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1.
Elife ; 3: e01883, 2014 May 06.
Article in English | MEDLINE | ID: mdl-24843009

ABSTRACT

In many cell types, lateral diffusion barriers compartmentalize the plasma membrane and, at least in budding yeast, the endoplasmic reticulum (ER). However, the molecular nature of these barriers, their mode of action and their cellular functions are unclear. Here, we show that misfolded proteins of the ER remain confined into the mother compartment of budding yeast cells. Confinement required the formation of a lateral diffusion barrier in the form of a distinct domain of the ER-membrane at the bud neck, in a septin-, Bud1 GTPase- and sphingolipid-dependent manner. The sphingolipids, but not Bud1, also contributed to barrier formation in the outer membrane of the dividing nucleus. Barrier-dependent confinement of ER stress into the mother cell promoted aging. Together, our data clarify the physical nature of lateral diffusion barriers in the ER and establish the role of such barriers in the asymmetric segregation of proteotoxic misfolded proteins during cell division and aging.DOI: http://dx.doi.org/10.7554/eLife.01883.001.


Subject(s)
Cell Division , Endoplasmic Reticulum Stress , Endoplasmic Reticulum/metabolism , Intracellular Membranes/metabolism , Saccharomyces cerevisiae/metabolism , Sphingolipids/metabolism , Cell Cycle Proteins/metabolism , Diffusion , Guanine Nucleotide Exchange Factors/metabolism , Microfilament Proteins/metabolism , Nuclear Envelope/metabolism , Permeability , Protein Folding , Saccharomyces cerevisiae/genetics , Saccharomyces cerevisiae/growth & development , Saccharomyces cerevisiae Proteins/metabolism , Septins/metabolism , Time Factors , rab GTP-Binding Proteins/metabolism
2.
Mol Cell Biol ; 26(19): 7299-317, 2006 Oct.
Article in English | MEDLINE | ID: mdl-16980630

ABSTRACT

A striking characteristic of a Rab protein is its steady-state localization to the cytosolic surface of a particular subcellular membrane. In this study, we have undertaken a combined bioinformatic and experimental approach to examine the evolutionary conservation of Rab protein localization. A comprehensive primary sequence classification shows that 10 out of the 11 Rab proteins identified in the yeast (Saccharomyces cerevisiae) genome can be grouped within a major subclass, each comprising multiple Rab orthologs from diverse species. We compared the locations of individual yeast Rab proteins with their localizations following ectopic expression in mammalian cells. Our results suggest that green fluorescent protein-tagged Rab proteins maintain localizations across large evolutionary distances and that the major known player in the Rab localization pathway, mammalian Rab-GDI, is able to function in yeast. These findings enable us to provide insight into novel gene functions and classify the uncharacterized Rab proteins Ypt10p (YBR264C) as being involved in endocytic function and Ypt11p (YNL304W) as being localized to the endoplasmic reticulum, where we demonstrate it is required for organelle inheritance.


Subject(s)
Computational Biology , GTP-Binding Proteins/metabolism , Saccharomyces cerevisiae Proteins/metabolism , Saccharomyces cerevisiae/metabolism , rab GTP-Binding Proteins/metabolism , Animals , Cells, Cultured , Endoplasmic Reticulum/metabolism , Fluorescence , Green Fluorescent Proteins/metabolism , Guanine Nucleotide Dissociation Inhibitors/metabolism , HeLa Cells , Humans , Principal Component Analysis , Protein Transport , Recombinant Fusion Proteins/metabolism , Saccharomyces cerevisiae/cytology
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