Cryo-EM structure supports a role of AQP7 as a junction protein.
Nat Commun
; 14(1): 600, 2023 02 03.
Article
en En
| MEDLINE
| ID: mdl-36737436
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 ß- 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.
Texto completo:
1
Banco de datos:
MEDLINE
Asunto principal:
Islotes Pancreáticos
/
Acuaporinas
/
Acuagliceroporinas
Límite:
Humans
Idioma:
En
Año:
2023
Tipo del documento:
Article