Cell-free reconstitution of vacuole membrane fragmentation reveals regulation of vacuole size and number by TORC1.
Identifieur interne : 001209 ( Main/Exploration ); précédent : 001208; suivant : 001210Cell-free reconstitution of vacuole membrane fragmentation reveals regulation of vacuole size and number by TORC1.
Auteurs : Lydie Michaillat [Suisse] ; Tonie Luise Baars ; Andreas MayerSource :
- Molecular biology of the cell [ 1939-4586 ] ; 2012.
Descripteurs français
- KwdFr :
- Facteurs de transcription (antagonistes et inhibiteurs), Facteurs de transcription (métabolisme), Fusion membranaire (MeSH), Guanosine triphosphate (composition chimique), Guanosine triphosphate (métabolisme), Hydrolyse (MeSH), Membranes intracellulaires (métabolisme), Membranes intracellulaires (ultrastructure), Protein Phosphatase 2 (métabolisme), Protéines G (métabolisme), Protéines de Saccharomyces cerevisiae (antagonistes et inhibiteurs), Protéines de Saccharomyces cerevisiae (métabolisme), Protéines du transport vésiculaire (métabolisme), Saccharomyces cerevisiae (composition chimique), Saccharomyces cerevisiae (métabolisme), Saccharomyces cerevisiae (physiologie), Sirolimus (pharmacologie), Système acellulaire (composition chimique), Vacuoles (composition chimique), Vacuoles (métabolisme), Vacuoles (ultrastructure).
- MESH :
- antagonistes et inhibiteurs : Facteurs de transcription, Protéines de Saccharomyces cerevisiae.
- composition chimique : Guanosine triphosphate, Saccharomyces cerevisiae, Système acellulaire, Vacuoles.
- métabolisme : Facteurs de transcription, Guanosine triphosphate, Membranes intracellulaires, Protein Phosphatase 2, Protéines G, Protéines de Saccharomyces cerevisiae, Protéines du transport vésiculaire, Saccharomyces cerevisiae, Vacuoles.
- pharmacologie : Sirolimus.
- physiologie : Saccharomyces cerevisiae.
- ultrastructure : Fusion membranaire, Hydrolyse, Membranes intracellulaires, Vacuoles.
English descriptors
- KwdEn :
- Cell-Free System (chemistry), GTP-Binding Proteins (metabolism), Guanosine Triphosphate (chemistry), Guanosine Triphosphate (metabolism), Hydrolysis (MeSH), Intracellular Membranes (metabolism), Intracellular Membranes (ultrastructure), Membrane Fusion (MeSH), Protein Phosphatase 2 (metabolism), Saccharomyces cerevisiae (chemistry), Saccharomyces cerevisiae (metabolism), Saccharomyces cerevisiae (physiology), Saccharomyces cerevisiae Proteins (antagonists & inhibitors), Saccharomyces cerevisiae Proteins (metabolism), Sirolimus (pharmacology), Transcription Factors (antagonists & inhibitors), Transcription Factors (metabolism), Vacuoles (chemistry), Vacuoles (metabolism), Vacuoles (ultrastructure), Vesicular Transport Proteins (metabolism).
- MESH :
- chemical , antagonists & inhibitors : Saccharomyces cerevisiae Proteins, Transcription Factors.
- chemical , chemistry : Guanosine Triphosphate.
- chemical , metabolism : GTP-Binding Proteins, Guanosine Triphosphate, Protein Phosphatase 2, Saccharomyces cerevisiae Proteins, Transcription Factors, Vesicular Transport Proteins.
- chemistry : Cell-Free System, Saccharomyces cerevisiae, Vacuoles.
- metabolism : Intracellular Membranes, Saccharomyces cerevisiae, Vacuoles.
- chemical , pharmacology : Sirolimus.
- physiology : Saccharomyces cerevisiae.
- ultrastructure : Intracellular Membranes, Vacuoles.
- Hydrolysis, Membrane Fusion.
Abstract
Size and copy number of organelles are influenced by an equilibrium of membrane fusion and fission. We studied this equilibrium on vacuoles-the lysosomes of yeast. Vacuole fusion can readily be reconstituted and quantified in vitro, but it had not been possible to study fission of the organelle in a similar way. Here we present a cell-free system that reconstitutes fragmentation of purified yeast vacuoles (lysosomes) into smaller vesicles. Fragmentation in vitro reproduces physiological aspects. It requires the dynamin-like GTPase Vps1p, V-ATPase pump activity, cytosolic proteins, and ATP and GTP hydrolysis. We used the in vitro system to show that the vacuole-associated TOR complex 1 (TORC1) stimulates vacuole fragmentation but not the opposing reaction of vacuole fusion. Under nutrient restriction, TORC1 is inactivated, and the continuing fusion activity then dominates the fusion/fission equilibrium, decreasing the copy number and increasing the volume of the vacuolar compartment. This result can explain why nutrient restriction not only induces autophagy and a massive buildup of vacuolar/lysosomal hydrolases, but also leads to a concomitant increase in volume of the vacuolar compartment by coalescence of the organelles into a single large compartment.
DOI: 10.1091/mbc.E11-08-0703
PubMed: 22238359
PubMed Central: PMC3290646
Affiliations:
Links toward previous steps (curation, corpus...)
Le document en format XML
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of organelles are influenced by an equilibrium of membrane fusion and fission. We studied this equilibrium on vacuoles-the lysosomes of yeast. Vacuole fusion can readily be reconstituted and quantified in vitro, but it had not been possible to study fission of the organelle in a similar way. Here we present a cell-free system that reconstitutes fragmentation of purified yeast vacuoles (lysosomes) into smaller vesicles. Fragmentation in vitro reproduces physiological aspects. It requires the dynamin-like GTPase Vps1p, V-ATPase pump activity, cytosolic proteins, and ATP and GTP hydrolysis. We used the in vitro system to show that the vacuole-associated TOR complex 1 (TORC1) stimulates vacuole fragmentation but not the opposing reaction of vacuole fusion. Under nutrient restriction, TORC1 is inactivated, and the continuing fusion activity then dominates the fusion/fission equilibrium, decreasing the copy number and increasing the volume of the vacuolar compartment. This result can explain why nutrient restriction not only induces autophagy and a massive buildup of vacuolar/lysosomal hydrolases, but also leads to a concomitant increase in volume of the vacuolar compartment by coalescence of the organelles into a single large compartment.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">22238359</PMID><DateCompleted><Year>2012</Year><Month>07</Month><Day>23</Day></DateCompleted><DateRevised><Year>2018</Year><Month>11</Month><Day>13</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1939-4586</ISSN><JournalIssue CitedMedium="Internet"><Volume>23</Volume><Issue>5</Issue><PubDate><Year>2012</Year><Month>Mar</Month></PubDate></JournalIssue><Title>Molecular biology of the cell</Title><ISOAbbreviation>Mol Biol Cell</ISOAbbreviation></Journal><ArticleTitle>Cell-free reconstitution of vacuole membrane fragmentation reveals regulation of vacuole size and number by TORC1.</ArticleTitle><Pagination><MedlinePgn>881-95</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1091/mbc.E11-08-0703</ELocationID><Abstract><AbstractText>Size and copy number of organelles are influenced by an equilibrium of membrane fusion and fission. We studied this equilibrium on vacuoles-the lysosomes of yeast. Vacuole fusion can readily be reconstituted and quantified in vitro, but it had not been possible to study fission of the organelle in a similar way. Here we present a cell-free system that reconstitutes fragmentation of purified yeast vacuoles (lysosomes) into smaller vesicles. Fragmentation in vitro reproduces physiological aspects. It requires the dynamin-like GTPase Vps1p, V-ATPase pump activity, cytosolic proteins, and ATP and GTP hydrolysis. We used the in vitro system to show that the vacuole-associated TOR complex 1 (TORC1) stimulates vacuole fragmentation but not the opposing reaction of vacuole fusion. Under nutrient restriction, TORC1 is inactivated, and the continuing fusion activity then dominates the fusion/fission equilibrium, decreasing the copy number and increasing the volume of the vacuolar compartment. This result can explain why nutrient restriction not only induces autophagy and a massive buildup of vacuolar/lysosomal hydrolases, but also leads to a concomitant increase in volume of the vacuolar compartment by coalescence of the organelles into a single large compartment.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Michaillat</LastName><ForeName>Lydie</ForeName><Initials>L</Initials><AffiliationInfo><Affiliation>Département de Biochimie, Université de Lausanne, 1066 Epalinges, Switzerland.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Baars</LastName><ForeName>Tonie Luise</ForeName><Initials>TL</Initials></Author><Author ValidYN="Y"><LastName>Mayer</LastName><ForeName>Andreas</ForeName><Initials>A</Initials></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. 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