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Superresolution microscopy reveals partial preassembly and subsequent bending of the clathrin coat during endocytosis

View ORCID ProfileMarkus Mund, View ORCID ProfileAline Tschanz, View ORCID ProfileYu-Le Wu, View ORCID ProfileFelix Frey, View ORCID ProfileJohanna L. Mehl, View ORCID ProfileMarko Kaksonen, View ORCID ProfileOri Avinoam, View ORCID ProfileUlrich S. Schwarz, View ORCID ProfileJonas Ries
doi: https://doi.org/10.1101/2021.10.12.463947
Markus Mund
1European Molecular Biology Laboratory, Cell Biology and Biophysics, Meyerhofstrasse 1, 69117 Heidelberg, Germany
2University of Geneva, Department of Biochemistry, Quai Ernest-Ansermet 30, 1205 Geneva, Switzerland
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Aline Tschanz
1European Molecular Biology Laboratory, Cell Biology and Biophysics, Meyerhofstrasse 1, 69117 Heidelberg, Germany
3Candidate for Joint PhD Programme of EMBL and University of Heidelberg
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Yu-Le Wu
1European Molecular Biology Laboratory, Cell Biology and Biophysics, Meyerhofstrasse 1, 69117 Heidelberg, Germany
3Candidate for Joint PhD Programme of EMBL and University of Heidelberg
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Felix Frey
4Kavli Institute of Nanoscience, Department of Bionanoscience, Delft University of Technology, Van der Maasweg 9, 2629 HZ Delft, The Netherlands
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Johanna L. Mehl
1European Molecular Biology Laboratory, Cell Biology and Biophysics, Meyerhofstrasse 1, 69117 Heidelberg, Germany
5ETH Zurich, Switzerland
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Marko Kaksonen
2University of Geneva, Department of Biochemistry, Quai Ernest-Ansermet 30, 1205 Geneva, Switzerland
6University of Geneva, NCCR Chemical Biology, Geneva, Switzerland
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Ori Avinoam
1European Molecular Biology Laboratory, Cell Biology and Biophysics, Meyerhofstrasse 1, 69117 Heidelberg, Germany
7Weizmann Institute of Science, Department of Biomolecular Sciences, Herzl St 234, Rehovot, Israel
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Ulrich S. Schwarz
8Institute for Theoretical Physics and Bioquant, Heidelberg University, Philosophenweg 19, 69120 Heidelberg, Germany
9Bioquant, Heidelberg University, Im Neuenheimer Feld 267, 69120 Heidelberg, Germany
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Jonas Ries
1European Molecular Biology Laboratory, Cell Biology and Biophysics, Meyerhofstrasse 1, 69117 Heidelberg, Germany
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  • For correspondence: Jonas.ries@embl.de
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Abstract

Eukaryotic cells use clathrin-mediated endocytosis to take up a large range of extracellular cargos. During endocytosis, a clathrin coat forms on the plasma membrane, but it remains controversial when and how it is remodeled into a spherical vesicle.

Here, we use 3D superresolution microscopy to determine the precise geometry of the clathrin coat at large numbers of endocytic sites. Through pseudo-temporal sorting, we determine the average trajectory of clathrin remodeling during endocytosis. We find that clathrin coats assemble first on flat membranes to 50% of the coat area, before they become rapidly and continuously bent, and confirm this mechanism in three cell lines. We introduce the cooperative curvature model, which is based on positive feedback for curvature generation. It accurately describes the measured shapes and dynamics of the clathrin coat and could represent a general mechanism for clathrin coat remodeling on the plasma membrane.

Competing Interest Statement

The authors have declared no competing interest.

Copyright 
The copyright holder for this preprint is the author/funder, who has granted bioRxiv a license to display the preprint in perpetuity. It is made available under a CC-BY-NC-ND 4.0 International license.
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Posted June 09, 2022.
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Superresolution microscopy reveals partial preassembly and subsequent bending of the clathrin coat during endocytosis
Markus Mund, Aline Tschanz, Yu-Le Wu, Felix Frey, Johanna L. Mehl, Marko Kaksonen, Ori Avinoam, Ulrich S. Schwarz, Jonas Ries
bioRxiv 2021.10.12.463947; doi: https://doi.org/10.1101/2021.10.12.463947
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Superresolution microscopy reveals partial preassembly and subsequent bending of the clathrin coat during endocytosis
Markus Mund, Aline Tschanz, Yu-Le Wu, Felix Frey, Johanna L. Mehl, Marko Kaksonen, Ori Avinoam, Ulrich S. Schwarz, Jonas Ries
bioRxiv 2021.10.12.463947; doi: https://doi.org/10.1101/2021.10.12.463947

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