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Cryo-EM reveals cholesterol binding in the lysosomal GPCR-like protein LYCHOS

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作者：
Zhao Jie[1,2] * ; Shen Qingya[3,4] * ; Yong Xihao[1,2] * ; Li Xin[5] ; Tian Xiaowen[1,2] ; Sun Suyue[1,2] ; Xu Zheng[1,2] ; Zhang Xiaoyu[1,2] ; Zhang Lu[5] ; Yang Hao[5] ; Shao Zhenhua[1,2] ; Xu Haoxing[6] ; Jiang Yiyang[7] ; Zhang Yan[3,4] ; Yan Wei[1] ;
机构： [1]Division of Nephrology and Kidney Research Institute, State Key Laboratory of Biotherapy, West China Hospital, Sichuan University, Chengdu, China. [2]Frontiers Medical Center, Tianfu Jincheng Laboratory, Chengdu, China. [3]Department of Pathology of Sir Run Shaw Hospital, Department of Pharmacology, and Liangzhu Laboratory, Zhejiang University School of Medicine, Hangzhou, China. [4]MOE Frontier Science Center for Brain Research and Brain-Machine Integration, Zhejiang University School of Medicine, Hangzhou, China. [5]NHC Key Lab of Transplant Engineering and Immunology, Regenerative Medicine Research Center, Institutes for Systems Genetics, Frontiers Science Center for Disease-Related Molecular Network, Metabolomics and Proteomics Technology Platform, West China Hospital, Sichuan University, Chengdu, China. [6]New Cornerstone Science Laboratory & Liangzhu Laboratory, the Second Affiliated Hospital & School of Basic Medical Sciences, Zhejiang University, Hangzhou, China. [7]Department of Hepatobiliary Surgery, Innovative Institute of Tumor Immunity and Medicine (ITIM), Anhui Province Key Laboratory of Tumor Immune Microenvironment and Immunotherapy, The First Affiliated Hospital of Anhui Medical University, Hefei, China.
出处：
DOI： 10.1038/s41594-024-01470-9
ISSN：

摘要：
Cholesterol plays a pivotal role in modulating the activity of mechanistic target of rapamycin complex 1 (mTOR1), thereby regulating cell growth and metabolic homeostasis. LYCHOS, a lysosome-localized G-protein-coupled receptor-like protein, emerges as a cholesterol sensor and is capable of transducing the cholesterol signal to affect the mTORC1 function. However, the precise mechanism by which LYCHOS recognizes cholesterol remains unknown. Here, using cryo-electron microscopy, we determined the three-dimensional structural architecture of LYCHOS in complex with cholesterol molecules, revealing a unique arrangement of two sequential structural domains. Through a comprehensive analysis of this structure, we elucidated the specific structural features of these two domains and their collaborative role in the process of cholesterol recognition by LYCHOS.© 2025. The Author(s), under exclusive licence to Springer Nature America, Inc.

基金：
This research was supported by the National Natural Science Foundation of China (32371288 to W.Y., 32200986 to J.Z.), the National Key R&D Program of China (2024YFA1107500 to Z.S.), National Natural Science Foundation of China (T2221004 to Z.S., 92353303 and 32141004 to Y.Z., 32000845 to Q.S., 82404716 to Z.X.), Science and Technology Department of Sichuan Province (2024ZDZX0055 to Z.S., 2024NSFJQ0052 to Z.S., 2024NSFSC1242 to J.Z., 25QNJJ2880 to Z.X.), 1.3.5 project for disciplines of excellence, West China Hospital, Sichuan University (ZYYC23022 to Z.S.), Frontiers Medical Center, Tianfu Jincheng Laboratory Foundation (TFJC2023010010 to Z.S.), the ‘Pioneer’ and ‘Leading Goose’ R&D Program of Zhejiang (2024C03147 to Y.Z.), the Ministry of Science and Technology (2019YFA0508800 to Y.Z.), the Key R&D Projects of Zhejiang Province (2021C03039 to Y.Z.), the Leading Innovative and Entrepreneur Team Introduction Program of Zhejiang (2020R01006 to Y.Z.), the National Key Research and Development Program of China (2022YFE0210100 to H.X.), the China Postdoctoral Science Foundation (BX20220219 to Z.X., 2022M712275 to J.Z.) and Post-Doctoral Research Project, West China Hospital, Sichuan University (2021HXBH064 to J.Z.). We thank the staff of Zhejiang University Cryo-EM Center for technical support. We thank the Tianfu Jincheng Laboratory Cryo-EM Center and the High Performance Computing (HPC) center. We thank the Sichuan University, West China Hospital of Metabolomics and Proteomics Technology Platform for mass spectrometric assay. This work used resources from the Duyu HPC Center, Sichuan University, and Big Data Platform at West China Hospital of Sichuan University (WCH-BDP).
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出版当年[2025]版：
无
最新[2023]版：
大类 | 1 区 生物学
小类 | 1 区 生化与分子生物学 1 区 生物物理 1 区 细胞生物学
第一作者：
第一作者机构： [1]Division of Nephrology and Kidney Research Institute, State Key Laboratory of Biotherapy, West China Hospital, Sichuan University, Chengdu, China. [2]Frontiers Medical Center, Tianfu Jincheng Laboratory, Chengdu, China.
共同第一作者：
通讯作者：
通讯机构： [1]Division of Nephrology and Kidney Research Institute, State Key Laboratory of Biotherapy, West China Hospital, Sichuan University, Chengdu, China. [2]Frontiers Medical Center, Tianfu Jincheng Laboratory, Chengdu, China. [3]Department of Pathology of Sir Run Shaw Hospital, Department of Pharmacology, and Liangzhu Laboratory, Zhejiang University School of Medicine, Hangzhou, China. [4]MOE Frontier Science Center for Brain Research and Brain-Machine Integration, Zhejiang University School of Medicine, Hangzhou, China.
推荐引用方式(GB/T 7714)：
Zhao Jie,Shen Qingya,Yong Xihao,et al.Cryo-EM reveals cholesterol binding in the lysosomal GPCR-like protein LYCHOS[J].Nature Structural & Molecular Biology.2025,doi:10.1038/s41594-024-01470-9.
APA：
Zhao Jie,Shen Qingya,Yong Xihao,Li Xin,Tian Xiaowen...&Yan Wei.(2025).Cryo-EM reveals cholesterol binding in the lysosomal GPCR-like protein LYCHOS.Nature Structural & Molecular Biology,,
MLA：
Zhao Jie,et al."Cryo-EM reveals cholesterol binding in the lysosomal GPCR-like protein LYCHOS".Nature Structural & Molecular Biology .(2025)

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