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TitleStructure and mechanism of human vesicular polyamine transporter.
Journal, issue, pagesNat Commun, Vol. 16, Issue 1, Page 4142, Year 2025
Publish dateMay 3, 2025
AuthorsYi Guo / Ge Yang / Haijiao Liu / Jin Chai / Jie Chen / John Shanklin / Qun Liu / Bin Liu / Min Lu /
PubMed AbstractPolyamines play essential roles in gene expression and modulate neuronal transmission in mammals. Vesicular polyamine transporters (VPAT) from the SLC18 family exploit the transmembrane H gradient to ...Polyamines play essential roles in gene expression and modulate neuronal transmission in mammals. Vesicular polyamine transporters (VPAT) from the SLC18 family exploit the transmembrane H gradient to translocate polyamines into secretory vesicles, enabling the quantal release of polyamine neuromodulators and underpinning learning and memory formation. Here, we report the cryo-electron microscopy structures of human VPAT in complex with spermine, spermidine, H, or tetrabenazine, elucidating discrete lumen-facing states of the antiporter and pivotal interactions between VPAT and its substrate or inhibitor. Leveraging structure-inspired mutagenesis studies and protein structure prediction, we deduce an unforeseen mechanism whereby the polyamine and H compete for multiple acidic protein residues both directly and indirectly, and rationalize how the antidopaminergic therapeutic tetrabenazine impedes vesicular transport of polyamines. This study unravels the mechanism of an H-coupled polyamine antiporter, reveals mechanistic diversity between VPAT and other SLC18 antiporters, and raises new prospects for combating human disorders of polyamine homeostasis.
External linksNat Commun / PubMed:40319071 / PubMed Central
MethodsEM (single particle)
Resolution3.3 - 3.97 Å
Structure data

46616

9d7u

EMDB-46616, PDB-9d7u:
The low pH structure
Method: EM (single particle) / Resolution: 3.97 Å

46617

9d7v

EMDB-46617, PDB-9d7v:
The spd-bound structure
Method: EM (single particle) / Resolution: 3.3 Å

46618

9d7w

EMDB-46618, PDB-9d7w:
The TBZ-bound structure
Method: EM (single particle) / Resolution: 3.3 Å

46619

9d7x

EMDB-46619, PDB-9d7x:
The spm-bound structure
Method: EM (single particle) / Resolution: 3.4 Å

Chemicals

ChemComp-HOH:
WATER

ChemComp-SPD:
SPERMIDINE

ChemComp-YHL:
tetrabenazine

ChemComp-SPM:
SPERMINE

Source
  • homo sapiens (human)
KeywordsMEMBRANE PROTEIN

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