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...
Main Authors: | 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 |
---|---|
Format: | Article |
Language: | English |
Published: |
Nature Publishing Group
2019-06-01
|
Series: | Nature Communications |
Online Access: | https://doi.org/10.1038/s41467-019-10781-1 |
Similar Items
-
Role of Molecular Chaperonin CCT and Its Co-Chaperone PhLP1 in the Assembly of mTOR Complexes
by: Dhavale, Madhura Vinayak
Published: (2017) -
Folding for the Immune Synapse: CCT Chaperonin and the Cytoskeleton
by: Noa Beatriz Martín-Cófreces, et al.
Published: (2021-04-01) -
Studies on the eukaryotic chaperonin CCT
by: King, Mikayala D. A.
Published: (2003) -
Kinetic studies of actin folding by the chaperonin CCT
by: Stuart, Sarah Frances
Published: (2012) -
Assisted protein folding at low temperature: evolutionary adaptation of the Antarctic fish chaperonin CCT and its client proteins
by: Jorge Cuellar, et al.
Published: (2014-03-01)