Cryo-EM structure supports a role of AQP7 as a junction protein

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  • Peng Huang
  • Raminta Venskutonytė
  • Rashmi B Prasad
  • Hamidreza Ardalani
  • Sofia W de Maré
  • Xiao Fan
  • Ping Li
  • Peter Spégel
  • Nieng Yan
  • Gourdon, Pontus Emanuel
  • Isabella Artner
  • Karin Lindkvist-Petersson

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
JournalNature Communications
Issue number1
Number of pages12
Publication statusPublished - 2023
Externally publishedYes

    Research areas

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

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