Snf7 spirals sense and alter membrane curvature.


Journal

Nature communications
ISSN: 2041-1723
Titre abrégé: Nat Commun
Pays: England
ID NLM: 101528555

Informations de publication

Date de publication:
21 04 2022
Historique:
received: 18 12 2021
accepted: 03 04 2022
entrez: 22 4 2022
pubmed: 23 4 2022
medline: 26 4 2022
Statut: epublish

Résumé

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.

Identifiants

pubmed: 35449207
doi: 10.1038/s41467-022-29850-z
pii: 10.1038/s41467-022-29850-z
pmc: PMC9023468
doi:

Substances chimiques

Endosomal Sorting Complexes Required for Transport 0
Lipid Bilayers 0

Types de publication

Journal Article Research Support, N.I.H., Extramural Research Support, Non-U.S. Gov't

Langues

eng

Sous-ensembles de citation

IM

Pagination

2174

Informations de copyright

© 2022. The Author(s).

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Auteurs

Nebojsa Jukic (N)

Physiology, Biophysics and Systems Biology Graduate Program, Weill Cornell Medicine, New York, NY, 10065, USA.

Alma P Perrino (AP)

Department of Anesthesiology, Weill Cornell Medicine, New York, NY, 10065, USA.

Frédéric Humbert (F)

Department of Biochemistry, University of Geneva, CH-1211, Geneva, Switzerland.

Aurélien Roux (A)

Department of Biochemistry, University of Geneva, CH-1211, Geneva, Switzerland.
Swiss National Centre for Competence in Research Programme Chemical Biology, CH-1211, Geneva, Switzerland.

Simon Scheuring (S)

Department of Anesthesiology, Weill Cornell Medicine, New York, NY, 10065, USA. sis2019@med.cornell.edu.
Department of Physiology and Biophysics, Weill Cornell Medicine, New York, NY, 10065, USA. sis2019@med.cornell.edu.
Kavli Institute at Cornell for Nanoscale Science, Cornell University, Ithaca, New York, NY, 14853, USA. sis2019@med.cornell.edu.

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