Fine mapping of autophagy-related proteins during autophagosome formation in Saccharomyces cerevisiae.
Identifieur interne : 001052 ( Main/Exploration ); précédent : 001051; suivant : 001053Fine mapping of autophagy-related proteins during autophagosome formation in Saccharomyces cerevisiae.
Auteurs : Kuninori Suzuki [Japon] ; Manami Akioka ; Chika Kondo-Kakuta ; Hayashi Yamamoto ; Yoshinori OhsumiSource :
- Journal of cell science [ 1477-9137 ] ; 2013.
Descripteurs français
- KwdFr :
- Autophagie (physiologie), Phagosomes (génétique), Phagosomes (métabolisme), Phosphatidylinositol 3-kinases (génétique), Phosphatidylinositol 3-kinases (métabolisme), Protéines de Saccharomyces cerevisiae (génétique), Protéines de Saccharomyces cerevisiae (métabolisme), Saccharomyces cerevisiae (cytologie), Saccharomyces cerevisiae (génétique), Saccharomyces cerevisiae (métabolisme).
- MESH :
- cytologie : Saccharomyces cerevisiae.
- génétique : Phagosomes, Phosphatidylinositol 3-kinases, Protéines de Saccharomyces cerevisiae, Saccharomyces cerevisiae.
- métabolisme : Phagosomes, Phosphatidylinositol 3-kinases, Protéines de Saccharomyces cerevisiae, Saccharomyces cerevisiae.
- physiologie : Autophagie.
English descriptors
- KwdEn :
- Autophagy (physiology), Phagosomes (genetics), Phagosomes (metabolism), Phosphatidylinositol 3-Kinases (genetics), Phosphatidylinositol 3-Kinases (metabolism), Saccharomyces cerevisiae (cytology), Saccharomyces cerevisiae (genetics), Saccharomyces cerevisiae (metabolism), Saccharomyces cerevisiae Proteins (genetics), Saccharomyces cerevisiae Proteins (metabolism).
- MESH :
- chemical , genetics : Phosphatidylinositol 3-Kinases, Saccharomyces cerevisiae Proteins.
- cytology : Saccharomyces cerevisiae.
- genetics : Phagosomes, Saccharomyces cerevisiae.
- metabolism : Phagosomes, Phosphatidylinositol 3-Kinases, Saccharomyces cerevisiae, Saccharomyces cerevisiae Proteins.
- physiology : Autophagy.
Abstract
Autophagy is a bulk degradation system mediated by biogenesis of autophagosomes under starvation conditions. In Saccharomyces cerevisiae, a membrane sac called the isolation membrane (IM) is generated from the pre-autophagosomal structure (PAS); ultimately, the IM expands to become a mature autophagosome. Eighteen autophagy-related (Atg) proteins are engaged in autophagosome formation at the PAS. However, the cup-shaped IM was visualized just as a dot by fluorescence microscopy, posing a challenge to further understanding the detailed functions of Atg proteins during IM expansion. In this study, we visualized expanding IMs as cup-shaped structures using fluorescence microscopy by enlarging a selective cargo of autophagosomes, and finely mapped the localizations of Atg proteins. The PAS scaffold proteins (Atg13 and Atg17) and phosphatidylinositol 3-kinase complex I were localized to a position at the junction between the IM and the vacuolar membrane, termed the vacuole-IM contact site (VICS). By contrast, Atg1, Atg8 and the Atg16-Atg12-Atg5 complex were present at both the VICS and the cup-shaped IM. We designate this localization the 'IM' pattern. The Atg2-Atg18 complex and Atg9 localized to the edge of the IM, appearing as two or three dots, in close proximity to the endoplasmic reticulum exit sites. Thus, we designate these dots as the 'IM edge' pattern. These data suggest that Atg proteins play individual roles at spatially distinct locations during IM expansion. These findings will facilitate detailed investigations of the function of each Atg protein during autophagosome formation.
DOI: 10.1242/jcs.122960
PubMed: 23549786
Affiliations:
Links toward previous steps (curation, corpus...)
Le document en format XML
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uniqKey="Akioka M" first="Manami" last="Akioka">Manami Akioka</name></author><author><name sortKey="Kondo Kakuta, Chika" sort="Kondo Kakuta, Chika" uniqKey="Kondo Kakuta C" first="Chika" last="Kondo-Kakuta">Chika Kondo-Kakuta</name></author><author><name sortKey="Yamamoto, Hayashi" sort="Yamamoto, Hayashi" uniqKey="Yamamoto H" first="Hayashi" last="Yamamoto">Hayashi Yamamoto</name></author><author><name sortKey="Ohsumi, Yoshinori" sort="Ohsumi, Yoshinori" uniqKey="Ohsumi Y" first="Yoshinori" last="Ohsumi">Yoshinori Ohsumi</name></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2013">2013</date><idno type="RBID">pubmed:23549786</idno><idno type="pmid">23549786</idno><idno type="doi">10.1242/jcs.122960</idno><idno type="wicri:Area/Main/Corpus">001046</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Corpus" wicri:corpus="PubMed">001046</idno><idno type="wicri:Area/Main/Curation">001046</idno><idno type="wicri:explorRef" 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de Kantō</region></placeName></affiliation></author><author><name sortKey="Akioka, Manami" sort="Akioka, Manami" uniqKey="Akioka M" first="Manami" last="Akioka">Manami Akioka</name></author><author><name sortKey="Kondo Kakuta, Chika" sort="Kondo Kakuta, Chika" uniqKey="Kondo Kakuta C" first="Chika" last="Kondo-Kakuta">Chika Kondo-Kakuta</name></author><author><name sortKey="Yamamoto, Hayashi" sort="Yamamoto, Hayashi" uniqKey="Yamamoto H" first="Hayashi" last="Yamamoto">Hayashi Yamamoto</name></author><author><name sortKey="Ohsumi, Yoshinori" sort="Ohsumi, Yoshinori" uniqKey="Ohsumi Y" first="Yoshinori" last="Ohsumi">Yoshinori Ohsumi</name></author></analytic><series><title level="j">Journal of cell science</title><idno type="eISSN">1477-9137</idno><imprint><date when="2013" type="published">2013</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Autophagy (physiology)</term><term>Phagosomes (genetics)</term><term>Phagosomes (metabolism)</term><term>Phosphatidylinositol 3-Kinases (genetics)</term><term>Phosphatidylinositol 3-Kinases (metabolism)</term><term>Saccharomyces cerevisiae (cytology)</term><term>Saccharomyces cerevisiae (genetics)</term><term>Saccharomyces cerevisiae (metabolism)</term><term>Saccharomyces cerevisiae Proteins (genetics)</term><term>Saccharomyces cerevisiae Proteins (metabolism)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Autophagie (physiologie)</term><term>Phagosomes (génétique)</term><term>Phagosomes (métabolisme)</term><term>Phosphatidylinositol 3-kinases (génétique)</term><term>Phosphatidylinositol 3-kinases (métabolisme)</term><term>Protéines de Saccharomyces cerevisiae (génétique)</term><term>Protéines de Saccharomyces cerevisiae (métabolisme)</term><term>Saccharomyces cerevisiae (cytologie)</term><term>Saccharomyces cerevisiae (génétique)</term><term>Saccharomyces cerevisiae (métabolisme)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Phosphatidylinositol 3-Kinases</term><term>Saccharomyces cerevisiae Proteins</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>Phagosomes</term><term>Saccharomyces cerevisiae</term></keywords><keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Phagosomes</term><term>Phosphatidylinositol 3-kinases</term><term>Protéines de Saccharomyces cerevisiae</term><term>Saccharomyces cerevisiae</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Phagosomes</term><term>Phosphatidylinositol 3-Kinases</term><term>Saccharomyces cerevisiae</term><term>Saccharomyces cerevisiae Proteins</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Phagosomes</term><term>Phosphatidylinositol 3-kinases</term><term>Protéines de Saccharomyces cerevisiae</term><term>Saccharomyces cerevisiae</term></keywords><keywords scheme="MESH" qualifier="physiologie" xml:lang="fr"><term>Autophagie</term></keywords><keywords scheme="MESH" qualifier="physiology" xml:lang="en"><term>Autophagy</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Autophagy is a bulk degradation system mediated by biogenesis of autophagosomes under starvation conditions. In Saccharomyces cerevisiae, a membrane sac called the isolation membrane (IM) is generated from the pre-autophagosomal structure (PAS); ultimately, the IM expands to become a mature autophagosome. Eighteen autophagy-related (Atg) proteins are engaged in autophagosome formation at the PAS. However, the cup-shaped IM was visualized just as a dot by fluorescence microscopy, posing a challenge to further understanding the detailed functions of Atg proteins during IM expansion. In this study, we visualized expanding IMs as cup-shaped structures using fluorescence microscopy by enlarging a selective cargo of autophagosomes, and finely mapped the localizations of Atg proteins. The PAS scaffold proteins (Atg13 and Atg17) and phosphatidylinositol 3-kinase complex I were localized to a position at the junction between the IM and the vacuolar membrane, termed the vacuole-IM contact site (VICS). By contrast, Atg1, Atg8 and the Atg16-Atg12-Atg5 complex were present at both the VICS and the cup-shaped IM. We designate this localization the 'IM' pattern. The Atg2-Atg18 complex and Atg9 localized to the edge of the IM, appearing as two or three dots, in close proximity to the endoplasmic reticulum exit sites. Thus, we designate these dots as the 'IM edge' pattern. These data suggest that Atg proteins play individual roles at spatially distinct locations during IM expansion. These findings will facilitate detailed investigations of the function of each Atg protein during autophagosome formation.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">23549786</PMID><DateCompleted><Year>2013</Year><Month>11</Month><Day>12</Day></DateCompleted><DateRevised><Year>2013</Year><Month>06</Month><Day>13</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1477-9137</ISSN><JournalIssue CitedMedium="Internet"><Volume>126</Volume><Issue>Pt 11</Issue><PubDate><Year>2013</Year><Month>Jun</Month><Day>01</Day></PubDate></JournalIssue><Title>Journal of cell science</Title><ISOAbbreviation>J Cell Sci</ISOAbbreviation></Journal><ArticleTitle>Fine mapping of autophagy-related proteins during autophagosome formation in Saccharomyces cerevisiae.</ArticleTitle><Pagination><MedlinePgn>2534-44</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1242/jcs.122960</ELocationID><Abstract><AbstractText>Autophagy is a bulk degradation system mediated by biogenesis of autophagosomes under starvation conditions. In Saccharomyces cerevisiae, a membrane sac called the isolation membrane (IM) is generated from the pre-autophagosomal structure (PAS); ultimately, the IM expands to become a mature autophagosome. Eighteen autophagy-related (Atg) proteins are engaged in autophagosome formation at the PAS. However, the cup-shaped IM was visualized just as a dot by fluorescence microscopy, posing a challenge to further understanding the detailed functions of Atg proteins during IM expansion. In this study, we visualized expanding IMs as cup-shaped structures using fluorescence microscopy by enlarging a selective cargo of autophagosomes, and finely mapped the localizations of Atg proteins. The PAS scaffold proteins (Atg13 and Atg17) and phosphatidylinositol 3-kinase complex I were localized to a position at the junction between the IM and the vacuolar membrane, termed the vacuole-IM contact site (VICS). By contrast, Atg1, Atg8 and the Atg16-Atg12-Atg5 complex were present at both the VICS and the cup-shaped IM. We designate this localization the 'IM' pattern. The Atg2-Atg18 complex and Atg9 localized to the edge of the IM, appearing as two or three dots, in close proximity to the endoplasmic reticulum exit sites. Thus, we designate these dots as the 'IM edge' pattern. These data suggest that Atg proteins play individual roles at spatially distinct locations during IM expansion. These findings will facilitate detailed investigations of the function of each Atg protein during autophagosome formation.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Suzuki</LastName><ForeName>Kuninori</ForeName><Initials>K</Initials><AffiliationInfo><Affiliation>Bioimaging Center, Graduate School of Frontier Sciences, University of Tokyo, FSB-101, 5-1-5 Kashiwanoha, Kashiwa, Chiba 277-8562, Japan. kuninori@k.u-tokyo.ac.jp</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Akioka</LastName><ForeName>Manami</ForeName><Initials>M</Initials></Author><Author ValidYN="Y"><LastName>Kondo-Kakuta</LastName><ForeName>Chika</ForeName><Initials>C</Initials></Author><Author ValidYN="Y"><LastName>Yamamoto</LastName><ForeName>Hayashi</ForeName><Initials>H</Initials></Author><Author ValidYN="Y"><LastName>Ohsumi</LastName><ForeName>Yoshinori</ForeName><Initials>Y</Initials></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>2013</Year><Month>04</Month><Day>02</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="D029701">Saccharomyces cerevisiae Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 2.7.1.-</RegistryNumber><NameOfSubstance UI="D019869">Phosphatidylinositol 3-Kinases</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D001343" 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MajorTopicYN="N">VICS</Keyword><Keyword MajorTopicYN="N">Vacuole-isolation membrane contact site</Keyword><Keyword MajorTopicYN="N">Yeast</Keyword></KeywordList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="entrez"><Year>2013</Year><Month>4</Month><Day>4</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2013</Year><Month>4</Month><Day>4</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2013</Year><Month>11</Month><Day>13</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">23549786</ArticleId><ArticleId IdType="pii">jcs.122960</ArticleId><ArticleId IdType="doi">10.1242/jcs.122960</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>Japon</li></country><region><li>Région de Kantō</li></region><settlement><li>Tokyo</li></settlement><orgName><li>Université de Tokyo</li></orgName></list><tree><noCountry><name sortKey="Akioka, Manami" sort="Akioka, Manami" uniqKey="Akioka M" first="Manami" last="Akioka">Manami Akioka</name><name sortKey="Kondo Kakuta, Chika" sort="Kondo Kakuta, Chika" uniqKey="Kondo Kakuta C" first="Chika" last="Kondo-Kakuta">Chika Kondo-Kakuta</name><name sortKey="Ohsumi, Yoshinori" sort="Ohsumi, Yoshinori" uniqKey="Ohsumi Y" first="Yoshinori" last="Ohsumi">Yoshinori Ohsumi</name><name sortKey="Yamamoto, Hayashi" sort="Yamamoto, Hayashi" uniqKey="Yamamoto H" first="Hayashi" last="Yamamoto">Hayashi Yamamoto</name></noCountry><country name="Japon"><region name="Région de Kantō"><name sortKey="Suzuki, Kuninori" sort="Suzuki, Kuninori" uniqKey="Suzuki K" first="Kuninori" last="Suzuki">Kuninori Suzuki</name></region></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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