IDEAS home Printed from https://ideas.repec.org/a/nat/natcom/v14y2023i1d10.1038_s41467-023-36272-y.html
   My bibliography  Save this article

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
    as

    Download full text from publisher

    File URL: https://www.nature.com/articles/s41467-023-36272-y
    File Function: Abstract
    Download Restriction: no
    File URL: https://libkey.io/10.1038/s41467-023-36272-y?utm_source=ideas
    LibKey link: if access is restricted and if your library uses this service, LibKey will redirect you to where you can use your library subscription to access this item
    ---><---

    References listed on IDEAS

    as
    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.
    Full references (including those not matched with items on IDEAS)

    Most related items

    These are the items that most often cite the same works as this one and are cited by the same works as this one.
    1. Yasunori Saitoh & Namiki Mitani-Ueno & Keisuke Saito & Kengo Matsuki & Sheng Huang & Lingli Yang & Naoki Yamaji & Hiroshi Ishikita & Jian-Ren Shen & Jian Feng Ma & Michihiro Suga, 2021. "Structural basis for high selectivity of a rice silicon channel Lsi1," Nature Communications, Nature, vol. 12(1), pages 1-14, December.
    2. John T. Petroff & Noah M. Dietzen & Ezry Santiago-McRae & Brett Deng & Maya S. Washington & Lawrence J. Chen & K. Trent Moreland & Zengqin Deng & Michael Rau & James A. J. Fitzpatrick & Peng Yuan & Th, 2022. "Open-channel structure of a pentameric ligand-gated ion channel reveals a mechanism of leaflet-specific phospholipid modulation," Nature Communications, Nature, vol. 13(1), pages 1-16, December.
    3. Zhenyu Yang & Chunyang Yu & Junjie Ding & Lihua Chen & Huiyu Liu & Yangzhi Ye & Pan Li & Jiaolong Chen & Kim Jiayi Wu & Qiang-Yu Zhu & Yu-Quan Zhao & Xiaoning Liu & Xiaodong Zhuang & Shaodong Zhang, 2021. "A class of organic cages featuring twin cavities," Nature Communications, Nature, vol. 12(1), pages 1-10, December.
    4. Dagimhiwat H. Legesse & Chen Fan & Jinfeng Teng & Yuxuan Zhuang & Rebecca J. Howard & Colleen M. Noviello & Erik Lindahl & Ryan E. Hibbs, 2023. "Structural insights into opposing actions of neurosteroids on GABAA receptors," Nature Communications, Nature, vol. 14(1), pages 1-13, December.
    5. Ke Tian Tan & Shanshan Tao & Ning Huang & Donglin Jiang, 2021. "Water cluster in hydrophobic crystalline porous covalent organic frameworks," Nature Communications, Nature, vol. 12(1), pages 1-10, December.
    6. Wanbiao Chen & Rongfeng Zou & Yi Mei & Jiawei Li & Yumi Xuan & Bing Cui & Junjie Zou & Juncheng Wang & Shaoquan Lin & Zhe Zhang & Chongyuan Wang, 2024. "Structural insights into drug transport by an aquaglyceroporin," Nature Communications, Nature, vol. 15(1), pages 1-10, December.
    7. Guangli Liu & Bin Zhou & Jinwei Liu & Huazhang Zhao, 2020. "The Bionic Water Channel of Ultra-Short, High Affinity Carbon Nanotubes with High Water Permeability and Proton Selectivity," Sustainability, MDPI, vol. 13(1), pages 1-13, December.
    8. Shingo Hiroki & Hikari Yoshitane & Hinako Mitsui & Hirofumi Sato & Chie Umatani & Shinji Kanda & Yoshitaka Fukada & Yuichi Iino, 2022. "Molecular encoding and synaptic decoding of context during salt chemotaxis in C. elegans," Nature Communications, Nature, vol. 13(1), pages 1-15, December.
    9. Lalita Saini & Siva Sankar Nemala & Aparna Rathi & Suvigya Kaushik & Gopinadhan Kalon, 2022. "Selective transport of water molecules through interlayer spaces in graphite," Nature Communications, Nature, vol. 13(1), pages 1-7, December.
    10. Si-Hua Liu & Jun-Hao Zhou & Chunrui Wu & Peng Zhang & Xingzhong Cao & Jian-Ke Sun, 2024. "Sub-8 nm networked cage nanofilm with tunable nanofluidic channels for adaptive sieving," Nature Communications, Nature, vol. 15(1), pages 1-10, December.

    More about this item

    Statistics

    Access and download statistics

    Corrections

    All material on this site has been provided by the respective publishers and authors. You can help correct errors and omissions. When requesting a correction, please mention this item's handle: RePEc:nat:natcom:v:14:y:2023:i:1:d:10.1038_s41467-023-36272-y. See general information about how to correct material in RePEc.

    If you have authored this item and are not yet registered with RePEc, we encourage you to do it here. This allows to link your profile to this item. It also allows you to accept potential citations to this item that we are uncertain about.

    If CitEc recognized a bibliographic reference but did not link an item in RePEc to it, you can help with this form .

    If you know of missing items citing this one, you can help us creating those links by adding the relevant references in the same way as above, for each refering item. If you are a registered author of this item, you may also want to check the "citations" tab in your RePEc Author Service profile, as there may be some citations waiting for confirmation.

    For technical questions regarding this item, or to correct its authors, title, abstract, bibliographic or download information, contact: Sonal Shukla or Springer Nature Abstracting and Indexing (email available below). General contact details of provider: http://www.nature.com .

    Please note that corrections may take a couple of weeks to filter through the various RePEc services.

    IDEAS is a RePEc service. RePEc uses bibliographic data supplied by the respective publishers.