Aquaglyceroporin 7 (AQP7) facilitates glycerol flux across the plasma membrane with a critical physiological role linked to metabolism, obesity, and associated diseases. Here, we present the single-particle cryo-EM structure of AQP7 determined at 2.55 Å resolution adopting two adhering tetramers, stabilized by extracellularly exposed loops, in a configuration like that of the well-characterized interaction of AQP0 tetramers. The central pore, in-between the four monomers, displays well-defined densities restricted by two leucine filters. Gas chromatography mass spectrometry (GC/MS) results show that the AQP7 sample contains glycerol 3-phosphate (Gro3P), which is compatible with the identified features in the central pore. AQP7 is shown to be highly expressed in human pancreatic α- and β- cells suggesting that the identified AQP7 octamer assembly, in addition to its function as glycerol channel, may serve as junction proteins within the endocrine pancreas.

Original languageEnglish
Article number600
Pages (from-to)1-12
JournalNature Communications
Publication statusPublished - 2023

Subject classification (UKÄ)

  • Cell Biology
  • Medical Biotechnology

Free keywords

  • Humans
  • Aquaglyceroporins
  • Aquaporins/metabolism
  • Glycerol/metabolism
  • Cryoelectron Microscopy
  • Islets of Langerhans/metabolism


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