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TitleCryo-EM reveals cholesterol binding in the lysosomal GPCR-like protein LYCHOS.
Journal, issue, pagesNat Struct Mol Biol, Vol. 32, Issue 5, Page 896-904, Year 2025
Publish dateJan 17, 2025
AuthorsJie Zhao / Qingya Shen / Xihao Yong / Xin Li / Xiaowen Tian / Suyue Sun / Zheng Xu / Xiaoyu Zhang / Lu Zhang / Hao Yang / Zhenhua Shao / Haoxing Xu / Yiyang Jiang / Yan Zhang / Wei Yan /
PubMed AbstractCholesterol 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- ...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.
External linksNat Struct Mol Biol / PubMed:39824976
MethodsEM (single particle)
Resolution2.83 Å
Structure data

38930

8y56

EMDB-38930, PDB-8y56:
Cryo-EM reveals cholesterol binding in the lysosomal GPCR-like protein LYCHOS
Method: EM (single particle) / Resolution: 2.83 Å

Chemicals

ChemComp-NA:
Unknown entry

ChemComp-CLR:
CHOLESTEROL

ChemComp-DKB:
[(2R)-1-[2-azanylethoxy(oxidanyl)phosphoryl]oxy-3-hexadecanoyloxy-propan-2-yl] octadecanoate

ChemComp-HOH:
WATER

Source
  • homo sapiens (human)
KeywordsMEMBRANE PROTEIN / cholesterol / lysosome

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