IDEAS home Printed from https://ideas.repec.org/a/nat/natcom/v13y2022i1d10.1038_s41467-022-33420-8.html
   My bibliography  Save this article

Structural basis for the activity regulation of a potassium channel AKT1 from Arabidopsis

Author

Listed:
  • Yaming Lu

    (China Agricultural University)

  • Miao Yu

    (China Agricultural University)

  • Yutian Jia

    (China Agricultural University)

  • Fan Yang

    (China Agricultural University)

  • Yanming Zhang

    (China Agricultural University)

  • Xia Xu

    (China Agricultural University)

  • Xiaomin Li

    (Tsinghua University)

  • Fan Yang

    (Tsinghua University)

  • Jianlin Lei

    (Tsinghua University)

  • Yi Wang

    (China Agricultural University)

  • Guanghui Yang

    (China Agricultural University)

Abstract

The voltage-gated potassium channel AKT1 is responsible for primary K+ uptake in Arabidopsis roots. AKT1 is functionally activated through phosphorylation and negatively regulated by a potassium channel α-subunit AtKC1. However, the molecular basis for the modulation mechanism remains unclear. Here we report the structures of AKT1, phosphorylated-AKT1, a constitutively-active variant, and AKT1-AtKC1 complex. AKT1 is assembled in 2-fold symmetry at the cytoplasmic domain. Such organization appears to sterically hinder the reorientation of C-linkers during ion permeation. Phosphorylated-AKT1 adopts an alternate 4-fold symmetric conformation at cytoplasmic domain, which indicates conformational changes associated with symmetry switch during channel activation. To corroborate this finding, we perform structure-guided mutagenesis to disrupt the dimeric interface and identify a constitutively-active variant Asp379Ala mediates K+ permeation independently of phosphorylation. This variant predominantly adopts a 4-fold symmetric conformation. Furthermore, the AKT1-AtKC1 complex assembles in 2-fold symmetry. Together, our work reveals structural insight into the regulatory mechanism for AKT1.

Suggested Citation

  • Yaming Lu & Miao Yu & Yutian Jia & Fan Yang & Yanming Zhang & Xia Xu & Xiaomin Li & Fan Yang & Jianlin Lei & Yi Wang & Guanghui Yang, 2022. "Structural basis for the activity regulation of a potassium channel AKT1 from Arabidopsis," Nature Communications, Nature, vol. 13(1), pages 1-11, December.
  • Handle: RePEc:nat:natcom:v:13:y:2022:i:1:d:10.1038_s41467-022-33420-8
    DOI: 10.1038/s41467-022-33420-8
    as

    Download full text from publisher

    File URL: https://www.nature.com/articles/s41467-022-33420-8
    File Function: Abstract
    Download Restriction: no

    File URL: https://libkey.io/10.1038/s41467-022-33420-8?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. Yoni Haitin & Anne E. Carlson & William N. Zagotta, 2013. "The structural mechanism of KCNH-channel regulation by the eag domain," Nature, Nature, vol. 501(7467), pages 444-448, September.
    2. Tinatin I. Brelidze & Anne E. Carlson & Banumathi Sankaran & William N. Zagotta, 2012. "Structure of the carboxy-terminal region of a KCNH channel," Nature, Nature, vol. 481(7382), pages 530-533, January.
    3. Michael David Clark & Gustavo F. Contreras & Rong Shen & Eduardo Perozo, 2020. "Electromechanical coupling in the hyperpolarization-activated K+ channel KAT1," Nature, Nature, vol. 583(7814), pages 145-149, July.
    Full references (including those not matched with items on IDEAS)

    Citations

    Citations are extracted by the CitEc Project, subscribe to its RSS feed for this item.
    as


    Cited by:

    1. Yuhang Wang & Chengcai Pan & Qihao Chen & Qing Xie & Yiwei Gao & Lingli He & Yue Li & Yanli Dong & Xingyu Jiang & Yan Zhao, 2023. "Architecture and autoinhibitory mechanism of the plasma membrane Na+/H+ antiporter SOS1 in Arabidopsis," Nature Communications, Nature, vol. 14(1), pages 1-12, December.

    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. Michael P. Andreas & Tobias W. Giessen, 2024. "The biosynthesis of the odorant 2-methylisoborneol is compartmentalized inside a protein shell," Nature Communications, Nature, vol. 15(1), pages 1-17, December.
    2. Verena Burtscher & Jonathan Mount & Jian Huang & John Cowgill & Yongchang Chang & Kathleen Bickel & Jianhan Chen & Peng Yuan & Baron Chanda, 2024. "Structural basis for hyperpolarization-dependent opening of human HCN1 channel," Nature Communications, Nature, vol. 15(1), pages 1-13, December.
    3. Lucas J. Handlin & Natalie L. Macchi & Nicolas L. A. Dumaire & Lyuba Salih & Erin N. Lessie & Kyle S. McCommis & Aubin Moutal & Gucan Dai, 2024. "Membrane lipid nanodomains modulate HCN pacemaker channels in nociceptor DRG neurons," Nature Communications, Nature, vol. 15(1), pages 1-20, December.
    4. Mingfeng Zhang & Yuanyue Shan & Duanqing Pei, 2023. "Mechanism underlying delayed rectifying in human voltage-mediated activation Eag2 channel," Nature Communications, Nature, vol. 14(1), pages 1-11, December.
    5. Ting-Feng Lin & Guey-Mei Jow & Hsin-Yu Fang & Ssu-Ju Fu & Hao-Han Wu & Mei-Miao Chiu & Chung-Jiuan Jeng, 2014. "The Eag Domain Regulates the Voltage-Dependent Inactivation of Rat Eag1 K+ Channels," PLOS ONE, Public Library of Science, vol. 9(10), pages 1-14, October.
    6. Carlos A. Z. Bassetto & Flavio Costa & Carlo Guardiani & Francisco Bezanilla & Alberto Giacomello, 2023. "Noncanonical electromechanical coupling paths in cardiac hERG potassium channel," Nature Communications, Nature, vol. 14(1), pages 1-11, 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:13:y:2022:i:1:d:10.1038_s41467-022-33420-8. 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.