Structural and functional analysis of the role of the chaperonin CCT in mTOR complex assembly

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

doi:10.1038/s41467-019-10781-1

Nature Communications (Jun 2019)

Structural and functional analysis of the role of the chaperonin CCT in mTOR complex assembly

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

Affiliations

Jorge Cuéllar: Centro Nacional de Biotecnología, Campus de la Universidad Autónoma de Madrid
W. Grant Ludlam: Department of Chemistry and Biochemistry, Brigham Young University
Nicole C. Tensmeyer: Department of Chemistry and Biochemistry, Brigham Young University
Takuma Aoba: Department of Chemistry and Biochemistry, Brigham Young University
Madhura Dhavale: Department of Chemistry and Biochemistry, Brigham Young University
César Santiago: Centro Nacional de Biotecnología, Campus de la Universidad Autónoma de Madrid
M. Teresa Bueno-Carrasco: Centro Nacional de Biotecnología, Campus de la Universidad Autónoma de Madrid
Michael J. Mann: Department of Chemistry and Biochemistry, Brigham Young University
Rebecca L. Plimpton: Department of Chemistry and Biochemistry, Brigham Young University
Aman Makaju: Department of Internal Medicine, Nora Eccles Harrison Cardiovascular Research and Training Institute, University of Utah
Sarah Franklin: Department of Internal Medicine, Nora Eccles Harrison Cardiovascular Research and Training Institute, University of Utah
Barry M. Willardson: Department of Chemistry and Biochemistry, Brigham Young University
José M. Valpuesta: Centro Nacional de Biotecnología, Campus de la Universidad Autónoma de Madrid

DOI: https://doi.org/10.1038/s41467-019-10781-1
Journal volume & issue: Vol. 10, no. 1
pp. 1 – 14

Abstract

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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.

Published in Nature Communications

ISSN: 2041-1723 (Online)
Publisher: Nature Portfolio
Country of publisher: United Kingdom
LCC subjects: Science
Website: https://www.nature.com/ncomms/

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