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-Structure paper
タイトル | Structural and functional analysis of the role of the chaperonin CCT in mTOR complex assembly. |
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ジャーナル・号・ページ | Nat Commun, Vol. 10, Issue 1, Page 2865, Year 2019 |
掲載日 | 2019年6月28日 |
![]() | 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 / ![]() ![]() |
PubMed 要旨 | 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 ...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. |
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手法 | EM (単粒子) |
解像度 | 3.97 - 7.5 Å |
構造データ | ![]() EMDB-4503: |
化合物 | ![]() ChemComp-ADP: |
由来 |
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![]() | CHAPERONE / CCT / folding / WD40 / mLST8 |