IDEAS home Printed from https://ideas.repec.org/a/nat/natcom/v14y2023i1d10.1038_s41467-023-35915-4.html
   My bibliography  Save this article

Insights into the mechanism of phospholipid hydrolysis by plant non-specific phospholipase C

Author

Listed:
  • Ruyi Fan

    (Huazhong Agricultural University
    Chinese Academy of Agricultural Sciences)

  • Fen Zhao

    (Huazhong Agricultural University)

  • Zhou Gong

    (Chinese Academy of Sciences)

  • Yanke Chen

    (Chinese Academy of Sciences)

  • Bao Yang

    (Huazhong Agricultural University)

  • Chen Zhou

    (Huazhong Agricultural University)

  • Jie Zhang

    (Huazhong Agricultural University)

  • Zhangmeng Du

    (Huazhong Agricultural University)

  • Xuemin Wang

    (University of Missouri
    Donald Danforth Plant Science Center)

  • Ping Yin

    (Huazhong Agricultural University)

  • Liang Guo

    (Huazhong Agricultural University)

  • Zhu Liu

    (Huazhong Agricultural University
    Chinese Academy of Agricultural Sciences)

Abstract

Non-specific phospholipase C (NPC) hydrolyzes major membrane phospholipids to release diacylglycerol (DAG), a potent lipid-derived messenger regulating cell functions. Despite extensive studies on NPCs reveal their fundamental roles in plant growth and development, the mechanistic understanding of phospholipid-hydrolyzing by NPCs, remains largely unknown. Here we report the crystal structure of Arabidopsis NPC4 at a resolution of 2.1 Å. NPC4 is divided into a phosphoesterase domain (PD) and a C-terminal domain (CTD), and is structurally distinct from other characterized phospholipases. The previously uncharacterized CTD is indispensable for the full activity of NPC4. Mechanistically, CTD contributes NPC4 activity mainly via CTDα1-PD interaction, which ultimately stabilizes the catalytic pocket in PD. Together with a series of structure-guided biochemical studies, our work elucidates the structural basis and provides molecular mechanism of phospholipid hydrolysis by NPC4, and adds new insights into the members of phospholipase family.

Suggested Citation

  • Ruyi Fan & Fen Zhao & Zhou Gong & Yanke Chen & Bao Yang & Chen Zhou & Jie Zhang & Zhangmeng Du & Xuemin Wang & Ping Yin & Liang Guo & Zhu Liu, 2023. "Insights into the mechanism of phospholipid hydrolysis by plant non-specific phospholipase C," Nature Communications, Nature, vol. 14(1), pages 1-11, December.
  • Handle: RePEc:nat:natcom:v:14:y:2023:i:1:d:10.1038_s41467-023-35915-4
    DOI: 10.1038/s41467-023-35915-4
    as

    Download full text from publisher

    File URL: https://www.nature.com/articles/s41467-023-35915-4
    File Function: Abstract
    Download Restriction: no

    File URL: https://libkey.io/10.1038/s41467-023-35915-4?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. Valerie I. Khayyo & Reece M. Hoffmann & Huan Wang & Justin A. Bell & John E. Burke & Karen Reue & Michael V. Airola, 2020. "Crystal structure of a lipin/Pah phosphatidic acid phosphatase," Nature Communications, Nature, vol. 11(1), pages 1-11, December.
    2. Jay Xiaojun Tan & Toren Finkel, 2022. "A phosphoinositide signalling pathway mediates rapid lysosomal repair," Nature, Nature, vol. 609(7928), pages 815-821, September.
    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. Tomoki Naito & Haoning Yang & Dylan Hong Zheng Koh & Divyanshu Mahajan & Lei Lu & Yasunori Saheki, 2023. "Regulation of cellular cholesterol distribution via non-vesicular lipid transport at ER-Golgi contact sites," Nature Communications, Nature, vol. 14(1), pages 1-25, December.
    2. Nivea Pereira de Sa & Adam Taouil & Jinwoo Kim & Timothy Clement & Reece M. Hoffmann & John E. Burke & Robert C. Rizzo & Iwao Ojima & Maurizio Del Poeta & Michael V. Airola, 2021. "Structure and inhibition of Cryptococcus neoformans sterylglucosidase to develop antifungal agents," Nature Communications, Nature, vol. 12(1), pages 1-12, December.
    3. Dylan Hong Zheng Koh & Tomoki Naito & Minyoung Na & Yee Jie Yeap & Pritisha Rozario & Franklin L. Zhong & Kah-Leong Lim & Yasunori Saheki, 2023. "Visualization of accessible cholesterol using a GRAM domain-based biosensor," Nature Communications, Nature, vol. 14(1), pages 1-20, 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_s41467-023-35915-4. 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.