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Illuminating cholesterol-mTORC1 signaling: LYCHOS in focus.
- Source :
-
Structure (London, England : 1993) [Structure] 2025 Feb 06; Vol. 33 (2), pp. 218-220. - Publication Year :
- 2025
-
Abstract
- In a recent issue of Nature, Bayly-Jones et al. <superscript>1</superscript> report the first cryoelectron microscopy (cryo-EM) structure of the lysosomal transmembrane protein LYCHOS, which mediates cholesterol sensing by mTORC1. LYCHOS forms a homodimer, with cholesterol engagement at the transporter-GPCR domain interface, coupled to auxin binding at the transporter-like domain, suggesting multi-domain coordination as critical for cholesterol sensing.<br />Competing Interests: Declaration of interests R.Z. is co-founder and SAB member of Frontier Medicines and SAB member of Nine Square Therapeutics.<br /> (Copyright © 2025 Elsevier Inc. All rights reserved.)
- Subjects :
- Humans
Animals
Multiprotein Complexes metabolism
Multiprotein Complexes chemistry
Monomeric GTP-Binding Proteins
Mechanistic Target of Rapamycin Complex 1 metabolism
Mechanistic Target of Rapamycin Complex 1 chemistry
Cholesterol metabolism
Cholesterol chemistry
Signal Transduction
Cryoelectron Microscopy
Subjects
Details
- Language :
- English
- ISSN :
- 1878-4186
- Volume :
- 33
- Issue :
- 2
- Database :
- MEDLINE
- Journal :
- Structure (London, England : 1993)
- Publication Type :
- Academic Journal
- Accession number :
- 39919712
- Full Text :
- https://doi.org/10.1016/j.str.2025.01.009