotic expression of either CCTalpha or CCTdelta showed a loss of cell body microtubules, failed to assemble new cilia and died within 2 cell cycles. We also show that loss of CCT subunit activity leads to axoneme shortening and splaying of tips of axonemal microtubules. An epitope-tagged CCTalpha rescued the gene knockout phenotype and localized primarily to the tips of cilia. A mutation in CCTalpha, G346E, at a residue also present in the related protein implicated in the Bardet Biedel Syndrome, BBS6, also caused defects in cilia and impaired CCTalpha localization in cilia. CONCLUSIONS/SIGNIFICANCE: Our results demonstrate that the CCT subunits are essential and required for ciliary assembly and maintenance of axoneme structure, especially at the tips of cilia.
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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.