dc.contributor.author | Clay, L | en_US |
dc.contributor.author | Caudron, F | en_US |
dc.contributor.author | Denoth-Lippuner, A | en_US |
dc.contributor.author | Boettcher, B | en_US |
dc.contributor.author | Buvelot Frei, S | en_US |
dc.contributor.author | Snapp, EL | en_US |
dc.contributor.author | Barral, Y | en_US |
dc.date.accessioned | 2018-01-19T13:52:08Z | |
dc.date.available | 2014-04-08 | en_US |
dc.date.issued | 2014-05-06 | en_US |
dc.date.submitted | 2017-12-19T14:38:07.236Z | |
dc.identifier.uri | http://qmro.qmul.ac.uk/xmlui/handle/123456789/31435 | |
dc.description.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. | en_US |
dc.format.extent | e01883 - ? | en_US |
dc.language | eng | en_US |
dc.relation.ispartof | Elife | en_US |
dc.rights | This article is distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use and redistribution provided that the original author and source are credited. | |
dc.subject | ER stress | en_US |
dc.subject | aging | en_US |
dc.subject | asymmetric cell division | en_US |
dc.subject | diffusion barrier | en_US |
dc.subject | sphingolipids | en_US |
dc.subject | Cell Cycle Proteins | en_US |
dc.subject | Cell Division | en_US |
dc.subject | Diffusion | en_US |
dc.subject | Endoplasmic Reticulum | en_US |
dc.subject | Endoplasmic Reticulum Stress | en_US |
dc.subject | Guanine Nucleotide Exchange Factors | en_US |
dc.subject | Intracellular Membranes | en_US |
dc.subject | Microfilament Proteins | en_US |
dc.subject | Nuclear Envelope | en_US |
dc.subject | Permeability | en_US |
dc.subject | Protein Folding | en_US |
dc.subject | Saccharomyces cerevisiae | en_US |
dc.subject | Saccharomyces cerevisiae Proteins | en_US |
dc.subject | Septins | en_US |
dc.subject | Sphingolipids | en_US |
dc.subject | Time Factors | en_US |
dc.subject | rab GTP-Binding Proteins | en_US |
dc.title | A sphingolipid-dependent diffusion barrier confines ER stress to the yeast mother cell. | en_US |
dc.type | Article | |
dc.rights.holder | © 2014 Copyright Clay et al. | |
dc.identifier.doi | 10.7554/eLife.01883 | en_US |
pubs.author-url | https://www.ncbi.nlm.nih.gov/pubmed/24843009 | en_US |
pubs.notes | Not known | en_US |
pubs.publication-status | Published online | en_US |
pubs.volume | 3 | en_US |