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Clathrin modulates vesicle scission, but not invagination shape, in yeast endocytosis

  1. Wanda Kukulski  Is a corresponding author
  2. Andrea Picco
  3. Tanja Specht
  4. John AG Briggs
  5. Marko Kaksonen
  1. European Molecular Biology Laboratory, Germany
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Cite this article as: eLife 2016;5:e16036 doi: 10.7554/eLife.16036

Abstract

In a previous paper (1), the dynamic architecture of the protein machinery during clathrin-mediated endocytosis was visualized using a new live imaging and particle tracking method. Here, by combining this approach with correlative light and electron microscopy, we address the role of clathrin in this process. During endocytosis, clathrin forms a cage-like coat around the membrane and associated protein components. There is growing evidence that clathrin does not determine the membrane morphology of the invagination but rather modulates the progression of endocytosis. We investigate how the deletion of clathrin heavy chain impairs the dynamics and the morphology of the endocytic membrane in budding yeast. Our results show that clathrin is not required for elongating or shaping the endocytic membrane invagination. Instead, we find that clathrin contributes to the regularity of vesicle scission and thereby to controlling vesicle size.

Article and author information

Author details

  1. Wanda Kukulski

    Structural and Computational Biology Unit, European Molecular Biology Laboratory, Heidelberg, Germany
    For correspondence
    kukulski@mrc-lmb.cam.ac.uk
    Competing interests
    The authors declare that no competing interests exist.
  2. Andrea Picco

    Cell Biology and Biophysics Unit, European Molecular Biology Laboratory, Heidelberg, Germany
    Competing interests
    The authors declare that no competing interests exist.
  3. Tanja Specht

    Cell Biology and Biophysics Unit, European Molecular Biology Laboratory, Heidelberg, Germany
    Competing interests
    The authors declare that no competing interests exist.
  4. John AG Briggs

    Structural and Computational Biology Unit, European Molecular Biology Laboratory, Heidelberg, Germany
    Competing interests
    The authors declare that no competing interests exist.
  5. Marko Kaksonen

    Cell Biology and Biophysics Unit, European Molecular Biology Laboratory, Heidelberg, Germany
    Competing interests
    The authors declare that no competing interests exist.

Reviewing Editor

  1. Suzanne R Pfeffer, Stanford University School of Medicine, United States

Publication history

  1. Received: March 17, 2016
  2. Accepted: June 23, 2016
  3. Accepted Manuscript published: June 24, 2016 (version 1)
  4. Version of Record published: July 14, 2016 (version 2)

Copyright

© 2016, Kukulski et al.

This article is distributed under the terms of the Creative Commons Attribution License permitting unrestricted use and redistribution provided that the original author and source are credited.

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