The I-BAR protein Ivy1 is an effector of the Rab7 GTPase Ypt7 involved in vacuole membrane homeostasis.
Identifieur interne : 000B98 ( Main/Exploration ); précédent : 000B97; suivant : 000B99The I-BAR protein Ivy1 is an effector of the Rab7 GTPase Ypt7 involved in vacuole membrane homeostasis.
Auteurs : Johannes Numrich [Allemagne] ; Marie-Pierre Péli-Gulli [Suisse] ; Henning Arlt [Allemagne] ; Alessandro Sardu [Suisse] ; Janice Griffith [Pays-Bas] ; Tim Levine [Royaume-Uni] ; Siegfried Engelbrecht-Vandré [Allemagne] ; Fulvio Reggiori [Pays-Bas] ; Claudio De Virgilio [Suisse] ; Christian Ungermann [Allemagne]Source :
- Journal of cell science [ 1477-9137 ] ; 2015.
Descripteurs français
- KwdFr :
- Autophagie (MeSH), Complexe-1 cible mécanistique de la rapamycine (MeSH), Complexes multiprotéiques (MeSH), Endocytose (MeSH), Homéostasie (MeSH), Liaison aux protéines (MeSH), Membranes intracellulaires (métabolisme), Modèles biologiques (MeSH), Phosphatidyl inositols (métabolisme), Protéines G rab (métabolisme), Protéines de Saccharomyces cerevisiae (métabolisme), Protéines de transport (métabolisme), Saccharomyces cerevisiae (métabolisme), Saccharomyces cerevisiae (ultrastructure), Sérine-thréonine kinases TOR (MeSH), Transduction du signal (MeSH), Vacuoles (métabolisme), Vacuoles (ultrastructure).
- MESH :
- métabolisme : Membranes intracellulaires, Phosphatidyl inositols, Protéines G rab, Protéines de Saccharomyces cerevisiae, Protéines de transport, Saccharomyces cerevisiae, Vacuoles.
- ultrastructure : Autophagie, Complexe-1 cible mécanistique de la rapamycine, Complexes multiprotéiques, Endocytose, Homéostasie, Liaison aux protéines, Modèles biologiques, Saccharomyces cerevisiae, Sérine-thréonine kinases TOR, Transduction du signal, Vacuoles.
English descriptors
- KwdEn :
- Autophagy (MeSH), Carrier Proteins (metabolism), Endocytosis (MeSH), Homeostasis (MeSH), Intracellular Membranes (metabolism), Mechanistic Target of Rapamycin Complex 1 (MeSH), Models, Biological (MeSH), Multiprotein Complexes (MeSH), Phosphatidylinositols (metabolism), Protein Binding (MeSH), Saccharomyces cerevisiae (metabolism), Saccharomyces cerevisiae (ultrastructure), Saccharomyces cerevisiae Proteins (metabolism), Signal Transduction (MeSH), TOR Serine-Threonine Kinases (MeSH), Vacuoles (metabolism), Vacuoles (ultrastructure), rab GTP-Binding Proteins (metabolism).
- MESH :
- chemical , metabolism : Carrier Proteins, Phosphatidylinositols, Saccharomyces cerevisiae Proteins, rab GTP-Binding Proteins.
- metabolism : Intracellular Membranes, Saccharomyces cerevisiae, Vacuoles.
- ultrastructure : Saccharomyces cerevisiae, Vacuoles.
- Autophagy, Endocytosis, Homeostasis, Mechanistic Target of Rapamycin Complex 1, Models, Biological, Multiprotein Complexes, Protein Binding, Signal Transduction, TOR Serine-Threonine Kinases.
Abstract
Membrane fusion at the vacuole depends on a conserved machinery that includes SNAREs, the Rab7 homolog Ypt7 and its effector HOPS. Here, we demonstrate that Ypt7 has an unexpected additional function by controlling membrane homeostasis and nutrient-dependent signaling on the vacuole surface. We show that Ivy1, the yeast homolog of mammalian missing-in-metastasis (MIM), is a vacuolar effector of Ypt7-GTP and interacts with the EGO/ragulator complex, an activator of the target of rapamycin kinase complex 1 (TORC1) on vacuoles. Loss of Ivy1 does not affect EGO vacuolar localization and function. In combination with the deletion of individual subunits of the V-ATPase, however, we observed reduced TORC1 activity and massive enlargement of the vacuole surface. Consistent with this, Ivy1 localizes to invaginations at the vacuole surface and on liposomes in a phosphoinositide- and Ypt7-GTP-controlled manner, which suggests a role in microautophagy. Our data, thus, reveal that Ivy1 is a novel regulator of vacuole membrane homeostasis with connections to TORC1 signaling.
DOI: 10.1242/jcs.164905
PubMed: 25999476
Affiliations:
- Allemagne, Pays-Bas, Royaume-Uni, Suisse
- Basse-Saxe, Canton de Fribourg
- Fribourg, Osnabrück
- Université de Fribourg
Links toward previous steps (curation, corpus...)
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Germany.</nlm:affiliation><country xml:lang="fr">Allemagne</country><wicri:regionArea>University of Osnabrück, Department of Biology/Chemistry, Biochemistry section, Barbarastrasse 13, 49076 Osnabrück</wicri:regionArea><placeName><region type="land" nuts="2">Basse-Saxe</region><settlement type="city">Osnabrück</settlement></placeName></affiliation></author><author><name sortKey="Peli Gulli, Marie Pierre" sort="Peli Gulli, Marie Pierre" uniqKey="Peli Gulli M" first="Marie-Pierre" last="Péli-Gulli">Marie-Pierre Péli-Gulli</name><affiliation wicri:level="4"><nlm:affiliation>University of Fribourg, Department of Biology, Division of Biochemistry, Chemin du Musée 10, Fribourg CH-1700, Switzerland.</nlm:affiliation><country xml:lang="fr">Suisse</country><wicri:regionArea>University of Fribourg, Department of Biology, Division of Biochemistry, Chemin du Musée 10, Fribourg CH-1700</wicri:regionArea><orgName type="university">Université de Fribourg</orgName><placeName><settlement type="city">Fribourg</settlement><region nuts="3" type="region">Canton de Fribourg</region></placeName></affiliation></author><author><name sortKey="Arlt, Henning" sort="Arlt, Henning" uniqKey="Arlt H" first="Henning" last="Arlt">Henning Arlt</name><affiliation wicri:level="3"><nlm:affiliation>University of Osnabrück, Department of Biology/Chemistry, Biochemistry section, Barbarastrasse 13, 49076 Osnabrück, Germany.</nlm:affiliation><country xml:lang="fr">Allemagne</country><wicri:regionArea>University of Osnabrück, Department of Biology/Chemistry, Biochemistry section, Barbarastrasse 13, 49076 Osnabrück</wicri:regionArea><placeName><region type="land" nuts="2">Basse-Saxe</region><settlement type="city">Osnabrück</settlement></placeName></affiliation></author><author><name sortKey="Sardu, Alessandro" sort="Sardu, Alessandro" uniqKey="Sardu A" first="Alessandro" last="Sardu">Alessandro Sardu</name><affiliation wicri:level="4"><nlm:affiliation>University of Fribourg, Department of Biology, Division of Biochemistry, Chemin du Musée 10, Fribourg CH-1700, Switzerland.</nlm:affiliation><country xml:lang="fr">Suisse</country><wicri:regionArea>University of Fribourg, Department of Biology, Division of Biochemistry, Chemin du Musée 10, Fribourg CH-1700</wicri:regionArea><orgName type="university">Université de Fribourg</orgName><placeName><settlement type="city">Fribourg</settlement><region nuts="3" type="region">Canton de Fribourg</region></placeName></affiliation></author><author><name sortKey="Griffith, Janice" sort="Griffith, Janice" uniqKey="Griffith J" first="Janice" last="Griffith">Janice Griffith</name><affiliation wicri:level="1"><nlm:affiliation>University Medical Centre Utrecht, Center for Molecular Medicine, Department of Cell Biology, Heidelberglaan 100, Utrecht 3584 CX, The Netherlands.</nlm:affiliation><country xml:lang="fr">Pays-Bas</country><wicri:regionArea>University Medical Centre Utrecht, Center for Molecular Medicine, Department of Cell Biology, Heidelberglaan 100, Utrecht 3584 CX</wicri:regionArea><wicri:noRegion>Utrecht 3584 CX</wicri:noRegion></affiliation></author><author><name sortKey="Levine, Tim" sort="Levine, Tim" uniqKey="Levine T" first="Tim" last="Levine">Tim Levine</name><affiliation wicri:level="1"><nlm:affiliation>UCL Institute of Ophthalmology, Department of Cell Biology, 11-43 Bath St., London EC1V 9EL, UK.</nlm:affiliation><country xml:lang="fr">Royaume-Uni</country><wicri:regionArea>UCL Institute of Ophthalmology, Department of Cell Biology, 11-43 Bath St., London EC1V 9EL</wicri:regionArea><wicri:noRegion>London EC1V 9EL</wicri:noRegion></affiliation></author><author><name sortKey="Engelbrecht Vandre, Siegfried" sort="Engelbrecht Vandre, Siegfried" uniqKey="Engelbrecht Vandre S" first="Siegfried" last="Engelbrecht-Vandré">Siegfried Engelbrecht-Vandré</name><affiliation wicri:level="3"><nlm:affiliation>University of Osnabrück, Department of Biology/Chemistry, Biochemistry section, Barbarastrasse 13, 49076 Osnabrück, Germany.</nlm:affiliation><country xml:lang="fr">Allemagne</country><wicri:regionArea>University of Osnabrück, Department of Biology/Chemistry, Biochemistry section, Barbarastrasse 13, 49076 Osnabrück</wicri:regionArea><placeName><region type="land" nuts="2">Basse-Saxe</region><settlement type="city">Osnabrück</settlement></placeName></affiliation></author><author><name sortKey="Reggiori, Fulvio" sort="Reggiori, Fulvio" uniqKey="Reggiori F" first="Fulvio" last="Reggiori">Fulvio Reggiori</name><affiliation wicri:level="1"><nlm:affiliation>University Medical Centre Utrecht, Center for Molecular Medicine, Department of Cell Biology, Heidelberglaan 100, Utrecht 3584 CX, The Netherlands.</nlm:affiliation><country xml:lang="fr">Pays-Bas</country><wicri:regionArea>University Medical Centre Utrecht, Center for Molecular Medicine, Department of Cell Biology, Heidelberglaan 100, Utrecht 3584 CX</wicri:regionArea><wicri:noRegion>Utrecht 3584 CX</wicri:noRegion></affiliation></author><author><name sortKey="De Virgilio, Claudio" sort="De Virgilio, Claudio" uniqKey="De Virgilio C" first="Claudio" last="De Virgilio">Claudio De Virgilio</name><affiliation wicri:level="4"><nlm:affiliation>University of Fribourg, Department of Biology, Division of Biochemistry, Chemin du Musée 10, Fribourg CH-1700, Switzerland.</nlm:affiliation><country xml:lang="fr">Suisse</country><wicri:regionArea>University of Fribourg, Department of Biology, Division of Biochemistry, Chemin du Musée 10, Fribourg CH-1700</wicri:regionArea><orgName type="university">Université de Fribourg</orgName><placeName><settlement type="city">Fribourg</settlement><region nuts="3" type="region">Canton de Fribourg</region></placeName></affiliation></author><author><name sortKey="Ungermann, Christian" sort="Ungermann, Christian" uniqKey="Ungermann C" first="Christian" last="Ungermann">Christian Ungermann</name><affiliation wicri:level="3"><nlm:affiliation>University of Osnabrück, Department of Biology/Chemistry, Biochemistry section, Barbarastrasse 13, 49076 Osnabrück, Germany cu@uos.de.</nlm:affiliation><country wicri:rule="url">Allemagne</country><wicri:regionArea>University of Osnabrück, Department of Biology/Chemistry, Biochemistry section, Barbarastrasse 13, 49076 Osnabrück</wicri:regionArea><placeName><region type="land" nuts="2">Basse-Saxe</region><settlement type="city">Osnabrück</settlement></placeName></affiliation></author></analytic><series><title level="j">Journal of cell science</title><idno type="eISSN">1477-9137</idno><imprint><date when="2015" type="published">2015</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Autophagy (MeSH)</term><term>Carrier Proteins (metabolism)</term><term>Endocytosis (MeSH)</term><term>Homeostasis (MeSH)</term><term>Intracellular Membranes (metabolism)</term><term>Mechanistic Target of Rapamycin Complex 1 (MeSH)</term><term>Models, Biological (MeSH)</term><term>Multiprotein Complexes (MeSH)</term><term>Phosphatidylinositols (metabolism)</term><term>Protein Binding (MeSH)</term><term>Saccharomyces cerevisiae (metabolism)</term><term>Saccharomyces cerevisiae (ultrastructure)</term><term>Saccharomyces cerevisiae Proteins (metabolism)</term><term>Signal Transduction (MeSH)</term><term>TOR Serine-Threonine Kinases (MeSH)</term><term>Vacuoles (metabolism)</term><term>Vacuoles (ultrastructure)</term><term>rab GTP-Binding Proteins (metabolism)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Autophagie (MeSH)</term><term>Complexe-1 cible mécanistique de la rapamycine (MeSH)</term><term>Complexes multiprotéiques (MeSH)</term><term>Endocytose (MeSH)</term><term>Homéostasie (MeSH)</term><term>Liaison aux protéines (MeSH)</term><term>Membranes intracellulaires (métabolisme)</term><term>Modèles biologiques (MeSH)</term><term>Phosphatidyl inositols (métabolisme)</term><term>Protéines G rab (métabolisme)</term><term>Protéines de Saccharomyces cerevisiae (métabolisme)</term><term>Protéines de transport (métabolisme)</term><term>Saccharomyces cerevisiae (métabolisme)</term><term>Saccharomyces cerevisiae (ultrastructure)</term><term>Sérine-thréonine kinases TOR (MeSH)</term><term>Transduction du signal (MeSH)</term><term>Vacuoles (métabolisme)</term><term>Vacuoles (ultrastructure)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Carrier Proteins</term><term>Phosphatidylinositols</term><term>Saccharomyces cerevisiae Proteins</term><term>rab GTP-Binding Proteins</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Intracellular Membranes</term><term>Saccharomyces cerevisiae</term><term>Vacuoles</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Membranes intracellulaires</term><term>Phosphatidyl inositols</term><term>Protéines G rab</term><term>Protéines de Saccharomyces cerevisiae</term><term>Protéines de transport</term><term>Saccharomyces cerevisiae</term><term>Vacuoles</term></keywords><keywords scheme="MESH" qualifier="ultrastructure" xml:lang="en"><term>Saccharomyces cerevisiae</term><term>Vacuoles</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Autophagy</term><term>Endocytosis</term><term>Homeostasis</term><term>Mechanistic Target of Rapamycin Complex 1</term><term>Models, Biological</term><term>Multiprotein Complexes</term><term>Protein Binding</term><term>Signal Transduction</term><term>TOR Serine-Threonine Kinases</term></keywords><keywords scheme="MESH" qualifier="ultrastructure" xml:lang="fr"><term>Autophagie</term><term>Complexe-1 cible mécanistique de la rapamycine</term><term>Complexes multiprotéiques</term><term>Endocytose</term><term>Homéostasie</term><term>Liaison aux protéines</term><term>Modèles biologiques</term><term>Saccharomyces cerevisiae</term><term>Sérine-thréonine kinases TOR</term><term>Transduction du signal</term><term>Vacuoles</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Membrane fusion at the vacuole depends on a conserved machinery that includes SNAREs, the Rab7 homolog Ypt7 and its effector HOPS. Here, we demonstrate that Ypt7 has an unexpected additional function by controlling membrane homeostasis and nutrient-dependent signaling on the vacuole surface. We show that Ivy1, the yeast homolog of mammalian missing-in-metastasis (MIM), is a vacuolar effector of Ypt7-GTP and interacts with the EGO/ragulator complex, an activator of the target of rapamycin kinase complex 1 (TORC1) on vacuoles. Loss of Ivy1 does not affect EGO vacuolar localization and function. In combination with the deletion of individual subunits of the V-ATPase, however, we observed reduced TORC1 activity and massive enlargement of the vacuole surface. Consistent with this, Ivy1 localizes to invaginations at the vacuole surface and on liposomes in a phosphoinositide- and Ypt7-GTP-controlled manner, which suggests a role in microautophagy. Our data, thus, reveal that Ivy1 is a novel regulator of vacuole membrane homeostasis with connections to TORC1 signaling. </div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">25999476</PMID><DateCompleted><Year>2016</Year><Month>03</Month><Day>27</Day></DateCompleted><DateRevised><Year>2017</Year><Month>11</Month><Day>16</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1477-9137</ISSN><JournalIssue CitedMedium="Internet"><Volume>128</Volume><Issue>13</Issue><PubDate><Year>2015</Year><Month>Jul</Month><Day>01</Day></PubDate></JournalIssue><Title>Journal of cell science</Title><ISOAbbreviation>J Cell Sci</ISOAbbreviation></Journal><ArticleTitle>The I-BAR protein Ivy1 is an effector of the Rab7 GTPase Ypt7 involved in vacuole membrane homeostasis.</ArticleTitle><Pagination><MedlinePgn>2278-92</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1242/jcs.164905</ELocationID><Abstract><AbstractText>Membrane fusion at the vacuole depends on a conserved machinery that includes SNAREs, the Rab7 homolog Ypt7 and its effector HOPS. Here, we demonstrate that Ypt7 has an unexpected additional function by controlling membrane homeostasis and nutrient-dependent signaling on the vacuole surface. We show that Ivy1, the yeast homolog of mammalian missing-in-metastasis (MIM), is a vacuolar effector of Ypt7-GTP and interacts with the EGO/ragulator complex, an activator of the target of rapamycin kinase complex 1 (TORC1) on vacuoles. Loss of Ivy1 does not affect EGO vacuolar localization and function. In combination with the deletion of individual subunits of the V-ATPase, however, we observed reduced TORC1 activity and massive enlargement of the vacuole surface. Consistent with this, Ivy1 localizes to invaginations at the vacuole surface and on liposomes in a phosphoinositide- and Ypt7-GTP-controlled manner, which suggests a role in microautophagy. Our data, thus, reveal that Ivy1 is a novel regulator of vacuole membrane homeostasis with connections to TORC1 signaling. </AbstractText><CopyrightInformation>© 2015. Published by The Company of Biologists Ltd.</CopyrightInformation></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Numrich</LastName><ForeName>Johannes</ForeName><Initials>J</Initials><AffiliationInfo><Affiliation>University of Osnabrück, Department of Biology/Chemistry, Biochemistry section, Barbarastrasse 13, 49076 Osnabrück, Germany.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Péli-Gulli</LastName><ForeName>Marie-Pierre</ForeName><Initials>MP</Initials><AffiliationInfo><Affiliation>University of Fribourg, Department of Biology, Division of Biochemistry, Chemin du Musée 10, Fribourg CH-1700, Switzerland.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Arlt</LastName><ForeName>Henning</ForeName><Initials>H</Initials><AffiliationInfo><Affiliation>University of Osnabrück, Department of Biology/Chemistry, Biochemistry section, Barbarastrasse 13, 49076 Osnabrück, Germany.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Sardu</LastName><ForeName>Alessandro</ForeName><Initials>A</Initials><AffiliationInfo><Affiliation>University of Fribourg, Department of Biology, Division of Biochemistry, Chemin du Musée 10, Fribourg CH-1700, Switzerland.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Griffith</LastName><ForeName>Janice</ForeName><Initials>J</Initials><AffiliationInfo><Affiliation>University Medical Centre Utrecht, Center for Molecular Medicine, Department of Cell Biology, Heidelberglaan 100, Utrecht 3584 CX, The Netherlands.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Levine</LastName><ForeName>Tim</ForeName><Initials>T</Initials><AffiliationInfo><Affiliation>UCL Institute of Ophthalmology, Department of Cell Biology, 11-43 Bath St., London EC1V 9EL, UK.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Engelbrecht-Vandré</LastName><ForeName>Siegfried</ForeName><Initials>S</Initials><AffiliationInfo><Affiliation>University of Osnabrück, Department of Biology/Chemistry, Biochemistry section, Barbarastrasse 13, 49076 Osnabrück, Germany.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Reggiori</LastName><ForeName>Fulvio</ForeName><Initials>F</Initials><AffiliationInfo><Affiliation>University Medical Centre Utrecht, Center for Molecular Medicine, Department of Cell Biology, Heidelberglaan 100, Utrecht 3584 CX, The Netherlands.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>De Virgilio</LastName><ForeName>Claudio</ForeName><Initials>C</Initials><AffiliationInfo><Affiliation>University of Fribourg, Department of Biology, Division of Biochemistry, Chemin du Musée 10, Fribourg CH-1700, Switzerland.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Ungermann</LastName><ForeName>Christian</ForeName><Initials>C</Initials><AffiliationInfo><Affiliation>University of Osnabrück, Department of Biology/Chemistry, Biochemistry section, Barbarastrasse 13, 49076 Osnabrück, Germany cu@uos.de.</Affiliation></AffiliationInfo></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2015</Year><Month>05</Month><Day>21</Day></ArticleDate></Article><MedlineJournalInfo><Country>England</Country><MedlineTA>J Cell Sci</MedlineTA><NlmUniqueID>0052457</NlmUniqueID><ISSNLinking>0021-9533</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D002352">Carrier Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="C475841">IVY1 protein, S cerevisiae</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D046912">Multiprotein Complexes</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D010716">Phosphatidylinositols</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D029701">Saccharomyces cerevisiae Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 2.7.1.1</RegistryNumber><NameOfSubstance UI="D058570">TOR Serine-Threonine Kinases</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 2.7.11.1</RegistryNumber><NameOfSubstance UI="D000076222">Mechanistic Target of Rapamycin Complex 1</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 3.6.1.-</RegistryNumber><NameOfSubstance UI="C079005">YPT7 protein, S cerevisiae</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 3.6.5.2</RegistryNumber><NameOfSubstance UI="D020691">rab GTP-Binding Proteins</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D001343" MajorTopicYN="N">Autophagy</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D002352" MajorTopicYN="N">Carrier Proteins</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D004705" MajorTopicYN="N">Endocytosis</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D006706" MajorTopicYN="Y">Homeostasis</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D007425" MajorTopicYN="N">Intracellular Membranes</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D000076222" MajorTopicYN="N">Mechanistic Target of Rapamycin Complex 1</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D008954" MajorTopicYN="N">Models, Biological</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D046912" MajorTopicYN="N">Multiprotein Complexes</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D010716" MajorTopicYN="N">Phosphatidylinositols</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D011485" MajorTopicYN="N">Protein Binding</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D012441" MajorTopicYN="N">Saccharomyces cerevisiae</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName><QualifierName UI="Q000648" MajorTopicYN="N">ultrastructure</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D029701" MajorTopicYN="N">Saccharomyces cerevisiae Proteins</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D015398" MajorTopicYN="N">Signal Transduction</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D058570" MajorTopicYN="N">TOR Serine-Threonine Kinases</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D014617" MajorTopicYN="N">Vacuoles</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName><QualifierName UI="Q000648" MajorTopicYN="N">ultrastructure</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D020691" MajorTopicYN="N">rab GTP-Binding Proteins</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading></MeshHeadingList><KeywordList Owner="NOTNLM"><Keyword MajorTopicYN="N">EGO complex</Keyword><Keyword MajorTopicYN="N">Ivy1</Keyword><Keyword MajorTopicYN="N">TORC1</Keyword><Keyword MajorTopicYN="N">Vacuole biogenesis</Keyword><Keyword MajorTopicYN="N">Vps33</Keyword><Keyword MajorTopicYN="N">Ypt7</Keyword></KeywordList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="received"><Year>2014</Year><Month>10</Month><Day>22</Day></PubMedPubDate><PubMedPubDate PubStatus="accepted"><Year>2015</Year><Month>05</Month><Day>18</Day></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2015</Year><Month>5</Month><Day>23</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2015</Year><Month>5</Month><Day>23</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2016</Year><Month>3</Month><Day>28</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">25999476</ArticleId><ArticleId IdType="pii">jcs.164905</ArticleId><ArticleId IdType="doi">10.1242/jcs.164905</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>Allemagne</li><li>Pays-Bas</li><li>Royaume-Uni</li><li>Suisse</li></country><region><li>Basse-Saxe</li><li>Canton de Fribourg</li></region><settlement><li>Fribourg</li><li>Osnabrück</li></settlement><orgName><li>Université de Fribourg</li></orgName></list><tree><country name="Allemagne"><region name="Basse-Saxe"><name sortKey="Numrich, Johannes" sort="Numrich, Johannes" uniqKey="Numrich J" first="Johannes" last="Numrich">Johannes Numrich</name></region><name sortKey="Arlt, Henning" sort="Arlt, Henning" uniqKey="Arlt H" first="Henning" last="Arlt">Henning Arlt</name><name sortKey="Engelbrecht Vandre, Siegfried" sort="Engelbrecht Vandre, Siegfried" uniqKey="Engelbrecht Vandre S" first="Siegfried" last="Engelbrecht-Vandré">Siegfried Engelbrecht-Vandré</name><name sortKey="Ungermann, Christian" sort="Ungermann, Christian" uniqKey="Ungermann C" first="Christian" last="Ungermann">Christian Ungermann</name></country><country name="Suisse"><region name="Canton de Fribourg"><name sortKey="Peli Gulli, Marie Pierre" sort="Peli Gulli, Marie Pierre" uniqKey="Peli Gulli M" first="Marie-Pierre" last="Péli-Gulli">Marie-Pierre Péli-Gulli</name></region><name sortKey="De Virgilio, Claudio" sort="De Virgilio, Claudio" uniqKey="De Virgilio C" first="Claudio" last="De Virgilio">Claudio De Virgilio</name><name sortKey="Sardu, Alessandro" sort="Sardu, Alessandro" uniqKey="Sardu A" first="Alessandro" last="Sardu">Alessandro Sardu</name></country><country name="Pays-Bas"><noRegion><name sortKey="Griffith, Janice" sort="Griffith, Janice" uniqKey="Griffith J" first="Janice" last="Griffith">Janice Griffith</name></noRegion><name sortKey="Reggiori, Fulvio" sort="Reggiori, Fulvio" uniqKey="Reggiori F" first="Fulvio" last="Reggiori">Fulvio Reggiori</name></country><country name="Royaume-Uni"><noRegion><name sortKey="Levine, Tim" sort="Levine, Tim" uniqKey="Levine T" first="Tim" last="Levine">Tim Levine</name></noRegion></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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