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

Kukulski, W., Picco, A., Specht, T., Briggs, J. A. G., & Kaksonen, M. (2016). Clathrin modulates vesicle scission, but not invagination shape, in yeast endocytosis. Elife, 5: e16036. doi:10.7554/eLife.16036.

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 Creators:
Kukulski, W., Author
Picco, A., Author
Specht, T., Author
Briggs, John A. G.1, Author           
Kaksonen, M., Author
Affiliations:
1European Molecular Biology Laboratory, External Organizations, ou_3346677              

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Free keywords: electron-microscopy saccharomyces-cerevisiae correlated fluorescence mediated endocytosis plasma-membrane light-chain amphiphysin tomography dynamics sites Life Sciences & Biomedicine - Other Topics
 Abstract: In a previous paper (Piece et aL, 2015), 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.

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Language(s): eng - English
 Dates: 2016
 Publication Status: Issued
 Pages: -
 Publishing info: -
 Table of Contents: -
 Rev. Type: -
 Identifiers: Other: WOS:000380919500001
DOI: 10.7554/eLife.16036
ISSN: 2050-084X
 Degree: -

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Title: Elife
  Alternative Title : eLife
Source Genre: Journal
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Pages: - Volume / Issue: 5 Sequence Number: e16036 Start / End Page: - Identifier: -