Cryo-EM structure supports a role of AQP7 as a junction protein
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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.
Originalsprog | Engelsk |
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Artikelnummer | 600 |
Tidsskrift | Nature Communications |
Vol/bind | 14 |
Udgave nummer | 1 |
Antal sider | 12 |
ISSN | 2041-1723 |
DOI | |
Status | Udgivet - 2023 |
Eksternt udgivet | Ja |
Bibliografisk note
© 2023. The Author(s).
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