Cargando…

An Abp1-Dependent Route of Endocytosis Functions when the Classical Endocytic Pathway in Yeast Is Inhibited

Clathrin-mediated endocytosis (CME) is a well characterized pathway in both yeast and mammalian cells. An increasing number of alternative endocytic pathways have now been described in mammalian cells that can be both clathrin, actin, and Arf6- dependent or independent. In yeast, a single clathrin-m...

Descripción completa

Detalles Bibliográficos
Autores principales: Aghamohammadzadeh, Soheil, Smaczynska-de Rooij, Iwona I., Ayscough, Kathryn R.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Public Library of Science 2014
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4114835/
https://www.ncbi.nlm.nih.gov/pubmed/25072293
http://dx.doi.org/10.1371/journal.pone.0103311
_version_ 1782328492233326592
author Aghamohammadzadeh, Soheil
Smaczynska-de Rooij, Iwona I.
Ayscough, Kathryn R.
author_facet Aghamohammadzadeh, Soheil
Smaczynska-de Rooij, Iwona I.
Ayscough, Kathryn R.
author_sort Aghamohammadzadeh, Soheil
collection PubMed
description Clathrin-mediated endocytosis (CME) is a well characterized pathway in both yeast and mammalian cells. An increasing number of alternative endocytic pathways have now been described in mammalian cells that can be both clathrin, actin, and Arf6- dependent or independent. In yeast, a single clathrin-mediated pathway has been characterized in detail. However, disruption of this pathway in many mutant strains indicates that other uptake pathways might exist, at least for bulk lipid and fluid internalization. Using a combination of genetics and live cell imaging, here we show evidence for a novel endocytic pathway in S. cerevisiae that does not involve several of the proteins previously shown to be associated with the ‘classic’ pathway of endocytosis. This alternative pathway functions in the presence of low levels of the actin-disrupting drug latrunculin-A which inhibits movement of the proteins Sla1, Sla2, and Sac6, and is independent of dynamin function. We reveal that in the absence of the ‘classic’ pathway, the actin binding protein Abp1 is now essential for bulk endocytosis. This novel pathway appears to be distinct from another described alternative endocytic route in S. cerevisiae as it involves at least some proteins known to be associated with cortical actin patches rather than being mediated at formin-dependent endocytic sites. These data indicate that cells have the capacity to use overlapping sets of components to facilitate endocytosis under a range of conditions.
format Online
Article
Text
id pubmed-4114835
institution National Center for Biotechnology Information
language English
publishDate 2014
publisher Public Library of Science
record_format MEDLINE/PubMed
spelling pubmed-41148352014-08-04 An Abp1-Dependent Route of Endocytosis Functions when the Classical Endocytic Pathway in Yeast Is Inhibited Aghamohammadzadeh, Soheil Smaczynska-de Rooij, Iwona I. Ayscough, Kathryn R. PLoS One Research Article Clathrin-mediated endocytosis (CME) is a well characterized pathway in both yeast and mammalian cells. An increasing number of alternative endocytic pathways have now been described in mammalian cells that can be both clathrin, actin, and Arf6- dependent or independent. In yeast, a single clathrin-mediated pathway has been characterized in detail. However, disruption of this pathway in many mutant strains indicates that other uptake pathways might exist, at least for bulk lipid and fluid internalization. Using a combination of genetics and live cell imaging, here we show evidence for a novel endocytic pathway in S. cerevisiae that does not involve several of the proteins previously shown to be associated with the ‘classic’ pathway of endocytosis. This alternative pathway functions in the presence of low levels of the actin-disrupting drug latrunculin-A which inhibits movement of the proteins Sla1, Sla2, and Sac6, and is independent of dynamin function. We reveal that in the absence of the ‘classic’ pathway, the actin binding protein Abp1 is now essential for bulk endocytosis. This novel pathway appears to be distinct from another described alternative endocytic route in S. cerevisiae as it involves at least some proteins known to be associated with cortical actin patches rather than being mediated at formin-dependent endocytic sites. These data indicate that cells have the capacity to use overlapping sets of components to facilitate endocytosis under a range of conditions. Public Library of Science 2014-07-29 /pmc/articles/PMC4114835/ /pubmed/25072293 http://dx.doi.org/10.1371/journal.pone.0103311 Text en © 2014 Aghamohammadzadeh et al http://creativecommons.org/licenses/by/4.0/ This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are properly credited.
spellingShingle Research Article
Aghamohammadzadeh, Soheil
Smaczynska-de Rooij, Iwona I.
Ayscough, Kathryn R.
An Abp1-Dependent Route of Endocytosis Functions when the Classical Endocytic Pathway in Yeast Is Inhibited
title An Abp1-Dependent Route of Endocytosis Functions when the Classical Endocytic Pathway in Yeast Is Inhibited
title_full An Abp1-Dependent Route of Endocytosis Functions when the Classical Endocytic Pathway in Yeast Is Inhibited
title_fullStr An Abp1-Dependent Route of Endocytosis Functions when the Classical Endocytic Pathway in Yeast Is Inhibited
title_full_unstemmed An Abp1-Dependent Route of Endocytosis Functions when the Classical Endocytic Pathway in Yeast Is Inhibited
title_short An Abp1-Dependent Route of Endocytosis Functions when the Classical Endocytic Pathway in Yeast Is Inhibited
title_sort abp1-dependent route of endocytosis functions when the classical endocytic pathway in yeast is inhibited
topic Research Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4114835/
https://www.ncbi.nlm.nih.gov/pubmed/25072293
http://dx.doi.org/10.1371/journal.pone.0103311
work_keys_str_mv AT aghamohammadzadehsoheil anabp1dependentrouteofendocytosisfunctionswhentheclassicalendocyticpathwayinyeastisinhibited
AT smaczynskaderooijiwonai anabp1dependentrouteofendocytosisfunctionswhentheclassicalendocyticpathwayinyeastisinhibited
AT ayscoughkathrynr anabp1dependentrouteofendocytosisfunctionswhentheclassicalendocyticpathwayinyeastisinhibited
AT aghamohammadzadehsoheil abp1dependentrouteofendocytosisfunctionswhentheclassicalendocyticpathwayinyeastisinhibited
AT smaczynskaderooijiwonai abp1dependentrouteofendocytosisfunctionswhentheclassicalendocyticpathwayinyeastisinhibited
AT ayscoughkathrynr abp1dependentrouteofendocytosisfunctionswhentheclassicalendocyticpathwayinyeastisinhibited