IDEAS home Printed from https://ideas.repec.org/a/nat/nature/v468y2010i7325d10.1038_nature09583.html
   My bibliography  Save this article

Calcium-dependent phospholipid scrambling by TMEM16F

Author

Listed:
  • Jun Suzuki

    (Graduate School of Medicine, Kyoto University, Yoshida, Sakyo-ku, Kyoto 606-8501, Japan
    Core Research for Evolutional Science and Technology, Japan Science and Technology Corporation, Kyoto 606-8501, Japan)

  • Masato Umeda

    (Graduate School of Engineering, Kyoto University, Katsura, Nishikyo-ku, Kyoto 615-8510, Japan)

  • Peter J. Sims

    (University of Rochester Medical Center, 601 Elmwood Avenue, Rochester, New York 14642, USA)

  • Shigekazu Nagata

    (Graduate School of Medicine, Kyoto University, Yoshida, Sakyo-ku, Kyoto 606-8501, Japan
    Core Research for Evolutional Science and Technology, Japan Science and Technology Corporation, Kyoto 606-8501, Japan)

Abstract

Phospholipid scrambling The plasma membranes of eukaryotic cells have an asymmetrical distribution of phospholipids. Lipid asymmetry can be disrupted during biological processes such as apoptosis, when phosphatidylserine in the inner leaflet of the membrane is exposed on the outer membrane. It has been proposed that activation of a phospholipid scramblase catalyses bidirectional transbilayer movement of phospholipids, and now a protein corresponding to this activity has been identified as TMEM16F, a member of the TMEM16 family of transmembrane proteins. Furthermore, a patient with Scott syndrome, which results from a defect in phospholipid scrambling activity, was found to carry a mutation in the gene encoding TMEM16F.

Suggested Citation

  • Jun Suzuki & Masato Umeda & Peter J. Sims & Shigekazu Nagata, 2010. "Calcium-dependent phospholipid scrambling by TMEM16F," Nature, Nature, vol. 468(7325), pages 834-838, December.
    • Handle: RePEc:nat:nature:v:468:y:2010:i:7325:d:10.1038_nature09583
    DOI: 10.1038/nature09583
    as

    Download full text from publisher

    File URL: https://www.nature.com/articles/nature09583
    File Function: Abstract
    Download Restriction: Access to the full text of the articles in this series is restricted.
    File URL: https://libkey.io/10.1038/nature09583?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
    ---><---

    As the access to this document is restricted, you may want to search for a different version of it.

    Citations

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


    Cited by:

    1. Panpan Zhang & Masahiro Maruoka & Ryo Suzuki & Hikaru Katani & Yu Dou & Daniel M. Packwood & Hidetaka Kosako & Motomu Tanaka & Jun Suzuki, 2023. "Extracellular calcium functions as a molecular glue for transmembrane helices to activate the scramblase Xkr4," Nature Communications, Nature, vol. 14(1), pages 1-13, December.
    2. Andy K. M. Lam & Sonja Rutz & Raimund Dutzler, 2022. "Inhibition mechanism of the chloride channel TMEM16A by the pore blocker 1PBC," Nature Communications, Nature, vol. 13(1), pages 1-13, December.
    3. Melanie Arndt & Carolina Alvadia & Monique S. Straub & Vanessa Clerico Mosina & Cristina Paulino & Raimund Dutzler, 2022. "Structural basis for the activation of the lipid scramblase TMEM16F," Nature Communications, Nature, vol. 13(1), pages 1-17, December.
    4. Han Niu & Masahiro Maruoka & Yuki Noguchi & Hidetaka Kosako & Jun Suzuki, 2024. "Phospholipid scrambling induced by an ion channel/metabolite transporter complex," Nature Communications, Nature, vol. 15(1), pages 1-15, December.
    5. Shengjie Feng & Cristina Puchades & Juyeon Ko & Hao Wu & Yifei Chen & Eric E. Figueroa & Shuo Gu & Tina W. Han & Brandon Ho & Tong Cheng & Junrui Li & Brian Shoichet & Yuh Nung Jan & Yifan Cheng & Lil, 2023. "Identification of a drug binding pocket in TMEM16F calcium-activated ion channel and lipid scramblase," Nature Communications, Nature, vol. 14(1), pages 1-12, December.
    6. Maria E. Falzone & Zhang Feng & Omar E. Alvarenga & Yangang Pan & ByoungCheol Lee & Xiaolu Cheng & Eva Fortea & Simon Scheuring & Alessio Accardi, 2022. "TMEM16 scramblases thin the membrane to enable lipid scrambling," Nature Communications, Nature, vol. 13(1), pages 1-14, December.
    7. Susan A. Leonhardt & Michael D. Purdy & Jonathan R. Grover & Ziwei Yang & Sandra Poulos & William E. McIntire & Elizabeth A. Tatham & Satchal K. Erramilli & Kamil Nosol & Kin Kui Lai & Shilei Ding & M, 2023. "Antiviral HIV-1 SERINC restriction factors disrupt virus membrane asymmetry," Nature Communications, Nature, vol. 14(1), pages 1-16, December.
    8. Zhongjie Ye & Nicola Galvanetto & Leonardo Puppulin & Simone Pifferi & Holger Flechsig & Melanie Arndt & Cesar Adolfo Sánchez Triviño & Michael Palma & Shifeng Guo & Horst Vogel & Anna Menini & Clemen, 2024. "Structural heterogeneity of the ion and lipid channel TMEM16F," Nature Communications, Nature, vol. 15(1), pages 1-15, December.
    9. Patrick Niekamp & Felix Scharte & Tolulope Sokoya & Laura Vittadello & Yeongho Kim & Yongqiang Deng & Elisabeth Südhoff & Angelika Hilderink & Mirco Imlau & Christopher J. Clarke & Michael Hensel & Ch, 2022. "Ca2+-activated sphingomyelin scrambling and turnover mediate ESCRT-independent lysosomal repair," Nature Communications, Nature, vol. 13(1), pages 1-16, 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:nature:v:468:y:2010:i:7325:d:10.1038_nature09583. 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.

    We have no bibliographic references for this item. You can help adding them by using 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.