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

Huang, Peng LU ; Venskutonytė, Raminta LU ; Prasad, Rashmi B LU ; Ardalani, Hamidreza LU ; de Maré, Sofia W LU ; Fan, Xiao ; Li, Ping LU ; Spégel, Peter LU ; Yan, Nieng and Gourdon, Pontus LU , et al. (2023) In Nature Communications 14. p.1-12
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... (More)

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.

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organization
publishing date
type
Contribution to journal
publication status
published
subject
keywords
Humans, Aquaglyceroporins, Aquaporins/metabolism, Glycerol/metabolism, Cryoelectron Microscopy, Islets of Langerhans/metabolism
in
Nature Communications
volume
14
article number
600
pages
1 - 12
publisher
Nature Publishing Group
external identifiers
  • pmid:36737436
  • scopus:85147458368
ISSN
2041-1723
DOI
10.1038/s41467-023-36272-y
language
English
LU publication?
yes
additional info
© 2023. The Author(s).
id
478c541d-90f8-43c7-818f-d1e7e52b4443
date added to LUP
2023-02-09 08:50:24
date last changed
2024-06-27 15:42:52
@article{478c541d-90f8-43c7-818f-d1e7e52b4443,
  abstract     = {{<p>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.</p>}},
  author       = {{Huang, Peng and Venskutonytė, Raminta and Prasad, Rashmi B and Ardalani, Hamidreza and de Maré, Sofia W and Fan, Xiao and Li, Ping and Spégel, Peter and Yan, Nieng and Gourdon, Pontus and Artner, Isabella and Lindkvist-Petersson, Karin}},
  issn         = {{2041-1723}},
  keywords     = {{Humans; Aquaglyceroporins; Aquaporins/metabolism; Glycerol/metabolism; Cryoelectron Microscopy; Islets of Langerhans/metabolism}},
  language     = {{eng}},
  pages        = {{1--12}},
  publisher    = {{Nature Publishing Group}},
  series       = {{Nature Communications}},
  title        = {{Cryo-EM structure supports a role of AQP7 as a junction protein}},
  url          = {{http://dx.doi.org/10.1038/s41467-023-36272-y}},
  doi          = {{10.1038/s41467-023-36272-y}},
  volume       = {{14}},
  year         = {{2023}},
}