Zinc starvation induces autophagy in yeast.
Identifieur interne : 000693 ( Main/Exploration ); précédent : 000692; suivant : 000694Zinc starvation induces autophagy in yeast.
Auteurs : Tomoko Kawamata ; Tetsuro Horie [Japon] ; Miou Matsunami ; Michiko Sasaki ; Yoshinori Ohsumi [Japon]Source :
- The Journal of biological chemistry [ 1083-351X ] ; 2017.
Descripteurs français
- KwdFr :
- Alcohol dehydrogenase (génétique), Alcohol dehydrogenase (métabolisme), Autophagie (MeSH), Complexe-1 cible mécanistique de la rapamycine (MeSH), Complexes multiprotéiques (génétique), Complexes multiprotéiques (métabolisme), Facteurs de transcription (génétique), Facteurs de transcription (métabolisme), Protéines de Saccharomyces cerevisiae (génétique), Protéines de Saccharomyces cerevisiae (métabolisme), Protéolyse (MeSH), Saccharomyces cerevisiae (génétique), Saccharomyces cerevisiae (métabolisme), Sérine-thréonine kinases TOR (génétique), Sérine-thréonine kinases TOR (métabolisme), Zinc (métabolisme).
- MESH :
- génétique : Alcohol dehydrogenase, Complexes multiprotéiques, Facteurs de transcription, Protéines de Saccharomyces cerevisiae, Saccharomyces cerevisiae, Sérine-thréonine kinases TOR.
- métabolisme : Alcohol dehydrogenase, Complexes multiprotéiques, Facteurs de transcription, Protéines de Saccharomyces cerevisiae, Saccharomyces cerevisiae, Sérine-thréonine kinases TOR, Zinc.
- Autophagie, Complexe-1 cible mécanistique de la rapamycine, Protéolyse.
English descriptors
- KwdEn :
- Alcohol Dehydrogenase (genetics), Alcohol Dehydrogenase (metabolism), Autophagy (MeSH), Mechanistic Target of Rapamycin Complex 1 (MeSH), Multiprotein Complexes (genetics), Multiprotein Complexes (metabolism), Proteolysis (MeSH), Saccharomyces cerevisiae (genetics), Saccharomyces cerevisiae (metabolism), Saccharomyces cerevisiae Proteins (genetics), Saccharomyces cerevisiae Proteins (metabolism), TOR Serine-Threonine Kinases (genetics), TOR Serine-Threonine Kinases (metabolism), Transcription Factors (genetics), Transcription Factors (metabolism), Zinc (metabolism).
- MESH :
- chemical , genetics : Alcohol Dehydrogenase, Multiprotein Complexes, Saccharomyces cerevisiae Proteins, TOR Serine-Threonine Kinases, Transcription Factors.
- chemical , metabolism : Alcohol Dehydrogenase, Multiprotein Complexes, Saccharomyces cerevisiae Proteins, TOR Serine-Threonine Kinases, Transcription Factors, Zinc.
- genetics : Saccharomyces cerevisiae.
- metabolism : Saccharomyces cerevisiae.
- Autophagy, Mechanistic Target of Rapamycin Complex 1, Proteolysis.
Abstract
Zinc is an essential nutrient for all forms of life. Within cells, most zinc is bound to protein. Because zinc serves as a catalytic or structural cofactor for many proteins, cells must maintain zinc homeostasis under severely zinc-deficient conditions. In yeast, the transcription factor Zap1 controls the expression of genes required for uptake and mobilization of zinc, but to date the fate of existing zinc-binding proteins under zinc starvation remains poorly understood. Autophagy is an evolutionarily conserved cellular degradation/recycling process in which cytoplasmic proteins and organelles are sequestered for degradation in the vacuole/lysosome. In this study, we investigated how autophagy functions under zinc starvation. Zinc depletion induced non-selective autophagy, which is important for zinc-limited growth. Induction of autophagy by zinc starvation was not directly related to transcriptional activation of Zap1. Instead, TORC1 inactivation directed zinc starvation-induced autophagy. Abundant zinc proteins, such as Adh1, Fba1, and ribosomal protein Rpl37, were degraded in an autophagy-dependent manner. But the targets of autophagy were not restricted to zinc-binding proteins. When cellular zinc is severely depleted, this non-selective autophagy plays a role in releasing zinc from the degraded proteins and recycling zinc for other essential purposes.
DOI: 10.1074/jbc.M116.762948
PubMed: 28264932
PubMed Central: PMC5437255
Affiliations:
Links toward previous steps (curation, corpus...)
Le document en format XML
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xml:lang="fr"><term>Autophagie</term><term>Complexe-1 cible mécanistique de la rapamycine</term><term>Protéolyse</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Zinc is an essential nutrient for all forms of life. Within cells, most zinc is bound to protein. Because zinc serves as a catalytic or structural cofactor for many proteins, cells must maintain zinc homeostasis under severely zinc-deficient conditions. In yeast, the transcription factor Zap1 controls the expression of genes required for uptake and mobilization of zinc, but to date the fate of existing zinc-binding proteins under zinc starvation remains poorly understood. Autophagy is an evolutionarily conserved cellular degradation/recycling process in which cytoplasmic proteins and organelles are sequestered for degradation in the vacuole/lysosome. In this study, we investigated how autophagy functions under zinc starvation. Zinc depletion induced non-selective autophagy, which is important for zinc-limited growth. Induction of autophagy by zinc starvation was not directly related to transcriptional activation of Zap1. Instead, TORC1 inactivation directed zinc starvation-induced autophagy. Abundant zinc proteins, such as Adh1, Fba1, and ribosomal protein Rpl37, were degraded in an autophagy-dependent manner. But the targets of autophagy were not restricted to zinc-binding proteins. When cellular zinc is severely depleted, this non-selective autophagy plays a role in releasing zinc from the degraded proteins and recycling zinc for other essential purposes.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">28264932</PMID><DateCompleted><Year>2017</Year><Month>06</Month><Day>08</Day></DateCompleted><DateRevised><Year>2018</Year><Month>11</Month><Day>13</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1083-351X</ISSN><JournalIssue CitedMedium="Internet"><Volume>292</Volume><Issue>20</Issue><PubDate><Year>2017</Year><Month>05</Month><Day>19</Day></PubDate></JournalIssue><Title>The Journal of biological chemistry</Title><ISOAbbreviation>J Biol Chem</ISOAbbreviation></Journal><ArticleTitle>Zinc starvation induces autophagy in yeast.</ArticleTitle><Pagination><MedlinePgn>8520-8530</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1074/jbc.M116.762948</ELocationID><Abstract><AbstractText>Zinc is an essential nutrient for all forms of life. Within cells, most zinc is bound to protein. Because zinc serves as a catalytic or structural cofactor for many proteins, cells must maintain zinc homeostasis under severely zinc-deficient conditions. In yeast, the transcription factor Zap1 controls the expression of genes required for uptake and mobilization of zinc, but to date the fate of existing zinc-binding proteins under zinc starvation remains poorly understood. Autophagy is an evolutionarily conserved cellular degradation/recycling process in which cytoplasmic proteins and organelles are sequestered for degradation in the vacuole/lysosome. In this study, we investigated how autophagy functions under zinc starvation. Zinc depletion induced non-selective autophagy, which is important for zinc-limited growth. Induction of autophagy by zinc starvation was not directly related to transcriptional activation of Zap1. Instead, TORC1 inactivation directed zinc starvation-induced autophagy. Abundant zinc proteins, such as Adh1, Fba1, and ribosomal protein Rpl37, were degraded in an autophagy-dependent manner. But the targets of autophagy were not restricted to zinc-binding proteins. When cellular zinc is severely depleted, this non-selective autophagy plays a role in releasing zinc from the degraded proteins and recycling zinc for other essential purposes.</AbstractText><CopyrightInformation>© 2017 by The American Society for Biochemistry and Molecular Biology, Inc.</CopyrightInformation></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Kawamata</LastName><ForeName>Tomoko</ForeName><Initials>T</Initials><AffiliationInfo><Affiliation>From the Research Unit for Cell Biology, Institute of Innovative Research, Tokyo Institute of Technology, Yokohama 226-8503 and.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Horie</LastName><ForeName>Tetsuro</ForeName><Initials>T</Initials><AffiliationInfo><Affiliation>From the Research Unit for Cell Biology, Institute of Innovative Research, Tokyo Institute of Technology, Yokohama 226-8503 and.</Affiliation></AffiliationInfo><AffiliationInfo><Affiliation>the Research Center for Odontology, School of Life Dentistry at Tokyo, The Nippon Dental University, Chiyoda-ku, Tokyo 102-8159, Japan.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Matsunami</LastName><ForeName>Miou</ForeName><Initials>M</Initials><AffiliationInfo><Affiliation>From the Research Unit for Cell Biology, Institute of Innovative Research, Tokyo Institute of Technology, Yokohama 226-8503 and.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Sasaki</LastName><ForeName>Michiko</ForeName><Initials>M</Initials><AffiliationInfo><Affiliation>From the Research Unit for Cell Biology, Institute of Innovative Research, Tokyo Institute of Technology, Yokohama 226-8503 and.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Ohsumi</LastName><ForeName>Yoshinori</ForeName><Initials>Y</Initials><AffiliationInfo><Affiliation>From the Research Unit for Cell Biology, Institute of Innovative Research, Tokyo Institute of Technology, Yokohama 226-8503 and yohsumi@iri.titech.ac.jp.</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>2017</Year><Month>03</Month><Day>06</Day></ArticleDate></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>J Biol Chem</MedlineTA><NlmUniqueID>2985121R</NlmUniqueID><ISSNLinking>0021-9258</ISSNLinking></MedlineJournalInfo><ChemicalList><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>0</RegistryNumber><NameOfSubstance UI="D014157">Transcription Factors</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="C103264">ZAP1 protein, S cerevisiae</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.1.1.1</RegistryNumber><NameOfSubstance UI="C516801">ADH1 protein, S cerevisiae</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.1.1.1</RegistryNumber><NameOfSubstance UI="D000426">Alcohol Dehydrogenase</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>J41CSQ7QDS</RegistryNumber><NameOfSubstance UI="D015032">Zinc</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D000426" MajorTopicYN="N">Alcohol Dehydrogenase</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D001343" MajorTopicYN="Y">Autophagy</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D000076222" MajorTopicYN="N">Mechanistic Target of Rapamycin Complex 1</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D046912" MajorTopicYN="N">Multiprotein Complexes</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D059748" MajorTopicYN="N">Proteolysis</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D012441" MajorTopicYN="N">Saccharomyces cerevisiae</DescriptorName><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="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D058570" MajorTopicYN="N">TOR Serine-Threonine Kinases</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D014157" MajorTopicYN="N">Transcription Factors</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D015032" MajorTopicYN="N">Zinc</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading></MeshHeadingList><KeywordList Owner="NOTNLM"><Keyword MajorTopicYN="Y">TOR complex (TORC)</Keyword><Keyword MajorTopicYN="Y">autophagy</Keyword><Keyword MajorTopicYN="Y">metal</Keyword><Keyword MajorTopicYN="Y">starvation</Keyword><Keyword MajorTopicYN="Y">yeast</Keyword><Keyword MajorTopicYN="Y">zinc</Keyword></KeywordList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="received"><Year>2016</Year><Month>10</Month><Day>13</Day></PubMedPubDate><PubMedPubDate PubStatus="revised"><Year>2017</Year><Month>02</Month><Day>22</Day></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2017</Year><Month>3</Month><Day>8</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2017</Year><Month>6</Month><Day>9</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate 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sortKey="Ohsumi, Yoshinori" sort="Ohsumi, Yoshinori" uniqKey="Ohsumi Y" first="Yoshinori" last="Ohsumi">Yoshinori Ohsumi</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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