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Título: | Structural and functional analysis of the role of the chaperonin CCT in mTOR complex assembly |
Autor: | Cuéllar, Jorge; Ludlam, W. Grant; Tensmeyer, Nicole C.; Aoba, Takuma; Dhavale, Madhura; Santiago, César CSIC ORCID ; Bueno-Carrasco, M. Teresa; Mann, Michael J.; Plimpton, Rebecca L.; Makaju, Aman; Franklin, Sarah; Willardson, Barry M.; Valpuesta, José M. CSIC ORCID | Palabras clave: | Chaperones Cryoelectron microscopy Kinases |
Fecha de publicación: | 2019 | Editor: | Springer Nature | Citación: | Nature Communications 10: 2865 (2019) | Resumen: | The mechanistic target of rapamycin (mTOR) kinase forms two multi-protein signaling complexes, mTORC1 and mTORC2, which are master regulators of cell growth, metabolism, survival and autophagy. Two of the subunits of these complexes are mLST8 and Raptor, β-propeller proteins that stabilize the mTOR kinase and recruit substrates, respectively. Here we report that the eukaryotic chaperonin CCT plays a key role in mTORC assembly and signaling by folding both mLST8 and Raptor. A high resolution (4.0 Å) cryo-EM structure of the human mLST8-CCT intermediate isolated directly from cells shows mLST8 in a near-native state bound to CCT deep within the folding chamber between the two CCT rings, and interacting mainly with the disordered N- and C-termini of specific CCT subunits of both rings. These findings describe a unique function of CCT in mTORC assembly and a distinct binding site in CCT for mLST8, far from those found for similar β-propeller proteins. | Versión del editor: | http://dx.doi.org/10.1038/s41467-019-10781-1 | URI: | http://hdl.handle.net/10261/241242 | DOI: | 10.1038/s41467-019-10781-1 | Identificadores: | doi: 10.1038/s41467-019-10781-1 e-issn: 2041-1723 |
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