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ATP-dependent membrane remodeling links EHD1 functions to endocytic recycling

Author

Listed:
  • Raunaq Deo

    (Indian Institute of Science Education and Research)

  • Manish S. Kushwah

    (Indian Institute of Science Education and Research)

  • Sukrut C. Kamerkar

    (Indian Institute of Science Education and Research)

  • Nagesh Y. Kadam

    (Indian Institute of Science Education and Research)

  • Srishti Dar

    (Indian Institute of Science Education and Research)

  • Kavita Babu

    (Indian Institute of Science Education and Research)

  • Anand Srivastava

    (Indian Institute of Science)

  • Thomas J. Pucadyil

    (Indian Institute of Science Education and Research)

Abstract

Endocytic and recycling pathways generate cargo-laden transport carriers by membrane fission. Classical dynamins, which generate transport carriers during endocytosis, constrict and cause fission of membrane tubes in response to GTP hydrolysis. Relatively, less is known about the ATP-binding Eps15-homology domain-containing protein1 (EHD1), a dynamin family member that functions at the endocytic-recycling compartment. Here, we show using cross complementation assays in C. elegans that EHD1’s membrane binding and ATP hydrolysis activities are necessary for endocytic recycling. Further, we show that ATP-bound EHD1 forms membrane-active scaffolds that bulge tubular model membranes. ATP hydrolysis promotes scaffold self-assembly, causing the bulge to extend and thin down intermediate regions on the tube. On tubes below 25 nm in radius, such thinning leads to scission. Molecular dynamics simulations corroborate this scission pathway. Deletion of N-terminal residues causes defects in stable scaffolding, scission and endocytic recycling. Thus, ATP hydrolysis-dependent membrane remodeling links EHD1 functions to endocytic recycling.

Suggested Citation

  • Raunaq Deo & Manish S. Kushwah & Sukrut C. Kamerkar & Nagesh Y. Kadam & Srishti Dar & Kavita Babu & Anand Srivastava & Thomas J. Pucadyil, 2018. "ATP-dependent membrane remodeling links EHD1 functions to endocytic recycling," Nature Communications, Nature, vol. 9(1), pages 1-15, December.
    • Handle: RePEc:nat:natcom:v:9:y:2018:i:1:d:10.1038_s41467-018-07586-z
    DOI: 10.1038/s41467-018-07586-z
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    Cited by:

    1. Arthur A. Melo & Thiemo Sprink & Jeffrey K. Noel & Elena Vázquez-Sarandeses & Chris Hoorn & Saif Mohd & Justus Loerke & Christian M. T. Spahn & Oliver Daumke, 2022. "Cryo-electron tomography reveals structural insights into the membrane remodeling mode of dynamin-like EHD filaments," Nature Communications, Nature, vol. 13(1), pages 1-13, December.
    2. Viola Nähse & Camilla Raiborg & Kia Wee Tan & Sissel Mørk & Maria Lyngaas Torgersen & Eva Maria Wenzel & Mireia Nager & Veijo T. Salo & Terje Johansen & Elina Ikonen & Kay Oliver Schink & Harald Stenm, 2023. "ATPase activity of DFCP1 controls selective autophagy," Nature Communications, Nature, vol. 14(1), pages 1-15, December.

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