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

Author

Listed:
  • Peng Huang

    (Lund University)

  • Raminta Venskutonytė

    (Lund University
    LINXS—Lund Institute of Advanced Neutron and X-ray Science)

  • Rashmi B. Prasad

    (Lund University Diabetes Centre, Clinical Research Center)

  • Hamidreza Ardalani

    (Lund University)

  • Sofia W. Maré

    (Lund University)

  • Xiao Fan

    (Princeton University)

  • Ping Li

    (Lund University)

  • Peter Spégel

    (Lund University)

  • Nieng Yan

    (Princeton University)

  • Pontus Gourdon

    (Lund University)

  • Isabella Artner

    (Lund University Diabetes Centre, Clinical Research Center)

  • Karin Lindkvist-Petersson

    (Lund University
    LINXS—Lund Institute of Advanced Neutron and X-ray Science)

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 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.

Suggested Citation

  • Peng Huang & Raminta Venskutonytė & Rashmi B. Prasad & Hamidreza Ardalani & Sofia W. Maré & Xiao Fan & Ping Li & Peter Spégel & Nieng Yan & Pontus Gourdon & Isabella Artner & Karin Lindkvist-Petersso, 2023. "Cryo-EM structure supports a role of AQP7 as a junction protein," Nature Communications, Nature, vol. 14(1), pages 1-12, December.
    • Handle: RePEc:nat:natcom:v:14:y:2023:i:1:d:10.1038_s41467-023-36272-y
    DOI: 10.1038/s41467-023-36272-y
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    References listed on IDEAS

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    1. Kazuyoshi Murata & Kaoru Mitsuoka & Teruhisa Hirai & Thomas Walz & Peter Agre & J. Bernard Heymann & Andreas Engel & Yoshinori Fujiyoshi, 2000. "Structural determinants of water permeation through aquaporin-1," Nature, Nature, vol. 407(6804), pages 599-605, October.
    2. Haixin Sui & Bong-Gyoon Han & John K. Lee & Peter Walian & Bing K. Jap, 2001. "Structural basis of water-specific transport through the AQP1 water channel," Nature, Nature, vol. 414(6866), pages 872-878, December.
    3. Thorsten Althoff & Ryan E. Hibbs & Surajit Banerjee & Eric Gouaux, 2014. "X-ray structures of GluCl in apo states reveal a gating mechanism of Cys-loop receptors," Nature, Nature, vol. 512(7514), pages 333-337, August.
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