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

Peng Huang, Raminta Venskutonytė, Rashmi B. Prasad, Hamidreza Ardalani, Sofia W. Maré, Xiao Fan, Ping Li, Peter Spégel, Nieng Yan, Pontus Gourdon, Isabella Artner and Karin Lindkvist-Petersson ()
Additional contact information
Peng Huang: Lund University
Raminta Venskutonytė: Lund University
Rashmi B. Prasad: Lund University Diabetes Centre, Clinical Research Center
Hamidreza Ardalani: Lund University
Sofia W. Maré: Lund University
Xiao Fan: Princeton University
Ping Li: Lund University
Peter Spégel: Lund University
Nieng Yan: Princeton University
Pontus Gourdon: Lund University
Isabella Artner: Lund University Diabetes Centre, Clinical Research Center
Karin Lindkvist-Petersson: Lund University

Nature Communications, 2023, vol. 14, issue 1, 1-12

Abstract: Abstract 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.

Date: 2023
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DOI: 10.1038/s41467-023-36272-y

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