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Structure paper

TitleInteractions between TTYH2 and APOE facilitate endosomal lipid transfer.
Journal, issue, pagesNature, Year 2025
Publish dateJun 25, 2025
AuthorsAnastasiia Sukalskaia / Andreas Karner / Anna Pugnetti / Florian Weber / Birgit Plochberger / Raimund Dutzler /
PubMed AbstractThe Tweety homologues (TTYHs) constitute a family of eukaryotic membrane proteins that, on the basis of structural features, were recently proposed to contribute to lipid transfer between soluble ...The Tweety homologues (TTYHs) constitute a family of eukaryotic membrane proteins that, on the basis of structural features, were recently proposed to contribute to lipid transfer between soluble carriers and cellular membranes. However, in the absence of supporting data, this function was hypothetical. Here through pull-down of endogenous proteins, we identify APOE as the interaction partner of human TTYH2. Subcellular fractionation and immunocytochemistry assays showed that both proteins colocalize in endosomal compartments. Characterization of the specific interaction between APOE and TTYH2 through binding assays and structural studies enabled us to identify an epitope in an extended domain of TTYH2 that faces the endosomal lumen. Structures of complexes with APOE-containing lipoprotein particles revealed a binding mode that places lipids in a suitable position to facilitate their diffusion into the membrane. Moreover, in vitro studies revealed that lipid transfer is accelerated by TTYH2. Collectively, our findings indicate that TTYH2 has a role in the unloading of APOE-containing lipoproteins after they are endocytosed. These results define a new protein class that facilitates the extraction of lipids from and their insertion into cellular membranes. Although ubiquitous, this process could be of particular relevance in the brain, where APOE is involved in the transfer of lipids between astrocytes and neurons.
External linksNature / PubMed:40562935
MethodsEM (single particle)
Resolution2.74 - 13.64 Å
Structure data

51106

9g6x

EMDB-51106, PDB-9g6x:
Cryo-EM structure of TTYH2 in complex with sybody 1 in GDN
Method: EM (single particle) / Resolution: 3.7 Å

51108

9g71

EMDB-51108, PDB-9g71:
Cryo-EM structure of TTYH2 in complex with lipids in GDN
Method: EM (single particle) / Resolution: 2.74 Å

53249

9qnr

EMDB-53249, PDB-9qnr:
Cryo-EM structure of TTYH3 in GDN after incubation with ApoE, map2
Method: EM (single particle) / Resolution: 2.91 Å

EMDB-53271: ApoE lipoprotein disc, map3
Method: EM (single particle) / Resolution: 13.64 Å

EMDB-53272: ApoE lipoprotein disc, map1
Method: EM (single particle) / Resolution: 7.54 Å

EMDB-53273: ApoE lipoprotein disc, map2
Method: EM (single particle) / Resolution: 9.54 Å

EMDB-53290: TTYH2 in complex with sybody 2 in GDN
Method: EM (single particle) / Resolution: 4.26 Å

EMDB-53291: TTYH2 in complex with sybody 1 in cell-derived vesicles
Method: EM (single particle) / Resolution: 8.23 Å

EMDB-53292: TTYH2 in complex with lipidated ApoE in cell-derived vesicles
Method: EM (single particle) / Resolution: 10.71 Å

Chemicals

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

ChemComp-PLC:
DIUNDECYL PHOSPHATIDYL CHOLINE / phospholipid*YM

ChemComp-CLR:
CHOLESTEROL

ChemComp-CPL:
1-PALMITOYL-2-LINOLEOYL-SN-GLYCERO-3-PHOSPHOCHOLINE / phospholipid*YM

Source
  • vicugna pacos (alpaca)
  • homo sapiens (human)
  • synthetic construct (others)
KeywordsMEMBRANE PROTEIN / complex / sybody / nanobody / TTYH2 / lipid interactions

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