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Structure paper

TitleLYCHOS is a human hybrid of a plant-like PIN transporter and a GPCR.
Journal, issue, pagesNature, Vol. 634, Issue 8036, Page 1238-1244, Year 2024
Publish dateOct 2, 2024
AuthorsCharles Bayly-Jones / Christopher J Lupton / Alastair C Keen / Shuqi Dong / Chantel Mastos / Wentong Luo / Chunyi Qian / Gareth D Jones / Hari Venugopal / Yong-Gang Chang / Ronald J Clarke / Michelle L Halls / Andrew M Ellisdon /
PubMed AbstractLysosomes have crucial roles in regulating eukaryotic metabolism and cell growth by acting as signalling platforms to sense and respond to changes in nutrient and energy availability. LYCHOS (GPR155) ...Lysosomes have crucial roles in regulating eukaryotic metabolism and cell growth by acting as signalling platforms to sense and respond to changes in nutrient and energy availability. LYCHOS (GPR155) is a lysosomal transmembrane protein that functions as a cholesterol sensor, facilitating the cholesterol-dependent activation of the master protein kinase mechanistic target of rapamycin complex 1 (mTORC1). However, the structural basis of LYCHOS assembly and activity remains unclear. Here we determine several high-resolution cryo-electron microscopy structures of human LYCHOS, revealing a homodimeric transmembrane assembly of a transporter-like domain fused to a G-protein-coupled receptor (GPCR) domain. The class B2-like GPCR domain is captured in the apo state and packs against the surface of the transporter-like domain, providing an unusual example of a GPCR as a domain in a larger transmembrane assembly. Cholesterol sensing is mediated by a conserved cholesterol-binding motif, positioned between the GPCR and transporter domains. We reveal that the LYCHOS transporter-like domain is an orthologue of the plant PIN-FORMED (PIN) auxin transporter family, and has greater structural similarity to plant auxin transporters than to known human transporters. Activity assays support a model in which the LYCHOS transporter and GPCR domains coordinate to sense cholesterol and regulate mTORC1 activation.
External linksNature / PubMed:39358511 / PubMed Central
MethodsEM (single particle)
Resolution2.4 - 3.0 Å
Structure data

41912

8u54

EMDB-41912, PDB-8u54:
The mTORC1 cholesterol sensor LYCHOS (GPR155)
Method: EM (single particle) / Resolution: 2.65 Å

41913

8u56

EMDB-41913, PDB-8u56:
The mTORC1 cholesterol sensor LYCHOS (GPR155)
Method: EM (single particle) / Resolution: 2.75 Å

41914

8u58

EMDB-41914, PDB-8u58:
The mTORC1 cholesterol sensor LYCHOS (GPR155) with tryptophan
Method: EM (single particle) / Resolution: 2.45 Å

41916

8u5c

EMDB-41916, PDB-8u5c:
The mTORC1 cholesterol sensor LYCHOS (GPR155) with cholesterol
Method: EM (single particle) / Resolution: 2.68 Å

41929

8u5n

EMDB-41929, PDB-8u5n:
The mTORC1 cholesterol sensor LYCHOS (GPR155) - monomer with auxin
Method: EM (single particle) / Resolution: 3.0 Å

41930

8u5q

EMDB-41930, PDB-8u5q:
The mTORC1 cholesterol sensor LYCHOS (GPR155) - dimer with auxin
Method: EM (single particle) / Resolution: 2.4 Å

41934

8u5v

EMDB-41934, PDB-8u5v:
The mTORC1 cholesterol sensor LYCHOS (GPR155) - auxin bound, closed state
Method: EM (single particle) / Resolution: 2.77 Å

41935

8u5x

EMDB-41935, PDB-8u5x:
The mTORC1 cholesterol sensor LYCHOS (GPR155) - auxin bound, open state
Method: EM (single particle) / Resolution: 2.79 Å

Chemicals

ChemComp-NAG:
2-acetamido-2-deoxy-beta-D-glucopyranose

ChemComp-LMN:
Lauryl Maltose Neopentyl Glycol / detergent*YM

ChemComp-Y01:
CHOLESTEROL HEMISUCCINATE

ChemComp-IAC:
1H-INDOL-3-YLACETIC ACID / hormone*YM

Source
  • homo sapiens (human)
KeywordsMEMBRANE PROTEIN / PIN-FORMED / GPCR / Cholesterol / auxin / transporter / cell-growth / mTORC1 / cancer

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