The trehalose-6-phosphate phosphatase Tps2 regulates ATG8 transcription and autophagy in Saccharomyces cerevisiae.
Identifieur interne : 000025 ( Main/Exploration ); précédent : 000024; suivant : 000026The trehalose-6-phosphate phosphatase Tps2 regulates ATG8 transcription and autophagy in Saccharomyces cerevisiae.
Auteurs : Bongkeun Kim [Corée du Sud] ; Yongook Lee [Corée du Sud] ; Hyojeong Choi [Corée du Sud] ; Won-Ki Huh [Corée du Sud]Source :
- Autophagy [ 1554-8635 ] ; 2020.
Abstract
Macroautophagy/autophagy is an important catabolic process for maintaining cellular homeostasis by adapting to various stress conditions. Autophagy is mediated by a double-membrane autophagosome, which sequesters a portion of cytoplasmic components for delivery to the vacuole. Several autophagy-related (ATG) genes play crucial roles in autophagosome formation. The induction of ATG genes must be tightly regulated to maintain a proper autophagic activity, but their regulatory mechanisms are still largely unknown. Here, we report that the trehalose-6-phosphate phosphatase Tps2 functions as a positive regulator of autophagy in Saccharomyces cerevisiae. Cellular trehalose levels do not affect autophagy regulation by Tps2. Loss of Tps2 leads to impaired autophagic flux and reduced ATG8 expression under nitrogen starvation. In tps2Δ cells, Ume6 is predominantly dephosphorylated and represses ATG8 transcription by binding to its promoter region. Tps2 regulates nuclear translocation and activation of Rim15 kinase, a negative regulator of Ume6, by causing the dissociation of Rim15 from the 14-3-3 proteins Bmh1/2 under nitrogen starvation, suggesting that Rim15 mediates the function of Tps2 as a positive regulator of ATG8 induction. Furthermore, Tps2 plays a crucial role in the dephosphorylation of Ser1061 and Thr1075 residues of Rim15, which is important for controlling the dissociation of Rim15 from Bmh1/2 under nitrogen starvation. Together, our results reveal the role of Tps2 as a positive regulator of autophagy and provide new insight into the regulatory mechanisms of ATG gene expression.Abbreviations: ATG: autophagy-related; ChIP: chromatin immunoprecipitation; Co-IP: co-immunoprecipitation; DAPI: 4',6-diamidino-2-phenylindole; GFP: green fluorescent protein; PKA: protein kinase A; PtdIns3K: phosphatidylinositol 3-kinase; Rim15KI: kinase-inactive Rim15; Rim15-2A: Rim15S1061A,T1075A; TEM: transmission electron microscopy; TORC1: target of rapamycin complex 1.
DOI: 10.1080/15548627.2020.1746592
PubMed: 32240040
Affiliations:
Links toward previous steps (curation, corpus...)
Le document en format XML
<record><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">The trehalose-6-phosphate phosphatase Tps2 regulates <i>ATG8</i> transcription and autophagy in <i>Saccharomyces cerevisiae</i>.</title><author><name sortKey="Kim, Bongkeun" sort="Kim, Bongkeun" uniqKey="Kim B" first="Bongkeun" last="Kim">Bongkeun Kim</name><affiliation wicri:level="4"><nlm:affiliation>School of Biological Sciences, Seoul National University, Seoul, Republic of Korea.</nlm:affiliation><country xml:lang="fr">Corée du Sud</country><wicri:regionArea>School of Biological Sciences, Seoul National University, Seoul</wicri:regionArea><placeName><settlement type="city">Séoul</settlement><region type="capital">Région capitale de Séoul</region></placeName><orgName type="university">Université nationale de Séoul</orgName></affiliation></author><author><name sortKey="Lee, Yongook" sort="Lee, Yongook" uniqKey="Lee Y" first="Yongook" last="Lee">Yongook Lee</name><affiliation wicri:level="4"><nlm:affiliation>School of Biological Sciences, Seoul National University, Seoul, Republic of Korea.</nlm:affiliation><country xml:lang="fr">Corée du Sud</country><wicri:regionArea>School of Biological Sciences, Seoul National University, Seoul</wicri:regionArea><placeName><settlement type="city">Séoul</settlement><region type="capital">Région capitale de Séoul</region></placeName><orgName type="university">Université nationale de Séoul</orgName></affiliation></author><author><name sortKey="Choi, Hyojeong" sort="Choi, Hyojeong" uniqKey="Choi H" first="Hyojeong" last="Choi">Hyojeong Choi</name><affiliation wicri:level="4"><nlm:affiliation>School of Biological Sciences, Seoul National University, Seoul, Republic of Korea.</nlm:affiliation><country xml:lang="fr">Corée du Sud</country><wicri:regionArea>School of Biological Sciences, Seoul National University, Seoul</wicri:regionArea><placeName><settlement type="city">Séoul</settlement><region type="capital">Région capitale de Séoul</region></placeName><orgName type="university">Université nationale de Séoul</orgName></affiliation></author><author><name sortKey="Huh, Won Ki" sort="Huh, Won Ki" uniqKey="Huh W" first="Won-Ki" last="Huh">Won-Ki Huh</name><affiliation wicri:level="4"><nlm:affiliation>School of Biological Sciences, Seoul National University, Seoul, Republic of Korea.</nlm:affiliation><country xml:lang="fr">Corée du Sud</country><wicri:regionArea>School of Biological Sciences, Seoul National University, Seoul</wicri:regionArea><placeName><settlement type="city">Séoul</settlement><region type="capital">Région capitale de Séoul</region></placeName><orgName type="university">Université nationale de Séoul</orgName></affiliation><affiliation wicri:level="4"><nlm:affiliation>Institute of Microbiology, Seoul National University, Seoul, Republic of Korea.</nlm:affiliation><country xml:lang="fr">Corée du Sud</country><wicri:regionArea>Institute of Microbiology, Seoul National University, Seoul</wicri:regionArea><placeName><settlement type="city">Séoul</settlement><region type="capital">Région capitale de Séoul</region></placeName><orgName type="university">Université nationale de Séoul</orgName></affiliation></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2020">2020</date><idno type="RBID">pubmed:32240040</idno><idno type="pmid">32240040</idno><idno type="doi">10.1080/15548627.2020.1746592</idno><idno type="wicri:Area/Main/Corpus">000094</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Corpus" wicri:corpus="PubMed">000094</idno><idno type="wicri:Area/Main/Curation">000094</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Curation">000094</idno><idno type="wicri:Area/Main/Exploration">000094</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">The trehalose-6-phosphate phosphatase Tps2 regulates <i>ATG8</i> transcription and autophagy in <i>Saccharomyces cerevisiae</i>.</title><author><name sortKey="Kim, Bongkeun" sort="Kim, Bongkeun" uniqKey="Kim B" first="Bongkeun" last="Kim">Bongkeun Kim</name><affiliation wicri:level="4"><nlm:affiliation>School of Biological Sciences, Seoul National University, Seoul, Republic of Korea.</nlm:affiliation><country xml:lang="fr">Corée du Sud</country><wicri:regionArea>School of Biological Sciences, Seoul National University, Seoul</wicri:regionArea><placeName><settlement type="city">Séoul</settlement><region type="capital">Région capitale de Séoul</region></placeName><orgName type="university">Université nationale de Séoul</orgName></affiliation></author><author><name sortKey="Lee, Yongook" sort="Lee, Yongook" uniqKey="Lee Y" first="Yongook" last="Lee">Yongook Lee</name><affiliation wicri:level="4"><nlm:affiliation>School of Biological Sciences, Seoul National University, Seoul, Republic of Korea.</nlm:affiliation><country xml:lang="fr">Corée du Sud</country><wicri:regionArea>School of Biological Sciences, Seoul National University, Seoul</wicri:regionArea><placeName><settlement type="city">Séoul</settlement><region type="capital">Région capitale de Séoul</region></placeName><orgName type="university">Université nationale de Séoul</orgName></affiliation></author><author><name sortKey="Choi, Hyojeong" sort="Choi, Hyojeong" uniqKey="Choi H" first="Hyojeong" last="Choi">Hyojeong Choi</name><affiliation wicri:level="4"><nlm:affiliation>School of Biological Sciences, Seoul National University, Seoul, Republic of Korea.</nlm:affiliation><country xml:lang="fr">Corée du Sud</country><wicri:regionArea>School of Biological Sciences, Seoul National University, Seoul</wicri:regionArea><placeName><settlement type="city">Séoul</settlement><region type="capital">Région capitale de Séoul</region></placeName><orgName type="university">Université nationale de Séoul</orgName></affiliation></author><author><name sortKey="Huh, Won Ki" sort="Huh, Won Ki" uniqKey="Huh W" first="Won-Ki" last="Huh">Won-Ki Huh</name><affiliation wicri:level="4"><nlm:affiliation>School of Biological Sciences, Seoul National University, Seoul, Republic of Korea.</nlm:affiliation><country xml:lang="fr">Corée du Sud</country><wicri:regionArea>School of Biological Sciences, Seoul National University, Seoul</wicri:regionArea><placeName><settlement type="city">Séoul</settlement><region type="capital">Région capitale de Séoul</region></placeName><orgName type="university">Université nationale de Séoul</orgName></affiliation><affiliation wicri:level="4"><nlm:affiliation>Institute of Microbiology, Seoul National University, Seoul, Republic of Korea.</nlm:affiliation><country xml:lang="fr">Corée du Sud</country><wicri:regionArea>Institute of Microbiology, Seoul National University, Seoul</wicri:regionArea><placeName><settlement type="city">Séoul</settlement><region type="capital">Région capitale de Séoul</region></placeName><orgName type="university">Université nationale de Séoul</orgName></affiliation></author></analytic><series><title level="j">Autophagy</title><idno type="eISSN">1554-8635</idno><imprint><date when="2020" type="published">2020</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Macroautophagy/autophagy is an important catabolic process for maintaining cellular homeostasis by adapting to various stress conditions. Autophagy is mediated by a double-membrane autophagosome, which sequesters a portion of cytoplasmic components for delivery to the vacuole. Several autophagy-related (<i>ATG</i>) genes play crucial roles in autophagosome formation. The induction of <i>ATG</i> genes must be tightly regulated to maintain a proper autophagic activity, but their regulatory mechanisms are still largely unknown. Here, we report that the trehalose-6-phosphate phosphatase Tps2 functions as a positive regulator of autophagy in <i>Saccharomyces cerevisiae</i>. Cellular trehalose levels do not affect autophagy regulation by Tps2. Loss of Tps2 leads to impaired autophagic flux and reduced <i>ATG8</i> expression under nitrogen starvation. In <i>tps2</i>Δ cells, Ume6 is predominantly dephosphorylated and represses <i>ATG8</i> transcription by binding to its promoter region. Tps2 regulates nuclear translocation and activation of Rim15 kinase, a negative regulator of Ume6, by causing the dissociation of Rim15 from the 14-3-3 proteins Bmh1/2 under nitrogen starvation, suggesting that Rim15 mediates the function of Tps2 as a positive regulator of <i>ATG8</i> induction. Furthermore, Tps2 plays a crucial role in the dephosphorylation of Ser1061 and Thr1075 residues of Rim15, which is important for controlling the dissociation of Rim15 from Bmh1/2 under nitrogen starvation. Together, our results reveal the role of Tps2 as a positive regulator of autophagy and provide new insight into the regulatory mechanisms of <i>ATG</i> gene expression.<b>Abbreviations:</b> ATG: autophagy-related; ChIP: chromatin immunoprecipitation; Co-IP: co-immunoprecipitation; DAPI: 4',6-diamidino-2-phenylindole; GFP: green fluorescent protein; PKA: protein kinase A; PtdIns3K: phosphatidylinositol 3-kinase; Rim15KI: kinase-inactive Rim15; Rim15-2A: Rim15<sup>S1061A,T1075A</sup>; TEM: transmission electron microscopy; TORC1: target of rapamycin complex 1.</div></front></TEI><pubmed><MedlineCitation Status="Publisher" Owner="NLM"><PMID Version="1">32240040</PMID><DateRevised><Year>2020</Year><Month>04</Month><Day>02</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1554-8635</ISSN><JournalIssue CitedMedium="Internet"><PubDate><Year>2020</Year><Month>Apr</Month><Day>02</Day></PubDate></JournalIssue><Title>Autophagy</Title><ISOAbbreviation>Autophagy</ISOAbbreviation></Journal><ArticleTitle>The trehalose-6-phosphate phosphatase Tps2 regulates <i>ATG8</i> transcription and autophagy in <i>Saccharomyces cerevisiae</i>.</ArticleTitle><Pagination><MedlinePgn>1-15</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1080/15548627.2020.1746592</ELocationID><Abstract><AbstractText>Macroautophagy/autophagy is an important catabolic process for maintaining cellular homeostasis by adapting to various stress conditions. Autophagy is mediated by a double-membrane autophagosome, which sequesters a portion of cytoplasmic components for delivery to the vacuole. Several autophagy-related (<i>ATG</i>) genes play crucial roles in autophagosome formation. The induction of <i>ATG</i> genes must be tightly regulated to maintain a proper autophagic activity, but their regulatory mechanisms are still largely unknown. Here, we report that the trehalose-6-phosphate phosphatase Tps2 functions as a positive regulator of autophagy in <i>Saccharomyces cerevisiae</i>. Cellular trehalose levels do not affect autophagy regulation by Tps2. Loss of Tps2 leads to impaired autophagic flux and reduced <i>ATG8</i> expression under nitrogen starvation. In <i>tps2</i>Δ cells, Ume6 is predominantly dephosphorylated and represses <i>ATG8</i> transcription by binding to its promoter region. Tps2 regulates nuclear translocation and activation of Rim15 kinase, a negative regulator of Ume6, by causing the dissociation of Rim15 from the 14-3-3 proteins Bmh1/2 under nitrogen starvation, suggesting that Rim15 mediates the function of Tps2 as a positive regulator of <i>ATG8</i> induction. Furthermore, Tps2 plays a crucial role in the dephosphorylation of Ser1061 and Thr1075 residues of Rim15, which is important for controlling the dissociation of Rim15 from Bmh1/2 under nitrogen starvation. Together, our results reveal the role of Tps2 as a positive regulator of autophagy and provide new insight into the regulatory mechanisms of <i>ATG</i> gene expression.<b>Abbreviations:</b> ATG: autophagy-related; ChIP: chromatin immunoprecipitation; Co-IP: co-immunoprecipitation; DAPI: 4',6-diamidino-2-phenylindole; GFP: green fluorescent protein; PKA: protein kinase A; PtdIns3K: phosphatidylinositol 3-kinase; Rim15KI: kinase-inactive Rim15; Rim15-2A: Rim15<sup>S1061A,T1075A</sup>; TEM: transmission electron microscopy; TORC1: target of rapamycin complex 1.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Kim</LastName><ForeName>Bongkeun</ForeName><Initials>B</Initials><AffiliationInfo><Affiliation>School of Biological Sciences, Seoul National University, Seoul, Republic of Korea.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Lee</LastName><ForeName>Yongook</ForeName><Initials>Y</Initials><AffiliationInfo><Affiliation>School of Biological Sciences, Seoul National University, Seoul, Republic of Korea.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Choi</LastName><ForeName>Hyojeong</ForeName><Initials>H</Initials><AffiliationInfo><Affiliation>School of Biological Sciences, Seoul National University, Seoul, Republic of Korea.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Huh</LastName><ForeName>Won-Ki</ForeName><Initials>WK</Initials><Identifier Source="ORCID">https://orcid.org/0000-0002-9091-6594</Identifier><AffiliationInfo><Affiliation>School of Biological Sciences, Seoul National University, Seoul, Republic of Korea.</Affiliation></AffiliationInfo><AffiliationInfo><Affiliation>Institute of Microbiology, Seoul National University, Seoul, Republic of Korea.</Affiliation></AffiliationInfo></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2020</Year><Month>04</Month><Day>02</Day></ArticleDate></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>Autophagy</MedlineTA><NlmUniqueID>101265188</NlmUniqueID><ISSNLinking>1554-8627</ISSNLinking></MedlineJournalInfo><CitationSubset>IM</CitationSubset><KeywordList Owner="NOTNLM"><Keyword MajorTopicYN="N">ATG8</Keyword><Keyword MajorTopicYN="N">Rim15</Keyword><Keyword MajorTopicYN="N">Saccharomyces cerevisiae</Keyword><Keyword MajorTopicYN="N">Tps2</Keyword><Keyword MajorTopicYN="N">Ume6</Keyword><Keyword MajorTopicYN="N">autophagy</Keyword><Keyword MajorTopicYN="N">nitrogen starvation</Keyword><Keyword MajorTopicYN="N">trehalose</Keyword></KeywordList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="entrez"><Year>2020</Year><Month>4</Month><Day>3</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2020</Year><Month>4</Month><Day>3</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2020</Year><Month>4</Month><Day>3</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>aheadofprint</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">32240040</ArticleId><ArticleId IdType="doi">10.1080/15548627.2020.1746592</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>Corée du Sud</li></country><region><li>Région capitale de Séoul</li></region><settlement><li>Séoul</li></settlement><orgName><li>Université nationale de Séoul</li></orgName></list><tree><country name="Corée du Sud"><region name="Région capitale de Séoul"><name sortKey="Kim, Bongkeun" sort="Kim, Bongkeun" uniqKey="Kim B" first="Bongkeun" last="Kim">Bongkeun Kim</name></region><name sortKey="Choi, Hyojeong" sort="Choi, Hyojeong" uniqKey="Choi H" first="Hyojeong" last="Choi">Hyojeong Choi</name><name sortKey="Huh, Won Ki" sort="Huh, Won Ki" uniqKey="Huh W" first="Won-Ki" last="Huh">Won-Ki Huh</name><name sortKey="Huh, Won Ki" sort="Huh, Won Ki" uniqKey="Huh W" first="Won-Ki" last="Huh">Won-Ki Huh</name><name sortKey="Lee, Yongook" sort="Lee, Yongook" uniqKey="Lee Y" first="Yongook" last="Lee">Yongook Lee</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
EXPLOR_STEP=$WICRI_ROOT/Bois/explor/RapamycinFungusV1/Data/Main/Exploration
HfdSelect -h $EXPLOR_STEP/biblio.hfd -nk 000025 | SxmlIndent | more
Ou
HfdSelect -h $EXPLOR_AREA/Data/Main/Exploration/biblio.hfd -nk 000025 | SxmlIndent | more
Pour mettre un lien sur cette page dans le réseau Wicri
{{Explor lien
|wiki= Bois
|area= RapamycinFungusV1
|flux= Main
|étape= Exploration
|type= RBID
|clé= pubmed:32240040
|texte= The trehalose-6-phosphate phosphatase Tps2 regulates ATG8 transcription and autophagy in Saccharomyces cerevisiae.
}}
Pour générer des pages wiki
HfdIndexSelect -h $EXPLOR_AREA/Data/Main/Exploration/RBID.i -Sk "pubmed:32240040" \
| HfdSelect -Kh $EXPLOR_AREA/Data/Main/Exploration/biblio.hfd \
| NlmPubMed2Wicri -a RapamycinFungusV1
| This area was generated with Dilib version V0.6.38. |  |