Structural and functional analysis of the role of the chaperonin CCT in mTOR complex assembly
β-propeller domains are an important class of folding substrates for the eukaryotic cytosolic chaperonin CTT. Here the authors find that CTT contributes to the folding and assembly of two β-propeller proteins from mTOR complexes, mLST8 and Raptor, and determine the 4.0 Å cryoEM structure of a human...
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| Format: | Article |
| Language: | English |
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Nature Publishing Group
2019-06-01
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| Series: | Nature Communications |
| Online Access: | https://doi.org/10.1038/s41467-019-10781-1 |
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doaj-23eeb432bf314670b0ab58f513d2d7e92021-05-11T12:26:19ZengNature Publishing GroupNature Communications2041-17232019-06-0110111410.1038/s41467-019-10781-1Structural and functional analysis of the role of the chaperonin CCT in mTOR complex assemblyJorge Cuéllar0W. Grant Ludlam1Nicole C. Tensmeyer2Takuma Aoba3Madhura Dhavale4César Santiago5M. Teresa Bueno-Carrasco6Michael J. Mann7Rebecca L. Plimpton8Aman Makaju9Sarah Franklin10Barry M. Willardson11José M. Valpuesta12Centro Nacional de Biotecnología, Campus de la Universidad Autónoma de MadridDepartment of Chemistry and Biochemistry, Brigham Young UniversityDepartment of Chemistry and Biochemistry, Brigham Young UniversityDepartment of Chemistry and Biochemistry, Brigham Young UniversityDepartment of Chemistry and Biochemistry, Brigham Young UniversityCentro Nacional de Biotecnología, Campus de la Universidad Autónoma de MadridCentro Nacional de Biotecnología, Campus de la Universidad Autónoma de MadridDepartment of Chemistry and Biochemistry, Brigham Young UniversityDepartment of Chemistry and Biochemistry, Brigham Young UniversityDepartment of Internal Medicine, Nora Eccles Harrison Cardiovascular Research and Training Institute, University of UtahDepartment of Internal Medicine, Nora Eccles Harrison Cardiovascular Research and Training Institute, University of UtahDepartment of Chemistry and Biochemistry, Brigham Young UniversityCentro Nacional de Biotecnología, Campus de la Universidad Autónoma de Madridβ-propeller domains are an important class of folding substrates for the eukaryotic cytosolic chaperonin CTT. Here the authors find that CTT contributes to the folding and assembly of two β-propeller proteins from mTOR complexes, mLST8 and Raptor, and determine the 4.0 Å cryoEM structure of a human mLST8-CCT intermediate that shows mLST8 in a near-native state.https://doi.org/10.1038/s41467-019-10781-1 |
| collection |
DOAJ |
| language |
English |
| format |
Article |
| sources |
DOAJ |
| author |
Jorge Cuéllar W. Grant Ludlam Nicole C. Tensmeyer Takuma Aoba Madhura Dhavale César Santiago M. Teresa Bueno-Carrasco Michael J. Mann Rebecca L. Plimpton Aman Makaju Sarah Franklin Barry M. Willardson José M. Valpuesta |
| spellingShingle |
Jorge Cuéllar W. Grant Ludlam Nicole C. Tensmeyer Takuma Aoba Madhura Dhavale César Santiago M. Teresa Bueno-Carrasco Michael J. Mann Rebecca L. Plimpton Aman Makaju Sarah Franklin Barry M. Willardson José M. Valpuesta Structural and functional analysis of the role of the chaperonin CCT in mTOR complex assembly Nature Communications |
| author_facet |
Jorge Cuéllar W. Grant Ludlam Nicole C. Tensmeyer Takuma Aoba Madhura Dhavale César Santiago M. Teresa Bueno-Carrasco Michael J. Mann Rebecca L. Plimpton Aman Makaju Sarah Franklin Barry M. Willardson José M. Valpuesta |
| author_sort |
Jorge Cuéllar |
| title |
Structural and functional analysis of the role of the chaperonin CCT in mTOR complex assembly |
| title_short |
Structural and functional analysis of the role of the chaperonin CCT in mTOR complex assembly |
| title_full |
Structural and functional analysis of the role of the chaperonin CCT in mTOR complex assembly |
| title_fullStr |
Structural and functional analysis of the role of the chaperonin CCT in mTOR complex assembly |
| title_full_unstemmed |
Structural and functional analysis of the role of the chaperonin CCT in mTOR complex assembly |
| title_sort |
structural and functional analysis of the role of the chaperonin cct in mtor complex assembly |
| publisher |
Nature Publishing Group |
| series |
Nature Communications |
| issn |
2041-1723 |
| publishDate |
2019-06-01 |
| description |
β-propeller domains are an important class of folding substrates for the eukaryotic cytosolic chaperonin CTT. Here the authors find that CTT contributes to the folding and assembly of two β-propeller proteins from mTOR complexes, mLST8 and Raptor, and determine the 4.0 Å cryoEM structure of a human mLST8-CCT intermediate that shows mLST8 in a near-native state. |
| url |
https://doi.org/10.1038/s41467-019-10781-1 |
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