RapamycinFungusV1, Main, Exploration, bibRecord, 000C04

Target of rapamycin signaling mediates vacuolar fission caused by endoplasmic reticulum stress in Saccharomyces cerevisiae.

Identifieur interne : 000C04 ( Main/Exploration ); précédent : 000C03; suivant : 000C05

Target of rapamycin signaling mediates vacuolar fission caused by endoplasmic reticulum stress in Saccharomyces cerevisiae.

Auteurs : Bobbiejane Stauffer [États-Unis] ; Ted Powers [États-Unis]

Source :

Molecular biology of the cell [ 1939-4586 ] ; 2015.

RBID : pubmed:26466677

Descripteurs français

English descriptors

Abstract

The yeast vacuole is equivalent to the mammalian lysosome and, in response to diverse physiological and environmental stimuli, undergoes alterations both in size and number. Here we demonstrate that vacuoles fragment in response to stress within the endoplasmic reticulum (ER) caused by chemical or genetic perturbations. We establish that this response does not involve known signaling pathways linked previously to ER stress but instead requires the rapamycin-sensitive TOR Complex 1 (TORC1), a master regulator of cell growth, together with its downstream effectors, Tap42/Sit4 and Sch9. To identify additional factors required for ER stress-induced vacuolar fragmentation, we conducted a high-throughput, genome-wide visual screen for yeast mutants that are refractory to ER stress-induced changes in vacuolar morphology. We identified several genes shown previously to be required for vacuolar fusion and/or fission, validating the utility of this approach. We also identified a number of new components important for fragmentation, including a set of proteins involved in assembly of the V-ATPase. Remarkably, we find that one of these, Vph2, undergoes a change in intracellular localization in response to ER stress and, moreover, in a manner that requires TORC1 activity. Together these results reveal a new role for TORC1 in the regulation of vacuolar behavior.

DOI: 10.1091/mbc.E15-06-0344
PubMed: 26466677
PubMed Central: PMC4678019

Affiliations:

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Le document en format XML

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<term>Cell Proliferation (genetics)</term>
<term>Endoplasmic Reticulum (genetics)</term>
<term>Endoplasmic Reticulum Stress (genetics)</term>
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<term>Membrane Proteins (metabolism)</term>
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<term>Molecular Chaperones (metabolism)</term>
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<term>Protein-Serine-Threonine Kinases (metabolism)</term>
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<term>Saccharomyces cerevisiae Proteins (genetics)</term>
<term>Saccharomyces cerevisiae Proteins (metabolism)</term>
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<term>Transcription Factors (genetics)</term>
<term>Transcription Factors (metabolism)</term>
<term>Vacuoles (genetics)</term>
<term>Vacuoles (metabolism)</term>
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<term>Chaperons moléculaires (métabolisme)</term>
<term>Facteurs de transcription (génétique)</term>
<term>Facteurs de transcription (métabolisme)</term>
<term>Prolifération cellulaire (génétique)</term>
<term>Protein-Serine-Threonine Kinases (génétique)</term>
<term>Protein-Serine-Threonine Kinases (métabolisme)</term>
<term>Protéines adaptatrices de la transduction du signal (génétique)</term>
<term>Protéines adaptatrices de la transduction du signal (métabolisme)</term>
<term>Protéines de Saccharomyces cerevisiae (génétique)</term>
<term>Protéines de Saccharomyces cerevisiae (métabolisme)</term>
<term>Protéines membranaires (génétique)</term>
<term>Protéines membranaires (métabolisme)</term>
<term>Réticulum endoplasmique (génétique)</term>
<term>Saccharomyces cerevisiae (génétique)</term>
<term>Stress du réticulum endoplasmique (génétique)</term>
<term>Transduction du signal (MeSH)</term>
<term>Vacuoles (génétique)</term>
<term>Vacuoles (métabolisme)</term>
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<term>Membrane Proteins</term>
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<term>Protein-Serine-Threonine Kinases</term>
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<term>Saccharomyces cerevisiae</term>
<term>Vacuoles</term>
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<front><div type="abstract" xml:lang="en">The yeast vacuole is equivalent to the mammalian lysosome and, in response to diverse physiological and environmental stimuli, undergoes alterations both in size and number. Here we demonstrate that vacuoles fragment in response to stress within the endoplasmic reticulum (ER) caused by chemical or genetic perturbations. We establish that this response does not involve known signaling pathways linked previously to ER stress but instead requires the rapamycin-sensitive TOR Complex 1 (TORC1), a master regulator of cell growth, together with its downstream effectors, Tap42/Sit4 and Sch9. To identify additional factors required for ER stress-induced vacuolar fragmentation, we conducted a high-throughput, genome-wide visual screen for yeast mutants that are refractory to ER stress-induced changes in vacuolar morphology. We identified several genes shown previously to be required for vacuolar fusion and/or fission, validating the utility of this approach. We also identified a number of new components important for fragmentation, including a set of proteins involved in assembly of the V-ATPase. Remarkably, we find that one of these, Vph2, undergoes a change in intracellular localization in response to ER stress and, moreover, in a manner that requires TORC1 activity. Together these results reveal a new role for TORC1 in the regulation of vacuolar behavior. </div>
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Target of rapamycin signaling mediates vacuolar fission caused by endoplasmic reticulum stress in Saccharomyces cerevisiae.

Target of rapamycin signaling mediates vacuolar fission caused by endoplasmic reticulum stress in Saccharomyces cerevisiae.

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