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Fast actin disassembly and fimbrin mechanosensitivity support rapid turnover during clathrin-mediated endocytosis

Sayed Iman Mousavi, View ORCID ProfileMichael M. Lacy, Xiaobai Li, View ORCID ProfileJulien Berro
doi: https://doi.org/10.1101/2022.11.25.517735
Sayed Iman Mousavi
1Department of Molecular Biophysics and Biochemistry; Yale University, New Haven, CT, USA
2Nanobiology Institute, Yale University; West Haven, CT 06516, USA
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Michael M. Lacy
1Department of Molecular Biophysics and Biochemistry; Yale University, New Haven, CT, USA
2Nanobiology Institute, Yale University; West Haven, CT 06516, USA
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Xiaobai Li
1Department of Molecular Biophysics and Biochemistry; Yale University, New Haven, CT, USA
2Nanobiology Institute, Yale University; West Haven, CT 06516, USA
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Julien Berro
1Department of Molecular Biophysics and Biochemistry; Yale University, New Haven, CT, USA
2Nanobiology Institute, Yale University; West Haven, CT 06516, USA
3Department of Cell Biology, Yale University School of Medicine; New Haven, CT 06520, USA
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  • For correspondence: julien.berro@yale.edu
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Abstract

The actin cytoskeleton is central to force production in numerous cellular processes in eukaryotic cells. During clathrin-mediated endocytosis (CME), a dynamic actin meshwork is required to deform the membrane against high membrane tension or turgor pressure. Previous experimental work from our lab showed that several endocytic proteins, including actin and actin-interacting proteins, turn over several times during the formation of a vesicle during CME in yeast and their dwell-time distributions were reminiscent of Gamma distributions with a peak around 1 s (Lacy et al., 2019). However, the distribution for the filament crosslinking protein fimbrin contains a second peak around 0.5 s. To better understand the nature of these dwell-time distributions, here we developed a stochastic model for the dynamics of actin and its binding partners. Our model demonstrates that very fast actin filament disassembly is necessary to reproduce experimental dwell-time distributions. Our model also predicts that actin-binding proteins bind rapidly to nascent filaments and filaments are fully decorated. Last, our model predicts that fimbrin detachment from actin endocytic structures is mechanosensitive to explain the extra peak observed in the dwell-time distribution.

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 November 25, 2022.
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Fast actin disassembly and fimbrin mechanosensitivity support rapid turnover during clathrin-mediated endocytosis
Sayed Iman Mousavi, Michael M. Lacy, Xiaobai Li, Julien Berro
bioRxiv 2022.11.25.517735; doi: https://doi.org/10.1101/2022.11.25.517735
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Fast actin disassembly and fimbrin mechanosensitivity support rapid turnover during clathrin-mediated endocytosis
Sayed Iman Mousavi, Michael M. Lacy, Xiaobai Li, Julien Berro
bioRxiv 2022.11.25.517735; doi: https://doi.org/10.1101/2022.11.25.517735

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