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TitleStructural basis for lipid transport at membrane contact sites by the IST2-OSH6 complex.
Journal, issue, pagesNat Struct Mol Biol, Vol. 32, Issue 11, Page 2219-2230, Year 2025
Publish dateAug 27, 2025
AuthorsMelanie Arndt / Angela Schweri / Raimund Dutzler /
PubMed AbstractMembrane contact sites are hubs for interorganellar lipid transport within eukaryotic cells. As a principal tether bridging the endoplasmic reticulum (ER) and the plasma membrane in Saccharomyces ...Membrane contact sites are hubs for interorganellar lipid transport within eukaryotic cells. As a principal tether bridging the endoplasmic reticulum (ER) and the plasma membrane in Saccharomyces cerevisiae, the protein IST2 has a major role during lipid transport between both compartments. Here, we show a comprehensive investigation elucidating the structural and mechanistic properties of IST2 and its interaction with the soluble lipid transfer protein OSH6. The ER-embedded transmembrane domain of IST2 is homologous to the TMEM16 family and acts as a constitutively active lipid scramblase. The extended C terminus binds to the plasma membrane and the phosphatidylserine-phosphatidylinositol 4-phosphate exchanger OSH6. Through cellular growth assays and biochemical and structural studies, we characterized the interaction between both proteins and show that OSH6 remains associated with IST2 during lipid shuttling between membranes. These results highlight the role of the IST2-OSH6 complex in lipid trafficking and offer initial insights into the relevance of scramblases for carrier-like lipid transport mechanisms.
External linksNat Struct Mol Biol / PubMed:40866577 / PubMed Central
MethodsEM (single particle) / X-ray diffraction
Resolution1.84 - 4.2 Å
Structure data

52170

9hhe

EMDB-52170, PDB-9hhe:
Structure of the Ist2 TMEM16 homology domain in the detergent GDN
Method: EM (single particle) / Resolution: 2.84 Å

53200

9qja

EMDB-53200, PDB-9qja:
Structure of the transmembrane domain of full-length Ist2 at low resolution
Method: EM (single particle) / Resolution: 4.2 Å

53210

9qjt

EMDB-53210, PDB-9qjt:
Structure of the transmembrane domain of Ist2 in lipid nanodiscs (wide state)
Method: EM (single particle) / Resolution: 3.8 Å

53211

9qju

EMDB-53211, PDB-9qju:
Structure of the transmembrane domain of Ist2 in lipid nanodiscs (narrow state)
Method: EM (single particle) / Resolution: 3.34 Å

PDB-9hdh:
Structure of s.c.Osh6 in complex with Ist2 732-761 and POPS
Method: X-RAY DIFFRACTION / Resolution: 1.84 Å

PDB-9hdk:
Structure of s.c.Osh6 in complex with Ist2 732-756 and POPS
Method: X-RAY DIFFRACTION / Resolution: 1.93 Å

Chemicals

ChemComp-P5S:
O-[(R)-{[(2R)-2,3-bis(octadecanoyloxy)propyl]oxy}(hydroxy)phosphoryl]-L-serine

ChemComp-HOH:
WATER

Source
  • saccharomyces cerevisiae (brewer's yeast)
KeywordsLIPID TRANSPORT / Lipid transport protein / complex / Oxysterol-binding protein / membrane contact sites / MEMBRANE PROTEIN / TMEM16 proteins / lipid scramblase / tethering protein / scramblase / TMEM16 protein

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