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Delivery of endocytosed proteins to the cell–division plane requires change of pathway from recycling to secretion
Membrane trafficking is essential to fundamental processes in eukaryotic life, including cell growth and division. In plant cytokinesis, post-Golgi trafficking mediates a massive flow of vesicles that form the partitioning membrane but its regulation remains poorly understood. Here, we identify func...
Autores principales: | , , , , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
eLife Sciences Publications, Ltd
2014
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3979144/ https://www.ncbi.nlm.nih.gov/pubmed/24714496 http://dx.doi.org/10.7554/eLife.02131 |
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author | Richter, Sandra Kientz, Marika Brumm, Sabine Nielsen, Mads Eggert Park, Misoon Gavidia, Richard Krause, Cornelia Voss, Ute Beckmann, Hauke Mayer, Ulrike Stierhof, York-Dieter Jürgens, Gerd |
author_facet | Richter, Sandra Kientz, Marika Brumm, Sabine Nielsen, Mads Eggert Park, Misoon Gavidia, Richard Krause, Cornelia Voss, Ute Beckmann, Hauke Mayer, Ulrike Stierhof, York-Dieter Jürgens, Gerd |
author_sort | Richter, Sandra |
collection | PubMed |
description | Membrane trafficking is essential to fundamental processes in eukaryotic life, including cell growth and division. In plant cytokinesis, post-Golgi trafficking mediates a massive flow of vesicles that form the partitioning membrane but its regulation remains poorly understood. Here, we identify functionally redundant Arabidopsis ARF guanine-nucleotide exchange factors (ARF-GEFs) BIG1–BIG4 as regulators of post-Golgi trafficking, mediating late secretion from the trans-Golgi network but not recycling of endocytosed proteins to the plasma membrane, although the TGN also functions as an early endosome in plants. In contrast, BIG1-4 are absolutely required for trafficking of both endocytosed and newly synthesized proteins to the cell–division plane during cytokinesis, counteracting recycling to the plasma membrane. This change from recycling to secretory trafficking pathway mediated by ARF-GEFs confers specificity of cargo delivery to the division plane and might thus ensure that the partitioning membrane is completed on time in the absence of a cytokinesis-interphase checkpoint. DOI: http://dx.doi.org/10.7554/eLife.02131.001 |
format | Online Article Text |
id | pubmed-3979144 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2014 |
publisher | eLife Sciences Publications, Ltd |
record_format | MEDLINE/PubMed |
spelling | pubmed-39791442014-04-24 Delivery of endocytosed proteins to the cell–division plane requires change of pathway from recycling to secretion Richter, Sandra Kientz, Marika Brumm, Sabine Nielsen, Mads Eggert Park, Misoon Gavidia, Richard Krause, Cornelia Voss, Ute Beckmann, Hauke Mayer, Ulrike Stierhof, York-Dieter Jürgens, Gerd eLife Cell Biology Membrane trafficking is essential to fundamental processes in eukaryotic life, including cell growth and division. In plant cytokinesis, post-Golgi trafficking mediates a massive flow of vesicles that form the partitioning membrane but its regulation remains poorly understood. Here, we identify functionally redundant Arabidopsis ARF guanine-nucleotide exchange factors (ARF-GEFs) BIG1–BIG4 as regulators of post-Golgi trafficking, mediating late secretion from the trans-Golgi network but not recycling of endocytosed proteins to the plasma membrane, although the TGN also functions as an early endosome in plants. In contrast, BIG1-4 are absolutely required for trafficking of both endocytosed and newly synthesized proteins to the cell–division plane during cytokinesis, counteracting recycling to the plasma membrane. This change from recycling to secretory trafficking pathway mediated by ARF-GEFs confers specificity of cargo delivery to the division plane and might thus ensure that the partitioning membrane is completed on time in the absence of a cytokinesis-interphase checkpoint. DOI: http://dx.doi.org/10.7554/eLife.02131.001 eLife Sciences Publications, Ltd 2014-04-08 /pmc/articles/PMC3979144/ /pubmed/24714496 http://dx.doi.org/10.7554/eLife.02131 Text en Copyright © 2014, Richter et al http://creativecommons.org/licenses/by/3.0/ This article is distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/3.0/) , which permits unrestricted use and redistribution provided that the original author and source are credited. |
spellingShingle | Cell Biology Richter, Sandra Kientz, Marika Brumm, Sabine Nielsen, Mads Eggert Park, Misoon Gavidia, Richard Krause, Cornelia Voss, Ute Beckmann, Hauke Mayer, Ulrike Stierhof, York-Dieter Jürgens, Gerd Delivery of endocytosed proteins to the cell–division plane requires change of pathway from recycling to secretion |
title | Delivery of endocytosed proteins to the cell–division plane requires change of pathway from recycling to secretion |
title_full | Delivery of endocytosed proteins to the cell–division plane requires change of pathway from recycling to secretion |
title_fullStr | Delivery of endocytosed proteins to the cell–division plane requires change of pathway from recycling to secretion |
title_full_unstemmed | Delivery of endocytosed proteins to the cell–division plane requires change of pathway from recycling to secretion |
title_short | Delivery of endocytosed proteins to the cell–division plane requires change of pathway from recycling to secretion |
title_sort | delivery of endocytosed proteins to the cell–division plane requires change of pathway from recycling to secretion |
topic | Cell Biology |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3979144/ https://www.ncbi.nlm.nih.gov/pubmed/24714496 http://dx.doi.org/10.7554/eLife.02131 |
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