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The interaction network of the chaperonin CCT
Open accessAbstract
The eukaryotic cytosolic chaperonin containing TCP-1 (CCT) has an important function in maintaining cellular homoeostasis by assisting the folding of many proteins, including the cytoskeletal components actin and tubulin. Yet the nature of the proteins and cellular pathways dependent on CCT function has not been established globally. Here, we use proteomic and genomic approaches to define CCT interaction networks involving 136 proteins/genes that include links to the nuclear pore complex, chromatin remodelling, and protein degradation. Our study also identifies a third eukaryotic cytoskeletal system connected with CCT: the septin ring complex, which is essential for cytokinesis. CCT interactions with septins are ATP dependent, and disrupting the function of the chaperonin in yeast leads to loss of CCT-septin interaction and aberrant septin ring assembly. Our results therefore provide a rich framework for understanding the function of CCT in several essential cellular processes, including epigenetics and cell division.
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“in S. cerevisiae all five septin subunits physically interact with the CCT complex”
From Functional Genomic Screening Reveals Core Modulators of Echinocandin Stress Responses in Candida albicans (2018) · cites this paper as Dekker et al., 2008
In the citing paper
“the CCT interaction network includes over 136 genes involved in the nuclear pore complex, chromatin remodeling, and protein degradation in S. cerevisiae (Dekker et al., 2008”
From Functional Genomic Screening Reveals Core Modulators of Echinocandin Stress Responses in Candida albicans (2018) · cites this paper as Dekker et al., 2008
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Functional organization of the yeast proteome by systematic analysis of protein complexes
Gavin, A., Böesche, M., Krause, R., Grandi, P., Marzioch, M., Bauer, A., Schultz, J., Rick, J. M., Michon, A., Cruciat, C., et al. (2002) · Nature · doi:10.1038/415141a · Cited by 4,729
Systematic identification of protein complexes in Saccharomyces cerevisiae by mass spectrometry
Ho, Y., Gruhler, A., Heilbut, A. M., Bader, G. D., Moore, L., Adams, S., Millar, A., Taylor, P. P., Bennett, K. L., Boutilier, K., et al. (2002) · Nature · doi:10.1038/415180a · Cited by 3,573
Global landscape of protein complexes in the yeast Saccharomyces cerevisiae
Krogan, N. J., Cagney, G., Yu, H., Zhong, G., Guo, X., Ignatchenko, A., Li, J., Pu, S., Datta, N., Tikuisis, A., et al. (2006) · Nature · doi:10.1038/nature04670 · Cited by 2,969
Proteome survey reveals modularity of the yeast cell machinery
Gavin, A., Aloy, P., Grandi, P., Krause, R., Böesche, M., Marzioch, M., Rau, C., Jensen, L. J., Bastuck, S., Dümpelfeld, B., et al. (2006) · Nature · doi:10.1038/nature04532 · Cited by 2,570
Systematic Genetic Analysis with Ordered Arrays of Yeast Deletion Mutants
Tong, A. H. Y., Evangelista, M., Parsons, A. B., Xu, H., Bader, G. D., Pagé, N., Robinson, M., Raghibizadeh, S., Hogue, C. W. V., Bussey, H., et al. (2001) · Science · doi:10.1126/science.1065810 · Cited by 2,138
Self-citationGlobal Mapping of the Yeast Genetic Interaction Network
Tong, A. H. Y., Lesage, G., Bader, G. D., Ding, H., Xu, H., Xin, X., Young, J., Berriz, G. F., Brost, R. L., Chang, M., et al. (2004) · Science · doi:10.1126/science.1091317 · Cited by 2,089
Folding of Newly Translated Proteins In Vivo: The Role of Molecular Chaperones
Frydman, J. (2001) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.70.1.603 · Cited by 1,184
Genome sequence and gene compaction of the eukaryote parasite Encephalitozoon cuniculi
Katinka, M., Duprat, S., Cornillot, E., Méténier, G., Thomarat, F., Prensier, G., Barbe, V., Peyretaillade, E., Brottier, P., Wincker, P., et al. (2001) · Nature · doi:10.1038/35106579 · Cited by 1,051
Global analysis of protein phosphorylation in yeast
Ptacek, J., Devgan, G., Michaud, G. A., Zhu, H., Zhu, X., Fasolo, J., Guo, H., Jona, G., Breitkreutz, A., Sopko, R., et al. (2005) · Nature · doi:10.1038/nature04187 · Cited by 984
Logic of the Yeast Metabolic Cycle: Temporal Compartmentalization of Cellular Processes
Tu, B. P., Kudlicki, A. S., Rowicka, M., & McKnight, S. L. (2005) · Science · doi:10.1126/science.1120499 · Cited by 889
Research works printed but not linked: 1
- Amberg DC, Burke DJ, Strathern JN (2005) Methods in Yeast Genetics. Cold Spring Harbour, New York, USA: Cold Spring Harbour Laboratory Press
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Zeng, C., Han, S., Pan, Y., Huang, Z., Zhang, B., & Zhang, B. (2024) · Clinical and Translational Medicine · doi:10.1002/ctm2.1592 · Cited by 25
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Hodeify, R. F., Nandakumar, M., Own, M., Courjaret, R. J., Graumann, J., Hubrack, S., & Machaca, K. (2018) · Science Advances · doi:10.1126/sciadv.aau1935 · Cited by 24
Saleh, A. M., Jacobson, K. R., Kinzer‐Ursem, T. L., & Calve, S. (2019) · Cellular and Molecular Bioengineering · doi:10.1007/s12195-019-00592-1 · Cited by 23
Gomez, A., Perez, J., Reyes, A., Durán, Á., & Roncero, C. (2009) · Eukaryotic Cell · doi:10.1128/ec.00153-09 · Cited by 23
Svanström, A., & Grantham, J. (2015) · Cell Stress and Chaperones · doi:10.1007/s12192-015-0637-5 · Cited by 22
Biniossek, M. L., Lechel, A., Rudolph, K. L., Martens, U. M., & Zimmermann, S. (2013) · Journal of Proteomics · doi:10.1016/j.jprot.2013.08.007 · Cited by 20
Controlling the cortical actin motor
Grantham, J., Lassing, I., & Karlsson, R. (2012) · PROTOPLASMA · doi:10.1007/s00709-012-0403-9 · Cited by 20
Monzo, K., Dowd, S. R., Minden, J. S., & Sisson, J. C. (2010) · Developmental Biology · doi:10.1016/j.ydbio.2010.01.028 · Cited by 18
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Roobol, A., Roobol, J., Carden, M. J., Smith, M. E., Hershey, J. W. B., Bastide, A., Knight, J. R. P., Willis, A. E., & Smales, C. M. (2013) · Biochemical Journal · doi:10.1042/bj20130979 · Cited by 19
Mosrin-Huaman, C., Honorine, R., & Rahmouni, A. R. (2009) · Molecular and Cellular Biology · doi:10.1128/mcb.00272-09 · Cited by 19
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Wang, Y., Uraki, R., Hwang, J., & Fikrig, E. (2020) · Viruses · doi:10.3390/v12050519 · Cited by 18
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Bregier, C., Krzemień‐Ojak, Ł., Włoga, D., Jerka‐Dziadosz, M., Joachimiak, E., Batko, K., Filipiuk, I., Smietanka, U., Gaertig, J., Fabczak, S., et al. (2013) · Journal of Cellular Physiology · doi:10.1002/jcp.24384 · Cited by 18
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Altschuler, G. M., Dekker, C., McCormack, E. A., Morris, E. P., Klug, D. R., & Willison, K. R. (2009) · FEBS Letters · doi:10.1016/j.febslet.2009.01.031 · Cited by 17
Rizzolo, K., & Houry, W. A. (2018) · Journal of Biological Chemistry · doi:10.1074/jbc.tm118.002805 · Cited by 17
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Akhmetova, K., Chesnokov, I. N., & Fedorova, S. A. (2018) · Molecular Biology · doi:10.1134/s0026893317050028 · Cited by 17
Colina, F., Carbó, M. T. D., Cañal, M. J., & Valledor, L. (2020) · Environmental and Experimental Botany · doi:10.1016/j.envexpbot.2020.104261 · Cited by 16
Chen, L., Zhang, Z., Qiu, J., Zhang, L., Luo, X., & Jang, J. H. (2014) · PLoS ONE · doi:10.1371/journal.pone.0096085 · Cited by 16
RetractedSystems analysis of the genetic interaction network of yeast molecular chaperones
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Chen, J.-S., Chang, L.-C., Wu, C., Yeung, L.-K., & Lin, Y. (2011) · Experimental Diabetes Research · doi:10.1155/2011/565647 · Cited by 15
Linnert, J., Knapp, B., Güler, B. E., Boldt, K., Ueffing, M., & Uwe Wolfrum, B. (2023) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2023.1199069 · Cited by 14
Slater, L. H., Hett, E. C., Clatworthy, A. E., Mark, K. G., & Hung, D. T. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1302257110 · Cited by 14
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Coumans, J. V. F., Moens, P., Poljak, A., Al‐Jaaidi, S., Pereg, L. L., & Raftery, M. J. (2010) · PROTEOMICS · doi:10.1002/pmic.200900301 · Cited by 13
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Fania, C., Anastasia, L., Vasso, M., Papini, N., Capitanio, D., Venerando, B., & Gelfi, C. (2009) · Electrophoresis · doi:10.1002/elps.200800800 · Cited by 12
Gamberi, T., Magherini, F., Fiaschi, T., Landini, I., Massai, L., Valocchia, E., Bianchi, L., Bini, L., Gabbiani, C., Nobili, S., et al. (2015) · Molecular BioSystems · doi:10.1039/c5mb00008d · Cited by 12
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Denney, A. S., Weems, A. D., & McMurray, M. A. (2021) · G3 Genes Genomes Genetics · doi:10.1093/g3journal/jkab230 · Cited by 11
Jossé, L., Smales, C. M., & Tuite, M. F. (2011) · Methods in molecular biology · doi:10.1007/978-1-61779-433-9_32 · Cited by 11
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Akhmetova, K., Chesnokov, I. N., & Fedorova, S. A. (2018) · Molecular Biology · doi:10.7868/s0026898418020015 · Cited by 12
Wang, S., Zhen, L., Li, X., Xu, F., Li, P., & Zhang, D. (2022) · Frontiers in Oncology · doi:10.3389/fonc.2022.857148 · Cited by 10
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Chatzileontiadou, D. S. M., Samiotaki, M. K., Alexopoulou, A. N., Cotsiki, M., Panayotou, G., Stamatiadi, M., Balatsos, N. A. A., Leonidas, D. D., & Kontou, M. (2017) · Journal of Proteome Research · doi:10.1021/acs.jproteome.7b00335 · Cited by 10
Gan, B. Q., & Tang, B. L. (2010) · Aging Cell · doi:10.1111/j.1474-9726.2010.00597.x · Cited by 10
Versatile substrate protein recognition mechanism of the eukaryotic chaperonin CCT
Jayasinghe, M., Tewmey, C., & Stan, G. (2009) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.22644 · Cited by 10
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Narayanan, A., Pullepu, D., Reddy, P. K., Uddin, W., & Kabir, M. A. (2016) · Current Microbiology · doi:10.1007/s00284-016-1024-x · Cited by 10
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Huang, R., Yu, M., Li, C., Zhan, Y., Xu, W., Xu, F., Ge, C., Li, W., & Yang, X. (2012) · PROTEOMICS - CLINICAL APPLICATIONS · doi:10.1002/prca.201200009 · Cited by 9
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Li, R., Dalheimer, N., Müller, M. B. D., & Hartl, F. U. (2026) · Nature · doi:10.1038/s41586-025-10073-3 · Cited by 11
Lattmann, E., Deng, T., & Hajnal, A. (2021) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2020.616051 · Cited by 7
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Hassell, D., Denney, A. S., Singer, E. R., Benson, A., Roth, A., Ceglowski, J. R., Steingesser, M. G., & McMurray, M. A. (2022) · Molecular Biology of the Cell · doi:10.1091/mbc.e22-07-0262 · Cited by 8
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Korobko, I., Nadler-Holly, M., & Horovitz, A. (2016) · Journal of Molecular Biology · doi:10.1016/j.jmb.2016.09.017 · Cited by 7
Bracher, A., & Hartl, F. U. (2013) · Encyclopedia of Biological Chemistry · doi:10.1016/b978-0-12-378630-2.00080-3 · Cited by 7
Qu, Z., Tian, Z., Wei, L., Wang, C., Kuang, L., Yan, J., Wang, F. Y., Wang, N., Tu, J., Wang, X., et al. (2025) · Plant Biotechnology Journal · doi:10.1111/pbi.70184 · Cited by 6
Functional Residues in Proteins
Ahmad, S., Wang, J., Ahmad, Z., & Ahmad, F. (2011) · Journal of Amino Acids · doi:10.4061/2011/606354 · Cited by 7
Akhmetova, K., Balasov, M., Svitin, A., Chesnokova, E., Renfrow, M. B., & Chesnokov, I. N. (2017) · G3 Genes Genomes Genetics · doi:10.1534/g3.117.300186 · Cited by 5
Yu, K., Gong, J., Huang, C., Huang, H., Ye, H., Wang, G., & Zeng, C. (2015) · Cell Stress and Chaperones · doi:10.1007/s12192-015-0612-1 · Cited by 5
Sarkar, S., Haldar, S., Hajra, S., & Sinha, P. (2010) · FEMS Yeast Research · doi:10.1111/j.1567-1364.2010.00655.x · Cited by 5
Tocci, N., Weil, T., Perenzoni, D., Moretto, M., Nürk, N. M., Madriñán, S., Ferrazza, R., Guella, G., & Mattivi, F. (2020) · Metabolites · doi:10.3390/metabo10110459 · Cited by 5
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Han, S., & Kim, P. M. (2010) · Molecular Systems Biology · doi:10.1038/msb.2009.101 · Cited by 5
Linnert, J., Kusuluri, D. K., Güler, B. E., Patnaik, S. R., May‐Simera, H., & Wolfrum, U. (2025) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2025.1520723 · Cited by 6
Wilkinson, M. D., Ferreira, J. L., Beeby, M., Baum, J., & Willison, K. R. (2022) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2022.1057232 · Cited by 4
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Mak, W. S., Tsang, T. M., Chan, T. Y., & Lukov, G. L. (2021) · Proteomes · doi:10.3390/proteomes9040040 · Cited by 4
Feng, L., Li, H., Du, Y. F., Zhang, T., Zhu, Y., Li, Z., Zhao, L., Wang, X., Wang, G., Zhou, L., et al. (2022) · Frontiers in Medicine · doi:10.3389/fmed.2022.861371 · Cited by 4
Özdemir, A., Machida, K., Imataka, H., & Catling, A. D. (2015) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2015.11.082 · Cited by 4
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Ghahe, S. S., Drabikowski, K., Stasiak, M., & Topf, U. (2024) · Journal of Molecular Biology · doi:10.1016/j.jmb.2024.168838 · Cited by 4
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Zetka, M., Pezeshki, A., Dawson, R., Veld, P. J. H. I. ’., Jones, S. J. M., & Silva, N. (2025) · Nature Communications · doi:10.1038/s41467-025-64403-0 · Cited by 3
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Noi, K., Kitamura, A., Hirai, H., Hongo, K., Sakurai, T., Mizobata, T., & Kawata, Y. (2012) · American Journal of Molecular Biology · doi:10.4236/ajmb.2012.23028 · Cited by 3
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Chen, W., Yu, J., He, M., Hou, X., & Zhao, C. (2025) · Fish & Shellfish Immunology · doi:10.1016/j.fsi.2025.110517 · Cited by 3
Polyglutamined expanded androgen receptor interacts with chaperonin CCT
Pongtepaditep, S., Limjindaporn, T., Lertrit, P., Srisawat, C., & Limwongse, C. (2012) · European Journal of Medical Genetics · doi:10.1016/j.ejmg.2012.06.013 · Cited by 3
Components of an ESCRT-independent nuclear envelope assembly pathway
Sydir, E. M., Farra, M. H., Whitford, A. L., Hinojosa, S., Kao, P.-Y., Paulo, J. A., Swarup, S., Lusk, C. P., Harper, J. W., Lee, I., et al. (2026) · The Journal of Cell Biology · doi:10.1083/jcb.202601189 · Cited by 2
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Meng, X., Wang, X., Zhu, X., Zhang, R., Zhang, Z., & Sun, Y. (2023) · Virology Journal · doi:10.1186/s12985-023-02200-1 · Cited by 2
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Septins: Cytoskeletal Filaments with Structural and Regulatory Functions
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Wang, L., Li, P., Zeng, P., Xie, D., Gao, M., Ma, L., Sohail, A., & Zeng, F. (2024) · PLoS ONE · doi:10.1371/journal.pone.0313597 · Cited by 1
Li, Z., Zhao, Q., Jiang, W., Song, Q., Zhou, X., Shi, X., Zhang, Q., wang, Y., Lin, Y., Yin, Y., et al. (2026) · Science Advances · doi:10.1126/sciadv.aef3048 · Cited by 1
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Córdoba-Beldad, C. M., & Grantham, J. (2025) · European Journal of Cell Biology · doi:10.1016/j.ejcb.2025.151506 · Cited by 1
Narayanan, A., & Kabir, M. A. (2021) · Gene Reports · doi:10.1016/j.genrep.2021.101280 · Cited by 1
Yusof, N. A., Wong, C., Murad, A. M. A., Bakar, F. D. A., Mahadi, N. M., Rahman, A. Y. A., Zainuddin, N., & Najimudin, M. N. M. (2019) · Polish Polar Research · doi:10.24425/ppr.2019.129674 · Cited by 1
Functional Genomic and Chemical Biology Analysis of Echinocandin Resistance in Candida albicans
Caplan, T. (2018) · TSpace (University of Toronto) · Cited by 1
Filopodome proteomics identifies CCT8 as a MYO10 interactor critical for filopodia functionsPreprint
Popović, A., Ball, N. J., Miihkinen, M., Joshi, O., Dibus, M., Ojalill, M., Pylvänäinen, J. W., Ivaska, J., Goult, B. T., & Jacquemet, G. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.64898/2025.12.03.691809 · Cited by 1
Probing yeast molecular systems biology by new proteomics strategies
Helbig, A. O. (2010) · Utrecht University Repository (Utrecht University)
The Chaperonin Containing TCP-1 : Interactions with the Mammalian Cytoskeleton
Brackley, K. I. (2010) · Gothenburg University Publications Electronic Archive (Gothenburg University)
Role of members of the phosducin gene family in protein translation and folding
Sono‐Koree, N. K. (2010) · ScholarsArchive (Brigham Young University)
Salahuddin, P. (2015) · Journal of Biochemistry and Molecular Biology Research
The role of SEPT2 on neuronal development
Kim, H. J. (2009) · Rutgers University Community Repository (Rutgers University) · doi:10.7282/t3tx3fk0
Kinetic Studies of Actin Folding by the Chaperonin CCT
Stuart, S. F. (2011) · doi:10.25560/9702
Marszalek, R. (2011) · Spiral (Imperial College London) · doi:10.25560/9682
Evolution of Multiple Chaperonins: Innovation of Evolutionary Capacitors
Fares, M. A. (2017) · Heat shock proteins · doi:10.1007/978-981-10-4651-3_10
Dunham, W. H. (2012) · TSpace (University of Toronto)
Proteomic and phenotypic approaches to assess nutritional physiology in Atlantic salmon
Nuez-Ortin, W. (2017) · UTAS Research Repository · doi:10.25959/23239721
Bukharaeva, E. A., & Khuzakhmetova, V. F. (2017) · Биологические мембраны Журнал мембранной и клеточной биологии · doi:10.7868/s0233475517060019
Young, R., Cavodeassi, F., Hawkins, T. A., Stickney, H. L., Schwarz, Q., Lawrence, L. M., Wierzbicki, C., Gestri, G., Ambrosio, E. M., Klosner, A., et al. (2018) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/377119
Meng, X., Zhu, X., Zhang, R., & Zhang, Z. (2021) · Research Square · doi:10.21203/rs.3.rs-560607/v1
Regulation of epithelial cell migration and macropinocytosis by septin GTPases
Dolat, L., & Spiliotis, E. T. (2016) · doi:10.17918/etd-6833
Metadata
- Authors
- Dekker, C., Stirling, P. C., McCormack, E. A., Filmore, H., Paul, A., Brost, R. L., Costanzo, M., Boone, C., Leroux, M. R., & Willison, K. R.
- Affiliations
- Institute of Cancer Research (GB)
- Simon Fraser University (CA)
- University of Toronto (CA)
- Venue
- The EMBO Journal
- Published
- 2008-05-29
- Volume
- 27
- Issue
- 13
- Pages
- 1827-1839
- ISSN
- 0261-4189 (ISSN-L)
- 1460-2075
- PMC
- PMC2486426
- OpenAlex
- W2039639602
- Cited by
- 220
- References
- 59
- Citations by year
- 2026: 9 · 2025: 8 · 2024: 10 · 2023: 2 · 2022: 7 · 2021: 9 · 2020: 9 · 2019: 12 · 2018: 18 · 2017: 13 · 2016: 10 · 2015: 15 · 2014: 10 · 2013: 13 · 2012: 15
- FWCI
- 8.22
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- Locations
- The EMBO Journal (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- Genome Canada
- Michael Smith Health Research BC
- Cancer Research UK
- Canadian Institutes of Health Research
- Natural Sciences and Engineering Research Council of Canada
- 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 › Ubiquitin and proteasome pathways
- Keywords
- chaperonin CCT, TCP1, protein folding, protein-protein interaction network, nuclear pore complex, chromatin remodeling, protein degradation, septins, cytokinesis, actin folding, tubulin folding, epigenetics, cell division, yeast
- MeSH terms
- Saccharomyces cerevisiae, Chaperonins, Genomics, Saccharomyces cerevisiae Proteins, Proteomics, Multiprotein Complexes, Cytokinesis, Chaperonin Containing TCP-1
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