The t-complex polypeptide 1 complex is a chaperonin for tubulin and actin in vivo
Open accessAbstract
A role in folding newly translated cytoskeletal proteins in the cytosol of eukaryotes has been proposed for t-complex polypeptide 1 (TCP1). In this study, we investigated tubulin and actin biogenesis in Chinese hamster ovary (CHO) cells. When extracts of pulse-labeled cells were analyzed by anion-exchange and size-exclusion chromatography, newly synthesized alpha-tubulin, beta-tubulin, and actin were observed to enter a large molecular mass complex (approximately 900 kDa). These proteins were released from this complex capable, in the case of tubulin, of forming heterodimers. The large molecular mass complexes coeluted with TCP1 and could be immunoprecipitated by using an anti-TCP1 antibody. These findings demonstrate that there is a cytosolic pathway for folding tubulin and actin in vivo that involves the TCP1 complex.
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Cct8 is one of eight protein subunits of the CCT complex, which plays a role in the folding and assembly of cytoskeletal proteins.
“Cct8 is one of eight protein subunits of the CCT complex, which plays a role in the folding and assembly of cytoskeletal proteins”
From Functional Genomic Screening Reveals Core Modulators of Echinocandin Stress Responses in Candida albicans (2018) · cites this paper as Sternlicht et al., 1993
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- Authors
- Sternlicht, H., Farr, G. W., Sternlicht, M. L., Driscoll, J. K., Willison, K., & Yaffe, M. B.
- Affiliations
- Case Western Reserve University (US)
- Venue
- Proceedings of the National Academy of Sciences
- Publisher
- National Academy of Sciences
- Published
- 1993-10-15
- Volume
- 90
- Issue
- 20
- Pages
- 9422-9426
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- PMC
- PMC47580
- OpenAlex
- W2046006262
- Cited by
- 341
- References
- 27
- Citations by year
- 2026: 5 · 2025: 9 · 2024: 8 · 2023: 3 · 2022: 18 · 2021: 16 · 2020: 12 · 2019: 10 · 2018: 14 · 2017: 10 · 2016: 8 · 2015: 12 · 2014: 14 · 2013: 10 · 2012: 7
- FWCI
- 5.41
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Proceedings of the National Academy of Sciences (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- American Cancer Society
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Heat shock proteins research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Microtubule and mitosis dynamics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
- Keywords
- TCP1, chaperonin, tubulin, actin, protein folding, cytoskeletal proteins, alpha-tubulin, beta-tubulin, heterodimer formation, CHO cells
- MeSH terms
- Actins, Animals, Cricetinae, Precipitin Tests, Protein Binding, Protein Conformation, Proteins, Tubulin, Electrophoresis, Gel, Two-Dimensional, CHO Cells, Chaperonins, Macromolecular Substances, Chaperonin Containing TCP-1
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