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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Autores principales: 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
Formato: article
Lenguaje:EN
Publicado: Nature Portfolio 2019
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Acceso en línea:https://doaj.org/article/23eeb432bf314670b0ab58f513d2d7e9
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Sumario: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.