RapamycinFungusV1, Main, Exploration, bibRecord, 000071

Phase separation organizes the site of autophagosome formation.

Identifieur interne : 000071 ( Main/Exploration ); précédent : 000070; suivant : 000072

Phase separation organizes the site of autophagosome formation.

Auteurs : Yuko Fujioka [Japon] ; Jahangir Md Alam [Japon] ; Daisuke Noshiro [Japon] ; Kazunari Mouri [Japon] ; Toshio Ando [Japon] ; Yasushi Okada [Japon] ; Alexander I. May [Japon] ; Roland L. Knorr [Allemagne, Japon] ; Kuninori Suzuki [Japon] ; Yoshinori Ohsumi [Japon] ; Nobuo N. Noda [Japon]

Source :

Nature [ 1476-4687 ] ; 2020.

RBID : pubmed:32025038

Descripteurs français

English descriptors

Abstract

Many biomolecules undergo liquid-liquid phase separation to form liquid-like condensates that mediate diverse cellular functions^1,2. Autophagy is able to degrade such condensates using autophagosomes-double-membrane structures that are synthesized de novo at the pre-autophagosomal structure (PAS) in yeast^3-5. Whereas Atg proteins that associate with the PAS have been characterized, the physicochemical and functional properties of the PAS remain unclear owing to its small size and fragility. Here we show that the PAS is in fact a liquid-like condensate of Atg proteins. The autophagy-initiating Atg1 complex undergoes phase separation to form liquid droplets in vitro, and point mutations or phosphorylation that inhibit phase separation impair PAS formation in vivo. In vitro experiments show that Atg1-complex droplets can be tethered to membranes via specific protein-protein interactions, explaining the vacuolar membrane localization of the PAS in vivo. We propose that phase separation has a critical, active role in autophagy, whereby it organizes the autophagy machinery at the PAS.

DOI: 10.1038/s41586-020-1977-6
PubMed: 32025038

Affiliations:

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Le document en format XML

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<author><name sortKey="Ohsumi, Yoshinori" sort="Ohsumi, Yoshinori" uniqKey="Ohsumi Y" first="Yoshinori" last="Ohsumi">Yoshinori Ohsumi</name>
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<author><name sortKey="Noda, Nobuo N" sort="Noda, Nobuo N" uniqKey="Noda N" first="Nobuo N" last="Noda">Nobuo N. Noda</name>
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<sourceDesc><biblStruct><analytic><title xml:lang="en">Phase separation organizes the site of autophagosome formation.</title>
<author><name sortKey="Fujioka, Yuko" sort="Fujioka, Yuko" uniqKey="Fujioka Y" first="Yuko" last="Fujioka">Yuko Fujioka</name>
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<author><name sortKey="Alam, Jahangir Md" sort="Alam, Jahangir Md" uniqKey="Alam J" first="Jahangir Md" last="Alam">Jahangir Md Alam</name>
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<author><name sortKey="Noshiro, Daisuke" sort="Noshiro, Daisuke" uniqKey="Noshiro D" first="Daisuke" last="Noshiro">Daisuke Noshiro</name>
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<author><name sortKey="Okada, Yasushi" sort="Okada, Yasushi" uniqKey="Okada Y" first="Yasushi" last="Okada">Yasushi Okada</name>
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<author><name sortKey="May, Alexander I" sort="May, Alexander I" uniqKey="May A" first="Alexander I" last="May">Alexander I. May</name>
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<country xml:lang="fr">Japon</country>
<wicri:regionArea>Cell Biology Center, Institute of Innovative Research, Tokyo Institute of Technology, Yokohama</wicri:regionArea>
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<affiliation wicri:level="1"><nlm:affiliation>Tokyo Tech World Research Hub Initiative (WRHI), Institute of Innovative Research, Tokyo Institute of Technology, Yokohama, Japan.</nlm:affiliation>
<country xml:lang="fr">Japon</country>
<wicri:regionArea>Tokyo Tech World Research Hub Initiative (WRHI), Institute of Innovative Research, Tokyo Institute of Technology, Yokohama</wicri:regionArea>
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<author><name sortKey="Knorr, Roland L" sort="Knorr, Roland L" uniqKey="Knorr R" first="Roland L" last="Knorr">Roland L. Knorr</name>
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<author><name sortKey="Suzuki, Kuninori" sort="Suzuki, Kuninori" uniqKey="Suzuki K" first="Kuninori" last="Suzuki">Kuninori Suzuki</name>
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<author><name sortKey="Ohsumi, Yoshinori" sort="Ohsumi, Yoshinori" uniqKey="Ohsumi Y" first="Yoshinori" last="Ohsumi">Yoshinori Ohsumi</name>
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<author><name sortKey="Noda, Nobuo N" sort="Noda, Nobuo N" uniqKey="Noda N" first="Nobuo N" last="Noda">Nobuo N. Noda</name>
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<country xml:lang="fr">Japon</country>
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<profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Adaptor Proteins, Signal Transducing (chemistry)</term>
<term>Adaptor Proteins, Signal Transducing (genetics)</term>
<term>Adaptor Proteins, Signal Transducing (metabolism)</term>
<term>Autophagosomes (chemistry)</term>
<term>Autophagosomes (metabolism)</term>
<term>Autophagy (MeSH)</term>
<term>Autophagy-Related Proteins (chemistry)</term>
<term>Autophagy-Related Proteins (genetics)</term>
<term>Autophagy-Related Proteins (metabolism)</term>
<term>Mechanistic Target of Rapamycin Complex 1 (chemistry)</term>
<term>Mechanistic Target of Rapamycin Complex 1 (metabolism)</term>
<term>Multiprotein Complexes (chemistry)</term>
<term>Multiprotein Complexes (genetics)</term>
<term>Multiprotein Complexes (metabolism)</term>
<term>Phosphorylation (MeSH)</term>
<term>Point Mutation (MeSH)</term>
<term>Protein Binding (MeSH)</term>
<term>Protein Kinases (chemistry)</term>
<term>Protein Kinases (genetics)</term>
<term>Protein Kinases (metabolism)</term>
<term>Saccharomyces cerevisiae (chemistry)</term>
<term>Saccharomyces cerevisiae (cytology)</term>
<term>Saccharomyces cerevisiae (genetics)</term>
<term>Saccharomyces cerevisiae (metabolism)</term>
<term>Saccharomyces cerevisiae Proteins (chemistry)</term>
<term>Saccharomyces cerevisiae Proteins (genetics)</term>
<term>Saccharomyces cerevisiae Proteins (metabolism)</term>
<term>Vacuoles (metabolism)</term>
</keywords>
<keywords scheme="KwdFr" xml:lang="fr"><term>Autophagie (MeSH)</term>
<term>Autophagosomes (composition chimique)</term>
<term>Autophagosomes (métabolisme)</term>
<term>Complexe-1 cible mécanistique de la rapamycine (composition chimique)</term>
<term>Complexe-1 cible mécanistique de la rapamycine (métabolisme)</term>
<term>Complexes multiprotéiques (composition chimique)</term>
<term>Complexes multiprotéiques (génétique)</term>
<term>Complexes multiprotéiques (métabolisme)</term>
<term>Liaison aux protéines (MeSH)</term>
<term>Mutation ponctuelle (MeSH)</term>
<term>Phosphorylation (MeSH)</term>
<term>Protein kinases (composition chimique)</term>
<term>Protein kinases (génétique)</term>
<term>Protein kinases (métabolisme)</term>
<term>Protéines adaptatrices de la transduction du signal (composition chimique)</term>
<term>Protéines adaptatrices de la transduction du signal (génétique)</term>
<term>Protéines adaptatrices de la transduction du signal (métabolisme)</term>
<term>Protéines associées à l'autophagie (composition chimique)</term>
<term>Protéines associées à l'autophagie (génétique)</term>
<term>Protéines associées à l'autophagie (métabolisme)</term>
<term>Protéines de Saccharomyces cerevisiae (composition chimique)</term>
<term>Protéines de Saccharomyces cerevisiae (génétique)</term>
<term>Protéines de Saccharomyces cerevisiae (métabolisme)</term>
<term>Saccharomyces cerevisiae (composition chimique)</term>
<term>Saccharomyces cerevisiae (cytologie)</term>
<term>Saccharomyces cerevisiae (génétique)</term>
<term>Saccharomyces cerevisiae (métabolisme)</term>
<term>Vacuoles (métabolisme)</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Adaptor Proteins, Signal Transducing</term>
<term>Autophagy-Related Proteins</term>
<term>Mechanistic Target of Rapamycin Complex 1</term>
<term>Multiprotein Complexes</term>
<term>Protein Kinases</term>
<term>Saccharomyces cerevisiae Proteins</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Adaptor Proteins, Signal Transducing</term>
<term>Autophagy-Related Proteins</term>
<term>Multiprotein Complexes</term>
<term>Protein Kinases</term>
<term>Saccharomyces cerevisiae Proteins</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Adaptor Proteins, Signal Transducing</term>
<term>Autophagy-Related Proteins</term>
<term>Mechanistic Target of Rapamycin Complex 1</term>
<term>Multiprotein Complexes</term>
<term>Protein Kinases</term>
<term>Saccharomyces cerevisiae Proteins</term>
</keywords>
<keywords scheme="MESH" qualifier="chemistry" xml:lang="en"><term>Autophagosomes</term>
<term>Saccharomyces cerevisiae</term>
</keywords>
<keywords scheme="MESH" qualifier="composition chimique" xml:lang="fr"><term>Autophagosomes</term>
<term>Complexe-1 cible mécanistique de la rapamycine</term>
<term>Complexes multiprotéiques</term>
<term>Protein kinases</term>
<term>Protéines adaptatrices de la transduction du signal</term>
<term>Protéines associées à l'autophagie</term>
<term>Protéines de Saccharomyces cerevisiae</term>
<term>Saccharomyces cerevisiae</term>
</keywords>
<keywords scheme="MESH" qualifier="cytologie" xml:lang="fr"><term>Saccharomyces cerevisiae</term>
</keywords>
<keywords scheme="MESH" qualifier="cytology" xml:lang="en"><term>Saccharomyces cerevisiae</term>
</keywords>
<keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Saccharomyces cerevisiae</term>
</keywords>
<keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Complexes multiprotéiques</term>
<term>Protein kinases</term>
<term>Protéines adaptatrices de la transduction du signal</term>
<term>Protéines associées à l'autophagie</term>
<term>Protéines de Saccharomyces cerevisiae</term>
<term>Saccharomyces cerevisiae</term>
</keywords>
<keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Autophagosomes</term>
<term>Saccharomyces cerevisiae</term>
<term>Vacuoles</term>
</keywords>
<keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Autophagosomes</term>
<term>Complexe-1 cible mécanistique de la rapamycine</term>
<term>Complexes multiprotéiques</term>
<term>Protein kinases</term>
<term>Protéines adaptatrices de la transduction du signal</term>
<term>Protéines associées à l'autophagie</term>
<term>Protéines de Saccharomyces cerevisiae</term>
<term>Saccharomyces cerevisiae</term>
<term>Vacuoles</term>
</keywords>
<keywords scheme="MESH" xml:lang="en"><term>Autophagy</term>
<term>Phosphorylation</term>
<term>Point Mutation</term>
<term>Protein Binding</term>
</keywords>
<keywords scheme="MESH" xml:lang="fr"><term>Autophagie</term>
<term>Liaison aux protéines</term>
<term>Mutation ponctuelle</term>
<term>Phosphorylation</term>
</keywords>
</textClass>
</profileDesc>
</teiHeader>
<front><div type="abstract" xml:lang="en">Many biomolecules undergo liquid-liquid phase separation to form liquid-like condensates that mediate diverse cellular functions<sup>1,2</sup>
. Autophagy is able to degrade such condensates using autophagosomes-double-membrane structures that are synthesized de novo at the pre-autophagosomal structure (PAS) in yeast<sup>3-5</sup>
. Whereas Atg proteins that associate with the PAS have been characterized, the physicochemical and functional properties of the PAS remain unclear owing to its small size and fragility. Here we show that the PAS is in fact a liquid-like condensate of Atg proteins. The autophagy-initiating Atg1 complex undergoes phase separation to form liquid droplets in vitro, and point mutations or phosphorylation that inhibit phase separation impair PAS formation in vivo. In vitro experiments show that Atg1-complex droplets can be tethered to membranes via specific protein-protein interactions, explaining the vacuolar membrane localization of the PAS in vivo. We propose that phase separation has a critical, active role in autophagy, whereby it organizes the autophagy machinery at the PAS.</div>
</front>
</TEI>
<pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">32025038</PMID>
<DateCompleted><Year>2020</Year>
<Month>04</Month>
<Day>20</Day>
</DateCompleted>
<DateRevised><Year>2020</Year>
<Month>04</Month>
<Day>20</Day>
</DateRevised>
<Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1476-4687</ISSN>
<JournalIssue CitedMedium="Internet"><Volume>578</Volume>
<Issue>7794</Issue>
<PubDate><Year>2020</Year>
<Month>02</Month>
</PubDate>
</JournalIssue>
<Title>Nature</Title>
<ISOAbbreviation>Nature</ISOAbbreviation>
</Journal>
<ArticleTitle>Phase separation organizes the site of autophagosome formation.</ArticleTitle>
<Pagination><MedlinePgn>301-305</MedlinePgn>
</Pagination>
<ELocationID EIdType="doi" ValidYN="Y">10.1038/s41586-020-1977-6</ELocationID>
<Abstract><AbstractText>Many biomolecules undergo liquid-liquid phase separation to form liquid-like condensates that mediate diverse cellular functions<sup>1,2</sup>
. Autophagy is able to degrade such condensates using autophagosomes-double-membrane structures that are synthesized de novo at the pre-autophagosomal structure (PAS) in yeast<sup>3-5</sup>
. Whereas Atg proteins that associate with the PAS have been characterized, the physicochemical and functional properties of the PAS remain unclear owing to its small size and fragility. Here we show that the PAS is in fact a liquid-like condensate of Atg proteins. The autophagy-initiating Atg1 complex undergoes phase separation to form liquid droplets in vitro, and point mutations or phosphorylation that inhibit phase separation impair PAS formation in vivo. In vitro experiments show that Atg1-complex droplets can be tethered to membranes via specific protein-protein interactions, explaining the vacuolar membrane localization of the PAS in vivo. We propose that phase separation has a critical, active role in autophagy, whereby it organizes the autophagy machinery at the PAS.</AbstractText>
</Abstract>
<AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Fujioka</LastName>
<ForeName>Yuko</ForeName>
<Initials>Y</Initials>
<AffiliationInfo><Affiliation>Institute of Microbial Chemistry (BIKAKEN), Tokyo, Japan.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Alam</LastName>
<ForeName>Jahangir Md</ForeName>
<Initials>JM</Initials>
<AffiliationInfo><Affiliation>Institute of Microbial Chemistry (BIKAKEN), Tokyo, Japan.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Noshiro</LastName>
<ForeName>Daisuke</ForeName>
<Initials>D</Initials>
<AffiliationInfo><Affiliation>Institute of Microbial Chemistry (BIKAKEN), Tokyo, Japan.</Affiliation>
</AffiliationInfo>
<AffiliationInfo><Affiliation>Nano Life Science Institute (WPI-NanoLSI), Kanazawa University, Kanazawa, Japan.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Mouri</LastName>
<ForeName>Kazunari</ForeName>
<Initials>K</Initials>
<AffiliationInfo><Affiliation>Center for Biosystems Dynamics Research (BDR), RIKEN, Osaka, Japan.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Ando</LastName>
<ForeName>Toshio</ForeName>
<Initials>T</Initials>
<AffiliationInfo><Affiliation>Nano Life Science Institute (WPI-NanoLSI), Kanazawa University, Kanazawa, Japan.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Okada</LastName>
<ForeName>Yasushi</ForeName>
<Initials>Y</Initials>
<AffiliationInfo><Affiliation>Center for Biosystems Dynamics Research (BDR), RIKEN, Osaka, Japan.</Affiliation>
</AffiliationInfo>
<AffiliationInfo><Affiliation>Department of Physics, Universal Biology Institute (UBI) and International Research Center for Neurointelligence (WPI-IRCN), The University of Tokyo, Tokyo, Japan.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>May</LastName>
<ForeName>Alexander I</ForeName>
<Initials>AI</Initials>
<AffiliationInfo><Affiliation>Cell Biology Center, Institute of Innovative Research, Tokyo Institute of Technology, Yokohama, Japan.</Affiliation>
</AffiliationInfo>
<AffiliationInfo><Affiliation>Tokyo Tech World Research Hub Initiative (WRHI), Institute of Innovative Research, Tokyo Institute of Technology, Yokohama, Japan.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Knorr</LastName>
<ForeName>Roland L</ForeName>
<Initials>RL</Initials>
<AffiliationInfo><Affiliation>Department of Theory and Bio-Systems, Max Planck Institute of Colloids and Interfaces, Potsdam, Germany.</Affiliation>
</AffiliationInfo>
<AffiliationInfo><Affiliation>Graduate School and Faculty of Medicine, The University of Tokyo, Tokyo, Japan.</Affiliation>
</AffiliationInfo>
<AffiliationInfo><Affiliation>Max Planck Institute of Molecular Plant Physiology, Potsdam, Germany.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Suzuki</LastName>
<ForeName>Kuninori</ForeName>
<Initials>K</Initials>
<AffiliationInfo><Affiliation>Life Science Data Research Center, Graduate School of Frontier Sciences, The University of Tokyo, Kashiwa, Japan.</Affiliation>
</AffiliationInfo>
<AffiliationInfo><Affiliation>Collaborative Research Institute for Innovative Microbiology, The University of Tokyo, Tokyo, Japan.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Ohsumi</LastName>
<ForeName>Yoshinori</ForeName>
<Initials>Y</Initials>
<AffiliationInfo><Affiliation>Cell Biology Center, Institute of Innovative Research, Tokyo Institute of Technology, Yokohama, Japan.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Noda</LastName>
<ForeName>Nobuo N</ForeName>
<Initials>NN</Initials>
<AffiliationInfo><Affiliation>Institute of Microbial Chemistry (BIKAKEN), Tokyo, Japan. nn@bikaken.or.jp.</Affiliation>
</AffiliationInfo>
</Author>
</AuthorList>
<Language>eng</Language>
<PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType>
</PublicationTypeList>
<ArticleDate DateType="Electronic"><Year>2020</Year>
<Month>02</Month>
<Day>05</Day>
</ArticleDate>
</Article>
<MedlineJournalInfo><Country>England</Country>
<MedlineTA>Nature</MedlineTA>
<NlmUniqueID>0410462</NlmUniqueID>
<ISSNLinking>0028-0836</ISSNLinking>
</MedlineJournalInfo>
<ChemicalList><Chemical><RegistryNumber>0</RegistryNumber>
<NameOfSubstance UI="C413216">ATG13 protein, S cerevisiae</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>0</RegistryNumber>
<NameOfSubstance UI="D048868">Adaptor Proteins, Signal Transducing</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>0</RegistryNumber>
<NameOfSubstance UI="D000071183">Autophagy-Related Proteins</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>0</RegistryNumber>
<NameOfSubstance UI="D046912">Multiprotein Complexes</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>0</RegistryNumber>
<NameOfSubstance UI="D029701">Saccharomyces cerevisiae Proteins</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>EC 2.7.-</RegistryNumber>
<NameOfSubstance UI="D011494">Protein Kinases</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>EC 2.7.1.-</RegistryNumber>
<NameOfSubstance UI="C477823">ATG1 protein, S cerevisiae</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>EC 2.7.11.1</RegistryNumber>
<NameOfSubstance UI="D000076222">Mechanistic Target of Rapamycin Complex 1</NameOfSubstance>
</Chemical>
</ChemicalList>
<CitationSubset>IM</CitationSubset>
<CommentsCorrectionsList><CommentsCorrections RefType="CommentIn"><RefSource>Cell Res. 2020 May;30(5):372-373</RefSource>
<PMID Version="1">32203129</PMID>
</CommentsCorrections>
<CommentsCorrections RefType="CommentIn"><RefSource>Mol Cell. 2020 May 7;78(3):379-381</RefSource>
<PMID Version="1">32386541</PMID>
</CommentsCorrections>
</CommentsCorrectionsList>
<MeshHeadingList><MeshHeading><DescriptorName UI="D048868" MajorTopicYN="N">Adaptor Proteins, Signal Transducing</DescriptorName>
<QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName>
<QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName>
<QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D000071182" MajorTopicYN="N">Autophagosomes</DescriptorName>
<QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName>
<QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D001343" MajorTopicYN="N">Autophagy</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D000071183" MajorTopicYN="N">Autophagy-Related Proteins</DescriptorName>
<QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName>
<QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName>
<QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D000076222" MajorTopicYN="N">Mechanistic Target of Rapamycin Complex 1</DescriptorName>
<QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName>
<QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D046912" MajorTopicYN="N">Multiprotein Complexes</DescriptorName>
<QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName>
<QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName>
<QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D010766" MajorTopicYN="N">Phosphorylation</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D017354" MajorTopicYN="N">Point Mutation</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D011485" MajorTopicYN="N">Protein Binding</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D011494" MajorTopicYN="N">Protein Kinases</DescriptorName>
<QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName>
<QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName>
<QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D012441" MajorTopicYN="N">Saccharomyces cerevisiae</DescriptorName>
<QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName>
<QualifierName UI="Q000166" MajorTopicYN="Y">cytology</QualifierName>
<QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName>
<QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D029701" MajorTopicYN="N">Saccharomyces cerevisiae Proteins</DescriptorName>
<QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName>
<QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName>
<QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D014617" MajorTopicYN="N">Vacuoles</DescriptorName>
<QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName>
</MeshHeading>
</MeshHeadingList>
</MedlineCitation>
<PubmedData><History><PubMedPubDate PubStatus="received"><Year>2018</Year>
<Month>12</Month>
<Day>17</Day>
</PubMedPubDate>
<PubMedPubDate PubStatus="accepted"><Year>2019</Year>
<Month>12</Month>
<Day>02</Day>
</PubMedPubDate>
<PubMedPubDate PubStatus="pubmed"><Year>2020</Year>
<Month>2</Month>
<Day>7</Day>
<Hour>6</Hour>
<Minute>0</Minute>
</PubMedPubDate>
<PubMedPubDate PubStatus="medline"><Year>2020</Year>
<Month>4</Month>
<Day>21</Day>
<Hour>6</Hour>
<Minute>0</Minute>
</PubMedPubDate>
<PubMedPubDate PubStatus="entrez"><Year>2020</Year>
<Month>2</Month>
<Day>7</Day>
<Hour>6</Hour>
<Minute>0</Minute>
</PubMedPubDate>
</History>
<PublicationStatus>ppublish</PublicationStatus>
<ArticleIdList><ArticleId IdType="pubmed">32025038</ArticleId>
<ArticleId IdType="doi">10.1038/s41586-020-1977-6</ArticleId>
<ArticleId IdType="pii">10.1038/s41586-020-1977-6</ArticleId>
</ArticleIdList>
</PubmedData>
</pubmed>
<affiliations><list><country><li>Allemagne</li>
<li>Japon</li>
</country>
<region><li>Brandebourg</li>
<li>Région de Kantō</li>
</region>
<settlement><li>Potsdam</li>
<li>Tokyo</li>
</settlement>
<orgName><li>Université de Tokyo</li>
</orgName>
</list>
<tree><country name="Japon"><region name="Région de Kantō"><name sortKey="Fujioka, Yuko" sort="Fujioka, Yuko" uniqKey="Fujioka Y" first="Yuko" last="Fujioka">Yuko Fujioka</name>
</region>
<name sortKey="Alam, Jahangir Md" sort="Alam, Jahangir Md" uniqKey="Alam J" first="Jahangir Md" last="Alam">Jahangir Md Alam</name>
<name sortKey="Ando, Toshio" sort="Ando, Toshio" uniqKey="Ando T" first="Toshio" last="Ando">Toshio Ando</name>
<name sortKey="Knorr, Roland L" sort="Knorr, Roland L" uniqKey="Knorr R" first="Roland L" last="Knorr">Roland L. Knorr</name>
<name sortKey="May, Alexander I" sort="May, Alexander I" uniqKey="May A" first="Alexander I" last="May">Alexander I. May</name>
<name sortKey="May, Alexander I" sort="May, Alexander I" uniqKey="May A" first="Alexander I" last="May">Alexander I. May</name>
<name sortKey="Mouri, Kazunari" sort="Mouri, Kazunari" uniqKey="Mouri K" first="Kazunari" last="Mouri">Kazunari Mouri</name>
<name sortKey="Noda, Nobuo N" sort="Noda, Nobuo N" uniqKey="Noda N" first="Nobuo N" last="Noda">Nobuo N. Noda</name>
<name sortKey="Noshiro, Daisuke" sort="Noshiro, Daisuke" uniqKey="Noshiro D" first="Daisuke" last="Noshiro">Daisuke Noshiro</name>
<name sortKey="Noshiro, Daisuke" sort="Noshiro, Daisuke" uniqKey="Noshiro D" first="Daisuke" last="Noshiro">Daisuke Noshiro</name>
<name sortKey="Ohsumi, Yoshinori" sort="Ohsumi, Yoshinori" uniqKey="Ohsumi Y" first="Yoshinori" last="Ohsumi">Yoshinori Ohsumi</name>
<name sortKey="Okada, Yasushi" sort="Okada, Yasushi" uniqKey="Okada Y" first="Yasushi" last="Okada">Yasushi Okada</name>
<name sortKey="Okada, Yasushi" sort="Okada, Yasushi" uniqKey="Okada Y" first="Yasushi" last="Okada">Yasushi Okada</name>
<name sortKey="Suzuki, Kuninori" sort="Suzuki, Kuninori" uniqKey="Suzuki K" first="Kuninori" last="Suzuki">Kuninori Suzuki</name>
<name sortKey="Suzuki, Kuninori" sort="Suzuki, Kuninori" uniqKey="Suzuki K" first="Kuninori" last="Suzuki">Kuninori Suzuki</name>
</country>
<country name="Allemagne"><region name="Brandebourg"><name sortKey="Knorr, Roland L" sort="Knorr, Roland L" uniqKey="Knorr R" first="Roland L" last="Knorr">Roland L. Knorr</name>
</region>
<name sortKey="Knorr, Roland L" sort="Knorr, Roland L" uniqKey="Knorr R" first="Roland L" last="Knorr">Roland L. Knorr</name>
</country>
</tree>
</affiliations>
</record>

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	Serveur d'exploration sur la rapamycine et les champignons
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Serveur d'exploration sur la rapamycine et les champignons

Phase separation organizes the site of autophagosome formation.

Phase separation organizes the site of autophagosome formation.

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