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Yeast vacuoles fragment in an asymmetrical two-phase process with distinct protein requirements
Yeast vacuoles fragment and fuse in response to environmental conditions, such as changes in osmotic conditions or nutrient availability. Here we analyze osmotically induced vacuole fragmentation by time-lapse microscopy. Small fragmentation products originate directly from the large central vacuole...
Autores principales: | , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
The American Society for Cell Biology
2012
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3431934/ https://www.ncbi.nlm.nih.gov/pubmed/22787281 http://dx.doi.org/10.1091/mbc.E12-05-0347 |
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author | Zieger, Martin Mayer, Andreas |
author_facet | Zieger, Martin Mayer, Andreas |
author_sort | Zieger, Martin |
collection | PubMed |
description | Yeast vacuoles fragment and fuse in response to environmental conditions, such as changes in osmotic conditions or nutrient availability. Here we analyze osmotically induced vacuole fragmentation by time-lapse microscopy. Small fragmentation products originate directly from the large central vacuole. This happens by asymmetrical scission rather than by consecutive equal divisions. Fragmentation occurs in two distinct phases. Initially, vacuoles shrink and generate deep invaginations that leave behind tubular structures in their vicinity. Already this invagination requires the dynamin-like GTPase Vps1p and the vacuolar proton gradient. Invaginations are stabilized by phosphatidylinositol 3-phosphate (PI(3)P) produced by the phosphoinositide 3-kinase complex II. Subsequently, vesicles pinch off from the tips of the tubular structures in a polarized manner, directly generating fragmentation products of the final size. This phase depends on the production of phosphatidylinositol-3,5-bisphosphate and the Fab1 complex. It is accelerated by the PI(3)P- and phosphatidylinositol 3,5-bisphosphate–binding protein Atg18p. Thus vacuoles fragment in two steps with distinct protein and lipid requirements. |
format | Online Article Text |
id | pubmed-3431934 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2012 |
publisher | The American Society for Cell Biology |
record_format | MEDLINE/PubMed |
spelling | pubmed-34319342012-11-16 Yeast vacuoles fragment in an asymmetrical two-phase process with distinct protein requirements Zieger, Martin Mayer, Andreas Mol Biol Cell Articles Yeast vacuoles fragment and fuse in response to environmental conditions, such as changes in osmotic conditions or nutrient availability. Here we analyze osmotically induced vacuole fragmentation by time-lapse microscopy. Small fragmentation products originate directly from the large central vacuole. This happens by asymmetrical scission rather than by consecutive equal divisions. Fragmentation occurs in two distinct phases. Initially, vacuoles shrink and generate deep invaginations that leave behind tubular structures in their vicinity. Already this invagination requires the dynamin-like GTPase Vps1p and the vacuolar proton gradient. Invaginations are stabilized by phosphatidylinositol 3-phosphate (PI(3)P) produced by the phosphoinositide 3-kinase complex II. Subsequently, vesicles pinch off from the tips of the tubular structures in a polarized manner, directly generating fragmentation products of the final size. This phase depends on the production of phosphatidylinositol-3,5-bisphosphate and the Fab1 complex. It is accelerated by the PI(3)P- and phosphatidylinositol 3,5-bisphosphate–binding protein Atg18p. Thus vacuoles fragment in two steps with distinct protein and lipid requirements. The American Society for Cell Biology 2012-09-01 /pmc/articles/PMC3431934/ /pubmed/22787281 http://dx.doi.org/10.1091/mbc.E12-05-0347 Text en © 2012 Zieger and Mayer. This article is distributed by The American Society for Cell Biology under license from the author(s). Two months after publication it is available to the public under an Attribution–Noncommercial–Share Alike 3.0 Unported Creative Commons License (http://creativecommons.org/licenses/by-nc-sa/3.0). “ASCB®,” “The American Society for Cell Biology®,” and “Molecular Biology of the Cell®” are registered trademarks of The American Society of Cell BD; are registered trademarks of The American Society of Cell Biology. |
spellingShingle | Articles Zieger, Martin Mayer, Andreas Yeast vacuoles fragment in an asymmetrical two-phase process with distinct protein requirements |
title | Yeast vacuoles fragment in an asymmetrical two-phase process with distinct protein requirements |
title_full | Yeast vacuoles fragment in an asymmetrical two-phase process with distinct protein requirements |
title_fullStr | Yeast vacuoles fragment in an asymmetrical two-phase process with distinct protein requirements |
title_full_unstemmed | Yeast vacuoles fragment in an asymmetrical two-phase process with distinct protein requirements |
title_short | Yeast vacuoles fragment in an asymmetrical two-phase process with distinct protein requirements |
title_sort | yeast vacuoles fragment in an asymmetrical two-phase process with distinct protein requirements |
topic | Articles |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3431934/ https://www.ncbi.nlm.nih.gov/pubmed/22787281 http://dx.doi.org/10.1091/mbc.E12-05-0347 |
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