Cryo-EM structure supports a role of AQP7 as a junction protein
(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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- author
- organization
-
- EXODIAB: Excellence of Diabetes Research in Sweden
- Medical Structural Biology (research group)
- LINXS - Institute of advanced Neutron and X-ray Science
- Translational Muscle Research (research group)
- Centre for Analysis and Synthesis
- Department of Experimental Medical Science
- Membrane Protein Structural Biology (research group)
- Endocrine Cell Differentiation and Function (research group)
- StemTherapy: National Initiative on Stem Cells for Regenerative Therapy
- LUCC: Lund University Cancer Centre
- publishing date
- 2023
- 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
- 2024-09-19 23:30:54
@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}}, }