IDEAS home Printed from https://ideas.repec.org/a/nat/natcom/v15y2024i1d10.1038_s41467-024-46179-x.html
   My bibliography  Save this article

Cryo-EM structures reveal how phosphate release from Arp3 weakens actin filament branches formed by Arp2/3 complex

Author

Listed:
  • Sai Shashank Chavali

    (Yale University)

  • Steven Z. Chou

    (Yale University
    University of Connecticut Health Center)

  • Wenxiang Cao

    (Yale University)

  • Thomas D. Pollard

    (Yale University
    Yale University
    Yale University
    University of California)

  • Enrique M. Cruz

    (Yale University)

  • Charles V. Sindelar

    (Yale University)

Abstract

Arp2/3 complex nucleates branched actin filaments for cell and organelle movements. Here we report a 2.7 Å resolution cryo-EM structure of the mature branch junction formed by S. pombe Arp2/3 complex that provides details about interactions with both mother and daughter filaments. We determine a second structure at 3.2 Å resolution with the phosphate analog BeFx bound with ADP to Arp3 and ATP bound to Arp2. In this ADP-BeFx transition state the outer domain of Arp3 is rotated 2° toward the mother filament compared with the ADP state and makes slightly broader contacts with actin in both the mother and daughter filaments. Thus, dissociation of Pi from the ADP-Pi transition state reduces the interactions of Arp2/3 complex with the actin filaments and may contribute to the lower mechanical stability of mature branch junctions with ADP bound to the Arps. Our structures also reveal that the mother filament in contact with Arp2/3 complex is slightly bent and twisted, consistent with the preference of Arp2/3 complex binding curved actin filaments. The small degree of twisting constrains models of actin filament mechanics.

Suggested Citation

  • Sai Shashank Chavali & Steven Z. Chou & Wenxiang Cao & Thomas D. Pollard & Enrique M. Cruz & Charles V. Sindelar, 2024. "Cryo-EM structures reveal how phosphate release from Arp3 weakens actin filament branches formed by Arp2/3 complex," Nature Communications, Nature, vol. 15(1), pages 1-12, December.
    • Handle: RePEc:nat:natcom:v:15:y:2024:i:1:d:10.1038_s41467-024-46179-x
    DOI: 10.1038/s41467-024-46179-x
    as

    Download full text from publisher

    File URL: https://www.nature.com/articles/s41467-024-46179-x
    File Function: Abstract
    Download Restriction: no
    File URL: https://libkey.io/10.1038/s41467-024-46179-x?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. Matthew J. Reynolds & Carla Hachicho & Ayala G. Carl & Rui Gong & Gregory M. Alushin, 2022. "Bending forces and nucleotide state jointly regulate F-actin structure," Nature, Nature, vol. 611(7935), pages 380-386, November.
    2. Florian Fäßler & Georgi Dimchev & Victor-Valentin Hodirnau & William Wan & Florian K. M. Schur, 2020. "Cryo-electron tomography structure of Arp2/3 complex in cells reveals new insights into the branch junction," Nature Communications, Nature, vol. 11(1), pages 1-10, December.
    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. Kelli L. Hvorecny & Thomas E. Sladewski & Enrique M. Cruz & Justin M. Kollman & Aoife T. Heaslip, 2024. "Toxoplasma gondii actin filaments are tuned for rapid disassembly and turnover," Nature Communications, Nature, vol. 15(1), pages 1-16, December.
    2. Fred E. Fregoso & Malgorzata Boczkowska & Grzegorz Rebowski & Peter J. Carman & Trevor Eeuwen & Roberto Dominguez, 2023. "Mechanism of synergistic activation of Arp2/3 complex by cortactin and WASP-family proteins," Nature Communications, Nature, vol. 14(1), pages 1-11, December.
    3. Qianqian Ma & Wahyu Surya & Danxia He & Hanmeng Yang & Xiao Han & Mui Hoon Nai & Chwee Teck Lim & Jaume Torres & Yansong Miao, 2024. "Spa2 remodels ADP-actin via molecular condensation under glucose starvation," Nature Communications, Nature, vol. 15(1), pages 1-16, December.
    4. Sophie M. Travis & Brian P. Mahon & Wei Huang & Meisheng Ma & Michael J. Rale & Jodi Kraus & Derek J. Taylor & Rui Zhang & Sabine Petry, 2023. "Integrated model of the vertebrate augmin complex," Nature Communications, Nature, vol. 14(1), pages 1-10, December.
    5. Fred E. Fregoso & Trevor Eeuwen & Gleb Simanov & Grzegorz Rebowski & Malgorzata Boczkowska & Austin Zimmet & Alexis M. Gautreau & Roberto Dominguez, 2022. "Molecular mechanism of Arp2/3 complex inhibition by Arpin," Nature Communications, Nature, vol. 13(1), pages 1-12, December.
    6. Chisato Tsuji & Marston Bradshaw & Megan F. Allen & Molly L. Jackson & Judith Mantell & Ufuk Borucu & Alastair W. Poole & Paul Verkade & Ingeborg Hers & Danielle M. Paul & Mark P. Dodding, 2024. "CryoET reveals actin filaments within platelet microtubules," Nature Communications, Nature, vol. 15(1), pages 1-8, 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:15:y:2024:i:1:d:10.1038_s41467-024-46179-x. 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.