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Single-molecule turnover dynamics of actin and membrane coat proteins in clathrin-mediated endocytosis

Michael M. Lacy, David Baddeley, View ORCID ProfileJulien Berro
doi: https://doi.org/10.1101/617746
Michael M. Lacy
1Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, CT 06520
2NanoBiology Institute, Yale University, West Haven, CT 06516
3Integrated Graduate Program in Physical and Engineering Biology, Yale University, New Haven, CT 06520
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David Baddeley
2NanoBiology Institute, Yale University, West Haven, CT 06516
4Department of Cell Biology, Yale University, New Haven, CT 06520
5Auckland Bioengineering Institute, University of Auckland, Auckland 1010 New Zealand
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Julien Berro
1Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, CT 06520
2NanoBiology Institute, Yale University, West Haven, CT 06516
4Department of Cell Biology, Yale University, New Haven, CT 06520
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  • ORCID record for Julien Berro
  • For correspondence: julien.berro@yale.edu
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Abstract

Actin is required for clathrin-mediated endocytosis (CME) in yeast. Experimental observations indicate that this actin assembly generates force to deform the membrane and overcome the cell’s high turgor pressure, but the precise molecular details remain unresolved. Based on previous models, we predicted that actin at endocytic sites continually polymerize and disassemble, turning over multiple times during an endocytic event. Here we applied single-molecule speckle tracking in live fission yeast to directly measure this predicted turnover within the CME assembly for the first time. In contrast with the overall ~20-sec lifetimes of actin and actin-associated proteins in endocytic patches, we detected single-molecule residence times around 1 to 2 sec, and high turnover rates of membrane-associated proteins in CME. Furthermore, we find heterogeneous behaviors in many proteins’ motions. These results indicate that rapid and continuous turnover is a key feature of the endocytic machinery and suggest revising quantitative models of force production.

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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 April 24, 2019.
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Single-molecule turnover dynamics of actin and membrane coat proteins in clathrin-mediated endocytosis
Michael M. Lacy, David Baddeley, Julien Berro
bioRxiv 617746; doi: https://doi.org/10.1101/617746
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Single-molecule turnover dynamics of actin and membrane coat proteins in clathrin-mediated endocytosis
Michael M. Lacy, David Baddeley, Julien Berro
bioRxiv 617746; doi: https://doi.org/10.1101/617746

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