A pathway linking translation stress to checkpoint kinase 2 signaling in Neurospora crassa.
Identifieur interne : 000399 ( Main/Exploration ); précédent : 000398; suivant : 000400A pathway linking translation stress to checkpoint kinase 2 signaling in Neurospora crassa.
Auteurs : Axel C R. Diernfellner [Allemagne] ; Linda Lauinger [Allemagne] ; Anton Shostak [Allemagne] ; Michael Brunner [Allemagne]Source :
- Proceedings of the National Academy of Sciences of the United States of America [ 1091-6490 ] ; 2019.
Descripteurs français
- KwdFr :
- Biosynthèse des protéines (MeSH), Checkpoint kinase 2 (génétique), Checkpoint kinase 2 (métabolisme), Neurospora crassa (enzymologie), Neurospora crassa (génétique), Protéines fongiques (génétique), Protéines fongiques (métabolisme), Stress physiologique (MeSH), Sérine-thréonine kinases TOR (génétique), Sérine-thréonine kinases TOR (métabolisme), Transduction du signal (MeSH).
- MESH :
- enzymologie : Neurospora crassa.
- génétique : Checkpoint kinase 2, Neurospora crassa, Protéines fongiques, Sérine-thréonine kinases TOR.
- métabolisme : Checkpoint kinase 2, Protéines fongiques, Sérine-thréonine kinases TOR.
- Biosynthèse des protéines, Stress physiologique, Transduction du signal.
English descriptors
- KwdEn :
- Checkpoint Kinase 2 (genetics), Checkpoint Kinase 2 (metabolism), Fungal Proteins (genetics), Fungal Proteins (metabolism), Neurospora crassa (enzymology), Neurospora crassa (genetics), Protein Biosynthesis (MeSH), Signal Transduction (MeSH), Stress, Physiological (MeSH), TOR Serine-Threonine Kinases (genetics), TOR Serine-Threonine Kinases (metabolism).
- MESH :
- chemical , genetics : Checkpoint Kinase 2, Fungal Proteins, TOR Serine-Threonine Kinases.
- chemical , metabolism : Checkpoint Kinase 2, Fungal Proteins, TOR Serine-Threonine Kinases.
- enzymology : Neurospora crassa.
- genetics : Neurospora crassa.
- Protein Biosynthesis, Signal Transduction, Stress, Physiological.
Abstract
Checkpoint kinase 2 (CHK-2) is a key component of the DNA damage response (DDR). CHK-2 is activated by the PIP3-kinase-like kinases (PI3KKs) ataxia telangiectasia mutated (ATM) and ataxia telangiectasia and Rad3-related protein (ATR), and in metazoan also by DNA-dependent protein kinase catalytic subunit (DNA-PKcs). These DNA damage-dependent activation pathways are conserved and additional activation pathways of CHK-2 are not known. Here we show that PERIOD-4 (PRD-4), the CHK-2 ortholog of Neurospora crassa, is part of a signaling pathway that is activated when protein translation is compromised. Translation stress induces phosphorylation of PRD-4 by a PI3KK distinct from ATM and ATR. Our data indicate that the activating PI3KK is mechanistic target of rapamycin (mTOR). We provide evidence that translation stress is sensed by unbalancing the expression levels of an unstable protein phosphatase that antagonizes phosphorylation of PRD-4 by mTOR complex 1 (TORC1). Hence, Neurospora mTOR and PRD-4 appear to coordinate metabolic state and cell cycle progression.
DOI: 10.1073/pnas.1815396116
PubMed: 31413202
PubMed Central: PMC6717302
Affiliations:
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Le document en format XML
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Diernfellner</name><affiliation wicri:level="3"><nlm:affiliation>Biochemistry Center, Heidelberg University, D-69120 Heidelberg, Germany axel.diernfellner@bzh.uni-heidelberg.de michael.brunner@bzh.uni-heidelberg.de.</nlm:affiliation><country wicri:rule="url">Allemagne</country><wicri:regionArea>Biochemistry Center, Heidelberg University, D-69120 Heidelberg</wicri:regionArea><placeName><region type="land" nuts="1">Bade-Wurtemberg</region><region type="district" nuts="2">District de Karlsruhe</region><settlement type="city">Heidelberg</settlement></placeName></affiliation></author><author><name sortKey="Lauinger, Linda" sort="Lauinger, Linda" uniqKey="Lauinger L" first="Linda" last="Lauinger">Linda Lauinger</name><affiliation wicri:level="3"><nlm:affiliation>Biochemistry Center, Heidelberg University, D-69120 Heidelberg, Germany.</nlm:affiliation><country xml:lang="fr">Allemagne</country><wicri:regionArea>Biochemistry Center, Heidelberg University, D-69120 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Brunner</name><affiliation wicri:level="3"><nlm:affiliation>Biochemistry Center, Heidelberg University, D-69120 Heidelberg, Germany axel.diernfellner@bzh.uni-heidelberg.de michael.brunner@bzh.uni-heidelberg.de.</nlm:affiliation><country wicri:rule="url">Allemagne</country><wicri:regionArea>Biochemistry Center, Heidelberg University, D-69120 Heidelberg</wicri:regionArea><placeName><region type="land" nuts="1">Bade-Wurtemberg</region><region type="district" nuts="2">District de Karlsruhe</region><settlement type="city">Heidelberg</settlement></placeName></affiliation></author></analytic><series><title level="j">Proceedings of the National Academy of Sciences of the United States of America</title><idno type="eISSN">1091-6490</idno><imprint><date when="2019" type="published">2019</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Checkpoint Kinase 2 (genetics)</term><term>Checkpoint Kinase 2 (metabolism)</term><term>Fungal Proteins (genetics)</term><term>Fungal Proteins (metabolism)</term><term>Neurospora crassa (enzymology)</term><term>Neurospora crassa (genetics)</term><term>Protein Biosynthesis (MeSH)</term><term>Signal Transduction (MeSH)</term><term>Stress, Physiological (MeSH)</term><term>TOR Serine-Threonine Kinases (genetics)</term><term>TOR Serine-Threonine Kinases (metabolism)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Biosynthèse des protéines (MeSH)</term><term>Checkpoint kinase 2 (génétique)</term><term>Checkpoint kinase 2 (métabolisme)</term><term>Neurospora crassa (enzymologie)</term><term>Neurospora crassa (génétique)</term><term>Protéines fongiques (génétique)</term><term>Protéines fongiques (métabolisme)</term><term>Stress physiologique (MeSH)</term><term>Sérine-thréonine kinases TOR (génétique)</term><term>Sérine-thréonine kinases TOR (métabolisme)</term><term>Transduction du signal (MeSH)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Checkpoint Kinase 2</term><term>Fungal Proteins</term><term>TOR Serine-Threonine Kinases</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Checkpoint Kinase 2</term><term>Fungal Proteins</term><term>TOR Serine-Threonine Kinases</term></keywords><keywords scheme="MESH" qualifier="enzymologie" xml:lang="fr"><term>Neurospora crassa</term></keywords><keywords scheme="MESH" qualifier="enzymology" xml:lang="en"><term>Neurospora crassa</term></keywords><keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Neurospora crassa</term></keywords><keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Checkpoint kinase 2</term><term>Neurospora crassa</term><term>Protéines fongiques</term><term>Sérine-thréonine kinases TOR</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Checkpoint kinase 2</term><term>Protéines fongiques</term><term>Sérine-thréonine kinases TOR</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Protein Biosynthesis</term><term>Signal Transduction</term><term>Stress, Physiological</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Biosynthèse des protéines</term><term>Stress physiologique</term><term>Transduction du signal</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Checkpoint kinase 2 (CHK-2) is a key component of the DNA damage response (DDR). CHK-2 is activated by the PIP3-kinase-like kinases (PI3KKs) ataxia telangiectasia mutated (ATM) and ataxia telangiectasia and Rad3-related protein (ATR), and in metazoan also by DNA-dependent protein kinase catalytic subunit (DNA-PKcs). These DNA damage-dependent activation pathways are conserved and additional activation pathways of CHK-2 are not known. Here we show that PERIOD-4 (PRD-4), the CHK-2 ortholog of <i>Neurospora crassa</i>, is part of a signaling pathway that is activated when protein translation is compromised. Translation stress induces phosphorylation of PRD-4 by a PI3KK distinct from ATM and ATR. Our data indicate that the activating PI3KK is mechanistic target of rapamycin (mTOR). We provide evidence that translation stress is sensed by unbalancing the expression levels of an unstable protein phosphatase that antagonizes phosphorylation of PRD-4 by mTOR complex 1 (TORC1). Hence, <i>Neurospora</i> mTOR and PRD-4 appear to coordinate metabolic state and cell cycle progression.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">31413202</PMID><DateCompleted><Year>2020</Year><Month>03</Month><Day>24</Day></DateCompleted><DateRevised><Year>2020</Year><Month>03</Month><Day>24</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1091-6490</ISSN><JournalIssue CitedMedium="Internet"><Volume>116</Volume><Issue>35</Issue><PubDate><Year>2019</Year><Month>08</Month><Day>27</Day></PubDate></JournalIssue><Title>Proceedings of the National Academy of Sciences of the United States of America</Title><ISOAbbreviation>Proc Natl Acad Sci U S A</ISOAbbreviation></Journal><ArticleTitle>A pathway linking translation stress to checkpoint kinase 2 signaling in <i>Neurospora crassa</i>.</ArticleTitle><Pagination><MedlinePgn>17271-17279</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1073/pnas.1815396116</ELocationID><Abstract><AbstractText>Checkpoint kinase 2 (CHK-2) is a key component of the DNA damage response (DDR). CHK-2 is activated by the PIP3-kinase-like kinases (PI3KKs) ataxia telangiectasia mutated (ATM) and ataxia telangiectasia and Rad3-related protein (ATR), and in metazoan also by DNA-dependent protein kinase catalytic subunit (DNA-PKcs). These DNA damage-dependent activation pathways are conserved and additional activation pathways of CHK-2 are not known. Here we show that PERIOD-4 (PRD-4), the CHK-2 ortholog of <i>Neurospora crassa</i>, is part of a signaling pathway that is activated when protein translation is compromised. Translation stress induces phosphorylation of PRD-4 by a PI3KK distinct from ATM and ATR. Our data indicate that the activating PI3KK is mechanistic target of rapamycin (mTOR). We provide evidence that translation stress is sensed by unbalancing the expression levels of an unstable protein phosphatase that antagonizes phosphorylation of PRD-4 by mTOR complex 1 (TORC1). Hence, <i>Neurospora</i> mTOR and PRD-4 appear to coordinate metabolic state and cell cycle progression.</AbstractText><CopyrightInformation>Copyright © 2019 the Author(s). Published by PNAS.</CopyrightInformation></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Diernfellner</LastName><ForeName>Axel C R</ForeName><Initials>ACR</Initials><AffiliationInfo><Affiliation>Biochemistry Center, Heidelberg University, D-69120 Heidelberg, Germany axel.diernfellner@bzh.uni-heidelberg.de michael.brunner@bzh.uni-heidelberg.de.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Lauinger</LastName><ForeName>Linda</ForeName><Initials>L</Initials><AffiliationInfo><Affiliation>Biochemistry Center, Heidelberg University, D-69120 Heidelberg, Germany.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Shostak</LastName><ForeName>Anton</ForeName><Initials>A</Initials><AffiliationInfo><Affiliation>Biochemistry Center, Heidelberg University, D-69120 Heidelberg, Germany.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Brunner</LastName><ForeName>Michael</ForeName><Initials>M</Initials><AffiliationInfo><Affiliation>Biochemistry Center, Heidelberg University, D-69120 Heidelberg, Germany axel.diernfellner@bzh.uni-heidelberg.de michael.brunner@bzh.uni-heidelberg.de.</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>2019</Year><Month>08</Month><Day>14</Day></ArticleDate></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>Proc Natl Acad Sci U S A</MedlineTA><NlmUniqueID>7505876</NlmUniqueID><ISSNLinking>0027-8424</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D005656">Fungal Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 2.7.1.1</RegistryNumber><NameOfSubstance UI="D058570">TOR Serine-Threonine Kinases</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 2.7.1.11</RegistryNumber><NameOfSubstance UI="D064447">Checkpoint Kinase 2</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D064447" MajorTopicYN="N">Checkpoint Kinase 2</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D005656" MajorTopicYN="N">Fungal Proteins</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D009492" MajorTopicYN="N">Neurospora crassa</DescriptorName><QualifierName UI="Q000201" MajorTopicYN="Y">enzymology</QualifierName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D014176" MajorTopicYN="Y">Protein Biosynthesis</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D015398" MajorTopicYN="Y">Signal Transduction</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D013312" MajorTopicYN="Y">Stress, Physiological</DescriptorName></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></MeshHeadingList><KeywordList Owner="NOTNLM"><Keyword MajorTopicYN="Y">Neurospora crassa</Keyword><Keyword MajorTopicYN="Y">checkpoint kinase 2</Keyword><Keyword MajorTopicYN="Y">circadian clock</Keyword><Keyword MajorTopicYN="Y">mTOR</Keyword><Keyword MajorTopicYN="Y">translation inhibition</Keyword></KeywordList><CoiStatement>The authors declare no conflict of interest.</CoiStatement></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="pubmed"><Year>2019</Year><Month>8</Month><Day>16</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2020</Year><Month>3</Month><Day>25</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2019</Year><Month>8</Month><Day>16</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">31413202</ArticleId><ArticleId IdType="pii">1815396116</ArticleId><ArticleId IdType="doi">10.1073/pnas.1815396116</ArticleId><ArticleId IdType="pmc">PMC6717302</ArticleId></ArticleIdList><ReferenceList><Reference><Citation>Cancer Res. 2000 Nov 1;60(21):5934-6</Citation><ArticleIdList><ArticleId IdType="pubmed">11085506</ArticleId></ArticleIdList></Reference><Reference><Citation>EMBO J. 2001 Dec 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Diernfellner</name></region><name sortKey="Brunner, Michael" sort="Brunner, Michael" uniqKey="Brunner M" first="Michael" last="Brunner">Michael Brunner</name><name sortKey="Lauinger, Linda" sort="Lauinger, Linda" uniqKey="Lauinger L" first="Linda" last="Lauinger">Linda Lauinger</name><name sortKey="Shostak, Anton" sort="Shostak, Anton" uniqKey="Shostak A" first="Anton" last="Shostak">Anton Shostak</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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