Apoptosis inducing factor and mitochondrial NADH dehydrogenases: redox-controlled gear boxes to switch between mitochondrial biogenesis and cell death.
Identifieur interne : 000054 ( Main/Exploration ); précédent : 000053; suivant : 000055Apoptosis inducing factor and mitochondrial NADH dehydrogenases: redox-controlled gear boxes to switch between mitochondrial biogenesis and cell death.
Auteurs : Johannes M. Herrmann [Allemagne] ; Jan Riemer [Allemagne]Source :
- Biological chemistry [ 1437-4315 ] ; 2020.
Abstract
The mitochondrial complex I serves as entry point for NADH into the electron transport chain. In animals, fungi and plants, additional NADH dehydrogenases carry out the same electron transfer reaction, however they do not pump protons. The apoptosis inducing factor (AIF, AIFM1 in humans) is a famous member of this group as it was the first pro-apoptotic protein identified that can induce caspase-independent cell death. Recent studies on AIFM1 and the NADH dehydrogenase Nde1 of baker's yeast revealed two independent and experimentally separable activities of this class of enzymes: On the one hand, these proteins promote the functionality of mitochondrial respiration in different ways: They channel electrons into the respiratory chain and, at least in animals, promote the import of Mia40 (named MIA40 or CHCHD4 in humans) and the assembly of complex I. On the other hand, they can give rise to pro-apoptotic fragments that are released from the mitochondria to trigger cell death. Here we propose that AIFM1 and Nde1 serve as conserved redox switches which measure metabolic conditions on the mitochondrial surface and translate it into a binary life/death decision. This function is conserved among eukaryotic cells and apparently used to purge metabolically compromised cells from populations.
DOI: 10.1515/hsz-2020-0254
PubMed: 32769219
Affiliations:
- Allemagne
- District de Cologne, Rhénanie-Palatinat, Rhénanie-du-Nord-Westphalie
- Cologne, Kaiserslautern
- Université technique de Kaiserslautern
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Herrmann</name><affiliation wicri:level="4"><nlm:affiliation>Department of Cell Biology, University of Kaiserslautern, Erwin-Schrödinger-Strasse 13, D-67663 Kaiserslautern, Germany.</nlm:affiliation><country xml:lang="fr">Allemagne</country><wicri:regionArea>Department of Cell Biology, University of Kaiserslautern, Erwin-Schrödinger-Strasse 13, D-67663 Kaiserslautern</wicri:regionArea><placeName><region type="land" nuts="2">Rhénanie-Palatinat</region><settlement type="city">Kaiserslautern</settlement></placeName><orgName type="university">Université technique de Kaiserslautern</orgName></affiliation></author><author><name sortKey="Riemer, Jan" sort="Riemer, Jan" uniqKey="Riemer J" first="Jan" last="Riemer">Jan Riemer</name><affiliation wicri:level="3"><nlm:affiliation>Department of Biochemistry, University of Cologne, Zülpicher Str. 47A, D-50674 Cologne, Germany.</nlm:affiliation><country xml:lang="fr">Allemagne</country><wicri:regionArea>Department of Biochemistry, University of Cologne, Zülpicher Str. 47A, D-50674 Cologne</wicri:regionArea><placeName><region type="land" nuts="1">Rhénanie-du-Nord-Westphalie</region><region type="district" nuts="2">District de Cologne</region><settlement type="city">Cologne</settlement></placeName></affiliation></author></analytic><series><title level="j">Biological chemistry</title><idno type="eISSN">1437-4315</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">The mitochondrial complex I serves as entry point for NADH into the electron transport chain. In animals, fungi and plants, additional NADH dehydrogenases carry out the same electron transfer reaction, however they do not pump protons. The apoptosis inducing factor (AIF, AIFM1 in humans) is a famous member of this group as it was the first pro-apoptotic protein identified that can induce caspase-independent cell death. Recent studies on AIFM1 and the NADH dehydrogenase Nde1 of baker's yeast revealed two independent and experimentally separable activities of this class of enzymes: On the one hand, these proteins promote the functionality of mitochondrial respiration in different ways: They channel electrons into the respiratory chain and, at least in animals, promote the import of Mia40 (named MIA40 or CHCHD4 in humans) and the assembly of complex I. On the other hand, they can give rise to pro-apoptotic fragments that are released from the mitochondria to trigger cell death. Here we propose that AIFM1 and Nde1 serve as conserved redox switches which measure metabolic conditions on the mitochondrial surface and translate it into a binary life/death decision. This function is conserved among eukaryotic cells and apparently used to purge metabolically compromised cells from populations.</div></front></TEI><pubmed><MedlineCitation Status="Publisher" Owner="NLM"><PMID Version="1">32769219</PMID><DateRevised><Year>2020</Year><Month>08</Month><Day>25</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1437-4315</ISSN><JournalIssue CitedMedium="Internet"><PubDate><Year>2020</Year><Month>Aug</Month><Day>24</Day></PubDate></JournalIssue><Title>Biological chemistry</Title><ISOAbbreviation>Biol Chem</ISOAbbreviation></Journal><ArticleTitle>Apoptosis inducing factor and mitochondrial NADH dehydrogenases: redox-controlled gear boxes to switch between mitochondrial biogenesis and cell death.</ArticleTitle><ELocationID EIdType="doi" ValidYN="Y">10.1515/hsz-2020-0254</ELocationID><ELocationID EIdType="pii" ValidYN="Y">/j/bchm.ahead-of-print/hsz-2020-0254/hsz-2020-0254.xml</ELocationID><Abstract><AbstractText>The mitochondrial complex I serves as entry point for NADH into the electron transport chain. In animals, fungi and plants, additional NADH dehydrogenases carry out the same electron transfer reaction, however they do not pump protons. The apoptosis inducing factor (AIF, AIFM1 in humans) is a famous member of this group as it was the first pro-apoptotic protein identified that can induce caspase-independent cell death. Recent studies on AIFM1 and the NADH dehydrogenase Nde1 of baker's yeast revealed two independent and experimentally separable activities of this class of enzymes: On the one hand, these proteins promote the functionality of mitochondrial respiration in different ways: They channel electrons into the respiratory chain and, at least in animals, promote the import of Mia40 (named MIA40 or CHCHD4 in humans) and the assembly of complex I. On the other hand, they can give rise to pro-apoptotic fragments that are released from the mitochondria to trigger cell death. Here we propose that AIFM1 and Nde1 serve as conserved redox switches which measure metabolic conditions on the mitochondrial surface and translate it into a binary life/death decision. This function is conserved among eukaryotic cells and apparently used to purge metabolically compromised cells from populations.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Herrmann</LastName><ForeName>Johannes M</ForeName><Initials>JM</Initials><Identifier Source="ORCID">https://orcid.org/0000-0003-2081-4506</Identifier><AffiliationInfo><Affiliation>Department of Cell Biology, University of Kaiserslautern, Erwin-Schrödinger-Strasse 13, D-67663 Kaiserslautern, Germany.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Riemer</LastName><ForeName>Jan</ForeName><Initials>J</Initials><AffiliationInfo><Affiliation>Department of Biochemistry, University of Cologne, Zülpicher Str. 47A, D-50674 Cologne, Germany.</Affiliation></AffiliationInfo></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D016454">Review</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2020</Year><Month>08</Month><Day>24</Day></ArticleDate></Article><MedlineJournalInfo><Country>Germany</Country><MedlineTA>Biol Chem</MedlineTA><NlmUniqueID>9700112</NlmUniqueID><ISSNLinking>1431-6730</ISSNLinking></MedlineJournalInfo><CitationSubset>IM</CitationSubset><KeywordList Owner="NOTNLM"><Keyword MajorTopicYN="N">MIA40</Keyword><Keyword MajorTopicYN="N">cell death</Keyword><Keyword MajorTopicYN="N">complex I</Keyword><Keyword MajorTopicYN="N">mitochondria</Keyword><Keyword MajorTopicYN="N">protein import</Keyword><Keyword MajorTopicYN="N">redox</Keyword></KeywordList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="received"><Year>2020</Year><Month>07</Month><Day>15</Day></PubMedPubDate><PubMedPubDate PubStatus="accepted"><Year>2020</Year><Month>08</Month><Day>03</Day></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2020</Year><Month>8</Month><Day>10</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2020</Year><Month>8</Month><Day>10</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2020</Year><Month>8</Month><Day>10</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>aheadofprint</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">32769219</ArticleId><ArticleId IdType="doi">10.1515/hsz-2020-0254</ArticleId><ArticleId IdType="pii">/j/bchm.just-accepted/hsz-2020-0254/hsz-2020-0254.xml</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>Allemagne</li></country><region><li>District de Cologne</li><li>Rhénanie-Palatinat</li><li>Rhénanie-du-Nord-Westphalie</li></region><settlement><li>Cologne</li><li>Kaiserslautern</li></settlement><orgName><li>Université technique de Kaiserslautern</li></orgName></list><tree><country name="Allemagne"><region name="Rhénanie-Palatinat"><name sortKey="Herrmann, Johannes M" sort="Herrmann, Johannes M" uniqKey="Herrmann J" first="Johannes M" last="Herrmann">Johannes M. 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