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Snf7 spirals sense and alter membrane curvature

Author

Listed:
  • Nebojsa Jukic

    (Physiology, Biophysics and Systems Biology Graduate Program, Weill Cornell Medicine)

  • Alma P. Perrino

    (Weill Cornell Medicine)

  • Frédéric Humbert

    (University of Geneva)

  • Aurélien Roux

    (University of Geneva
    Swiss National Centre for Competence in Research Programme Chemical Biology)

  • Simon Scheuring

    (Weill Cornell Medicine
    Weill Cornell Medicine
    Cornell University, Ithaca)

Abstract

Endosomal Sorting Complex Required for Transport III (ESCRT-III) is a conserved protein system involved in many cellular processes resulting in membrane deformation and scission, topologically away from the cytoplasm. However, little is known about the transition of the planar membrane-associated protein assembly into a 3D structure. High-speed atomic force microscopy (HS-AFM) provided insights into assembly, structural dynamics and turnover of Snf7, the major ESCRT-III component, on planar supported lipid bilayers. Here, we develop HS-AFM experiments that remove the constraints of membrane planarity, crowdedness, and support rigidity. On non-planar membranes, Snf7 monomers are curvature insensitive, but Snf7-spirals selectively adapt their conformation to membrane geometry. In a non-crowded system, Snf7-spirals reach a critical radius, and remodel to minimize internal stress. On non-rigid supports, Snf7-spirals compact and buckle, deforming the underlying bilayer. These experiments provide direct evidence that Snf7 is sufficient to mediate topological transitions, in agreement with the loaded spiral spring model.

Suggested Citation

  • Nebojsa Jukic & Alma P. Perrino & Frédéric Humbert & Aurélien Roux & Simon Scheuring, 2022. "Snf7 spirals sense and alter membrane curvature," Nature Communications, Nature, vol. 13(1), pages 1-17, December.
  • Handle: RePEc:nat:natcom:v:13:y:2022:i:1:d:10.1038_s41467-022-29850-z
    DOI: 10.1038/s41467-022-29850-z
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    References listed on IDEAS

    as
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