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

Huang P, Venskutonytė R, Prasad RB, Ardalani H, de Maré SW, Fan X, Li P, Spégel P, Yan N, Gourdon P, Artner I, Lindkvist-Petersson K

Nat Commun 14 (1) 600 [2023-02-03; online 2023-02-03]

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.

Cryo-EM [Service]

PubMed 36737436

DOI 10.1038/s41467-023-36272-y

Crossref 10.1038/s41467-023-36272-y

pmc: PMC9898259
pii: 10.1038/s41467-023-36272-y

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