Autophagy regulator Atg9 is degraded by the proteasome.
Identifieur interne : 000144 ( Main/Exploration ); précédent : 000143; suivant : 000145Autophagy regulator Atg9 is degraded by the proteasome.
Auteurs : Guohui Hu [République populaire de Chine] ; Lizette Rios [États-Unis] ; Zhengwei Yan [République populaire de Chine] ; Angela M. Jasper [États-Unis] ; Dezzarae Luera [États-Unis] ; Shiwen Luo [République populaire de Chine] ; Hai Rao [États-Unis]Source :
- Biochemical and biophysical research communications [ 1090-2104 ] ; 2020.
Descripteurs français
- KwdFr :
- Autophagie (MeSH), Proteasome endopeptidase complex (métabolisme), Protéines associées à l'autophagie (métabolisme), Protéines de Saccharomyces cerevisiae (métabolisme), Protéines membranaires (métabolisme), Protéolyse (MeSH), Saccharomyces cerevisiae (cytologie), Saccharomyces cerevisiae (métabolisme).
- MESH :
English descriptors
- KwdEn :
- MESH :
- chemical , metabolism : Autophagy-Related Proteins, Membrane Proteins, Proteasome Endopeptidase Complex, Saccharomyces cerevisiae Proteins.
- cytology : Saccharomyces cerevisiae.
- metabolism : Saccharomyces cerevisiae.
- Autophagy, Proteolysis.
Abstract
Autophagy is a highly conserved biological process essential to protein, cellular and organismal homeostasis. As autophagy plays a critical role in cellular responses to various external and internal stimuli, it is important to understand the mechanism underlying autophagy regulation. Here, we monitor the stability of 17 key autophagy factors in the yeast S. cerevisiae and show that Atg9 and Atg14 are degraded under normal growth conditions. Whereas Atg14 is regulated by both the proteasome and autophagy, Atg9 turnover is normally mediated by the proteasome but impeded upon starvation or rapamycin treatment. Interestingly, distinct segments of Atg9 confer instability, suggesting that multiple pathways are involved in Atg9 degradation. Our results provide the foundation to further elucidate the physiological significance of Atg9 turnover and also the interplay between two major proteolytic systems (i.e., autophagy and the proteasome).
DOI: 10.1016/j.bbrc.2019.11.089
PubMed: 31759633
PubMed Central: PMC6954321
Affiliations:
Links toward previous steps (curation, corpus...)
Le document en format XML
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Jasper</name><affiliation wicri:level="1"><nlm:affiliation>Department of Molecular Medicine, the University of Texas Health, San Antonio, TX, 78229, USA.</nlm:affiliation><country xml:lang="fr">États-Unis</country><wicri:regionArea>Department of Molecular Medicine, the University of Texas Health, San Antonio, TX, 78229</wicri:regionArea><wicri:noRegion>78229</wicri:noRegion></affiliation></author><author><name sortKey="Luera, Dezzarae" sort="Luera, Dezzarae" uniqKey="Luera D" first="Dezzarae" last="Luera">Dezzarae Luera</name><affiliation wicri:level="1"><nlm:affiliation>Department of Molecular Medicine, the University of Texas Health, San Antonio, TX, 78229, USA.</nlm:affiliation><country xml:lang="fr">États-Unis</country><wicri:regionArea>Department of Molecular Medicine, the University of Texas Health, San Antonio, TX, 78229</wicri:regionArea><wicri:noRegion>78229</wicri:noRegion></affiliation></author><author><name sortKey="Luo, Shiwen" sort="Luo, Shiwen" uniqKey="Luo S" first="Shiwen" last="Luo">Shiwen Luo</name><affiliation wicri:level="3"><nlm:affiliation>Center for Experimental Medicine, the First Affiliated Hospital, Nanchang University, Nanchang, China.</nlm:affiliation><country xml:lang="fr">République populaire de Chine</country><wicri:regionArea>Center for Experimental Medicine, the First Affiliated Hospital, Nanchang University, Nanchang</wicri:regionArea><placeName><settlement type="city">Nanchang</settlement><region type="province">Jiangxi</region></placeName></affiliation></author><author><name sortKey="Rao, Hai" sort="Rao, Hai" uniqKey="Rao H" first="Hai" last="Rao">Hai Rao</name><affiliation wicri:level="1"><nlm:affiliation>Department of Molecular Medicine, the University of Texas Health, San Antonio, TX, 78229, USA. Electronic address: raoh@uthscsa.edu.</nlm:affiliation><country xml:lang="fr">États-Unis</country><wicri:regionArea>Department of Molecular Medicine, the University of Texas Health, San Antonio, TX, 78229</wicri:regionArea><wicri:noRegion>78229</wicri:noRegion></affiliation></author></analytic><series><title level="j">Biochemical and biophysical research communications</title><idno type="eISSN">1090-2104</idno><imprint><date when="2020" type="published">2020</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Autophagy (MeSH)</term><term>Autophagy-Related Proteins (metabolism)</term><term>Membrane Proteins (metabolism)</term><term>Proteasome Endopeptidase Complex (metabolism)</term><term>Proteolysis (MeSH)</term><term>Saccharomyces cerevisiae (cytology)</term><term>Saccharomyces cerevisiae (metabolism)</term><term>Saccharomyces cerevisiae Proteins (metabolism)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Autophagie (MeSH)</term><term>Proteasome endopeptidase complex (métabolisme)</term><term>Protéines associées à l'autophagie (métabolisme)</term><term>Protéines de Saccharomyces cerevisiae (métabolisme)</term><term>Protéines membranaires (métabolisme)</term><term>Protéolyse (MeSH)</term><term>Saccharomyces cerevisiae (cytologie)</term><term>Saccharomyces cerevisiae (métabolisme)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Autophagy-Related Proteins</term><term>Membrane Proteins</term><term>Proteasome Endopeptidase Complex</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="metabolism" xml:lang="en"><term>Saccharomyces cerevisiae</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Proteasome endopeptidase complex</term><term>Protéines associées à l'autophagie</term><term>Protéines de Saccharomyces cerevisiae</term><term>Protéines membranaires</term><term>Saccharomyces cerevisiae</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Autophagy</term><term>Proteolysis</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Autophagie</term><term>Protéolyse</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Autophagy is a highly conserved biological process essential to protein, cellular and organismal homeostasis. As autophagy plays a critical role in cellular responses to various external and internal stimuli, it is important to understand the mechanism underlying autophagy regulation. Here, we monitor the stability of 17 key autophagy factors in the yeast S. cerevisiae and show that Atg9 and Atg14 are degraded under normal growth conditions. Whereas Atg14 is regulated by both the proteasome and autophagy, Atg9 turnover is normally mediated by the proteasome but impeded upon starvation or rapamycin treatment. Interestingly, distinct segments of Atg9 confer instability, suggesting that multiple pathways are involved in Atg9 degradation. Our results provide the foundation to further elucidate the physiological significance of Atg9 turnover and also the interplay between two major proteolytic systems (i.e., autophagy and the proteasome).</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">31759633</PMID><DateCompleted><Year>2020</Year><Month>08</Month><Day>17</Day></DateCompleted><DateRevised><Year>2020</Year><Month>08</Month><Day>17</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1090-2104</ISSN><JournalIssue CitedMedium="Internet"><Volume>522</Volume><Issue>1</Issue><PubDate><Year>2020</Year><Month>01</Month><Day>29</Day></PubDate></JournalIssue><Title>Biochemical and biophysical research communications</Title><ISOAbbreviation>Biochem Biophys Res Commun</ISOAbbreviation></Journal><ArticleTitle>Autophagy regulator Atg9 is degraded by the proteasome.</ArticleTitle><Pagination><MedlinePgn>254-258</MedlinePgn></Pagination><ELocationID EIdType="pii" ValidYN="Y">S0006-291X(19)32215-6</ELocationID><ELocationID EIdType="doi" ValidYN="Y">10.1016/j.bbrc.2019.11.089</ELocationID><Abstract><AbstractText>Autophagy is a highly conserved biological process essential to protein, cellular and organismal homeostasis. As autophagy plays a critical role in cellular responses to various external and internal stimuli, it is important to understand the mechanism underlying autophagy regulation. Here, we monitor the stability of 17 key autophagy factors in the yeast S. cerevisiae and show that Atg9 and Atg14 are degraded under normal growth conditions. Whereas Atg14 is regulated by both the proteasome and autophagy, Atg9 turnover is normally mediated by the proteasome but impeded upon starvation or rapamycin treatment. Interestingly, distinct segments of Atg9 confer instability, suggesting that multiple pathways are involved in Atg9 degradation. Our results provide the foundation to further elucidate the physiological significance of Atg9 turnover and also the interplay between two major proteolytic systems (i.e., autophagy and the proteasome).</AbstractText><CopyrightInformation>Copyright © 2019 Elsevier Inc. All rights reserved.</CopyrightInformation></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Hu</LastName><ForeName>Guohui</ForeName><Initials>G</Initials><AffiliationInfo><Affiliation>Center for Experimental Medicine, the First Affiliated Hospital, Nanchang University, Nanchang, China; Department of General Medicine, the First Affiliated Hospital, Nanchang University, Nanchang, China.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Rios</LastName><ForeName>Lizette</ForeName><Initials>L</Initials><AffiliationInfo><Affiliation>Department of Molecular Medicine, the University of Texas Health, San Antonio, TX, 78229, USA.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Yan</LastName><ForeName>Zhengwei</ForeName><Initials>Z</Initials><AffiliationInfo><Affiliation>Center for Experimental Medicine, the First Affiliated Hospital, Nanchang University, Nanchang, China.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Jasper</LastName><ForeName>Angela M</ForeName><Initials>AM</Initials><AffiliationInfo><Affiliation>Department of Molecular Medicine, the University of Texas Health, San Antonio, TX, 78229, USA.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Luera</LastName><ForeName>Dezzarae</ForeName><Initials>D</Initials><AffiliationInfo><Affiliation>Department of Molecular Medicine, the University of Texas Health, San Antonio, TX, 78229, USA.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Luo</LastName><ForeName>Shiwen</ForeName><Initials>S</Initials><AffiliationInfo><Affiliation>Center for Experimental Medicine, the First Affiliated Hospital, Nanchang University, Nanchang, China.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Rao</LastName><ForeName>Hai</ForeName><Initials>H</Initials><AffiliationInfo><Affiliation>Department of Molecular Medicine, the University of Texas Health, San Antonio, TX, 78229, USA. Electronic address: raoh@uthscsa.edu.</Affiliation></AffiliationInfo></Author></AuthorList><Language>eng</Language><GrantList CompleteYN="Y"><Grant><GrantID>R01 GM118350</GrantID><Acronym>GM</Acronym><Agency>NIGMS NIH HHS</Agency><Country>United States</Country></Grant><Grant><GrantID>UL1 TR002645</GrantID><Acronym>TR</Acronym><Agency>NCATS NIH HHS</Agency><Country>United States</Country></Grant></GrantList><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D052061">Research Support, N.I.H., Extramural</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2019</Year><Month>11</Month><Day>21</Day></ArticleDate></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>Biochem Biophys Res 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Yan</name></country><country name="États-Unis"><noRegion><name sortKey="Rios, Lizette" sort="Rios, Lizette" uniqKey="Rios L" first="Lizette" last="Rios">Lizette Rios</name></noRegion><name sortKey="Jasper, Angela M" sort="Jasper, Angela M" uniqKey="Jasper A" first="Angela M" last="Jasper">Angela M. Jasper</name><name sortKey="Luera, Dezzarae" sort="Luera, Dezzarae" uniqKey="Luera D" first="Dezzarae" last="Luera">Dezzarae Luera</name><name sortKey="Rao, Hai" sort="Rao, Hai" uniqKey="Rao H" first="Hai" last="Rao">Hai Rao</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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