Calcium channel regulator Mid1 links TORC2-mediated changes in mitochondrial respiration to autophagy.
Identifieur interne : 000B34 ( Main/Exploration ); précédent : 000B33; suivant : 000B35Calcium channel regulator Mid1 links TORC2-mediated changes in mitochondrial respiration to autophagy.
Auteurs : Ariadne Vlahakis [États-Unis] ; Nerea Lopez Muniozguren [États-Unis] ; Ted Powers [États-Unis]Source :
- The Journal of cell biology [ 1540-8140 ] ; 2016.
Descripteurs français
- KwdFr :
- Acides aminés (métabolisme), Autophagie (MeSH), Calcineurine (métabolisme), Canaux calciques (métabolisme), Complexe-2 cible mécanistique de la rapamycine (MeSH), Complexes multiprotéiques (métabolisme), Glycoprotéines membranaires (métabolisme), Mitochondries (métabolisme), Modèles biologiques (MeSH), Protéines de Saccharomyces cerevisiae (métabolisme), Respiration cellulaire (MeSH), Saccharomyces cerevisiae (métabolisme), Sérine-thréonine kinases TOR (métabolisme).
- MESH :
- métabolisme : Acides aminés, Calcineurine, Canaux calciques, Complexes multiprotéiques, Glycoprotéines membranaires, Mitochondries, Protéines de Saccharomyces cerevisiae, Saccharomyces cerevisiae, Sérine-thréonine kinases TOR.
- Autophagie, Complexe-2 cible mécanistique de la rapamycine, Modèles biologiques, Respiration cellulaire.
English descriptors
- KwdEn :
- Amino Acids (metabolism), Autophagy (MeSH), Calcineurin (metabolism), Calcium Channels (metabolism), Cell Respiration (MeSH), Mechanistic Target of Rapamycin Complex 2 (MeSH), Membrane Glycoproteins (metabolism), Mitochondria (metabolism), Models, Biological (MeSH), Multiprotein Complexes (metabolism), Saccharomyces cerevisiae (metabolism), Saccharomyces cerevisiae Proteins (metabolism), TOR Serine-Threonine Kinases (metabolism).
- MESH :
- chemical , metabolism : Amino Acids, Calcineurin, Calcium Channels, Membrane Glycoproteins, Multiprotein Complexes, Saccharomyces cerevisiae Proteins, TOR Serine-Threonine Kinases.
- metabolism : Mitochondria, Saccharomyces cerevisiae.
- Autophagy, Cell Respiration, Mechanistic Target of Rapamycin Complex 2, Models, Biological.
Abstract
Autophagy is a catabolic process that recycles cytoplasmic contents and is crucial for cell survival during stress. The target of rapamycin (TOR) kinase regulates autophagy as part of two distinct protein complexes, TORC1 and TORC2. TORC1 negatively regulates autophagy according to nitrogen availability. In contrast, TORC2 functions as a positive regulator of autophagy during amino acid starvation, via its target kinase Ypk1, by repressing the activity of the calcium-dependent phosphatase calcineurin and promoting the general amino acid control (GAAC) response. Precisely how TORC2-Ypk1 signaling regulates calcineurin within this pathway remains unknown. Here we demonstrate that activation of calcineurin requires Mid1, an endoplasmic reticulum-localized calcium channel regulatory protein implicated in the oxidative stress response. We find that normal mitochondrial respiration is perturbed in TORC2-Ypk1-deficient cells, which results in the accumulation of mitochondrial-derived reactive oxygen species that signal to Mid1 to activate calcineurin, thereby inhibiting the GAAC response and autophagy. These findings describe a novel pathway involving TORC2, mitochondrial oxidative stress, and calcium homeostasis for autophagy regulation.
DOI: 10.1083/jcb.201605030
PubMed: 27899413
PubMed Central: PMC5166500
Affiliations:
Links toward previous steps (curation, corpus...)
Le document en format XML
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Vlahakis</name><affiliation wicri:level="2"><nlm:affiliation>Department of Molecular and Cellular Biology, College of Biological Sciences, University of California, Davis, Davis, CA 95616.</nlm:affiliation><country xml:lang="fr">États-Unis</country><placeName><region type="state">Californie</region></placeName><wicri:cityArea>Department of Molecular and Cellular Biology, College of Biological Sciences, University of California, Davis, Davis</wicri:cityArea></affiliation></author><author><name sortKey="Lopez Muniozguren, Nerea" sort="Lopez Muniozguren, Nerea" uniqKey="Lopez Muniozguren N" first="Nerea" last="Lopez Muniozguren">Nerea Lopez Muniozguren</name><affiliation wicri:level="2"><nlm:affiliation>Department of Molecular and Cellular Biology, College of Biological Sciences, University of California, Davis, Davis, CA 95616.</nlm:affiliation><country xml:lang="fr">États-Unis</country><placeName><region type="state">Californie</region></placeName><wicri:cityArea>Department of Molecular and Cellular Biology, College of Biological Sciences, University of California, Davis, Davis</wicri:cityArea></affiliation></author><author><name sortKey="Powers, Ted" sort="Powers, Ted" uniqKey="Powers T" first="Ted" last="Powers">Ted Powers</name><affiliation wicri:level="1"><nlm:affiliation>Department of Molecular and Cellular Biology, College of Biological Sciences, University of California, Davis, Davis, CA 95616 tpowers@ucdavis.edu.</nlm:affiliation><country wicri:rule="url">États-Unis</country><wicri:regionArea>Department of Molecular and Cellular Biology, College of Biological Sciences, University of California, Davis, Davis</wicri:regionArea><wicri:noRegion>Davis</wicri:noRegion></affiliation></author></analytic><series><title level="j">The Journal of cell biology</title><idno type="eISSN">1540-8140</idno><imprint><date when="2016" type="published">2016</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Amino Acids (metabolism)</term><term>Autophagy (MeSH)</term><term>Calcineurin (metabolism)</term><term>Calcium Channels (metabolism)</term><term>Cell Respiration (MeSH)</term><term>Mechanistic Target of Rapamycin Complex 2 (MeSH)</term><term>Membrane Glycoproteins (metabolism)</term><term>Mitochondria (metabolism)</term><term>Models, Biological (MeSH)</term><term>Multiprotein Complexes (metabolism)</term><term>Saccharomyces cerevisiae (metabolism)</term><term>Saccharomyces cerevisiae Proteins (metabolism)</term><term>TOR Serine-Threonine Kinases (metabolism)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Acides aminés (métabolisme)</term><term>Autophagie (MeSH)</term><term>Calcineurine (métabolisme)</term><term>Canaux calciques (métabolisme)</term><term>Complexe-2 cible mécanistique de la rapamycine (MeSH)</term><term>Complexes multiprotéiques (métabolisme)</term><term>Glycoprotéines membranaires (métabolisme)</term><term>Mitochondries (métabolisme)</term><term>Modèles biologiques (MeSH)</term><term>Protéines de Saccharomyces cerevisiae (métabolisme)</term><term>Respiration cellulaire (MeSH)</term><term>Saccharomyces cerevisiae (métabolisme)</term><term>Sérine-thréonine kinases TOR (métabolisme)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Amino Acids</term><term>Calcineurin</term><term>Calcium Channels</term><term>Membrane Glycoproteins</term><term>Multiprotein Complexes</term><term>Saccharomyces cerevisiae Proteins</term><term>TOR Serine-Threonine Kinases</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Mitochondria</term><term>Saccharomyces cerevisiae</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Acides aminés</term><term>Calcineurine</term><term>Canaux calciques</term><term>Complexes multiprotéiques</term><term>Glycoprotéines membranaires</term><term>Mitochondries</term><term>Protéines de Saccharomyces cerevisiae</term><term>Saccharomyces cerevisiae</term><term>Sérine-thréonine kinases TOR</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Autophagy</term><term>Cell Respiration</term><term>Mechanistic Target of Rapamycin Complex 2</term><term>Models, Biological</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Autophagie</term><term>Complexe-2 cible mécanistique de la rapamycine</term><term>Modèles biologiques</term><term>Respiration cellulaire</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Autophagy is a catabolic process that recycles cytoplasmic contents and is crucial for cell survival during stress. The target of rapamycin (TOR) kinase regulates autophagy as part of two distinct protein complexes, TORC1 and TORC2. TORC1 negatively regulates autophagy according to nitrogen availability. In contrast, TORC2 functions as a positive regulator of autophagy during amino acid starvation, via its target kinase Ypk1, by repressing the activity of the calcium-dependent phosphatase calcineurin and promoting the general amino acid control (GAAC) response. Precisely how TORC2-Ypk1 signaling regulates calcineurin within this pathway remains unknown. Here we demonstrate that activation of calcineurin requires Mid1, an endoplasmic reticulum-localized calcium channel regulatory protein implicated in the oxidative stress response. We find that normal mitochondrial respiration is perturbed in TORC2-Ypk1-deficient cells, which results in the accumulation of mitochondrial-derived reactive oxygen species that signal to Mid1 to activate calcineurin, thereby inhibiting the GAAC response and autophagy. These findings describe a novel pathway involving TORC2, mitochondrial oxidative stress, and calcium homeostasis for autophagy regulation.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">27899413</PMID><DateCompleted><Year>2017</Year><Month>05</Month><Day>29</Day></DateCompleted><DateRevised><Year>2019</Year><Month>10</Month><Day>23</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1540-8140</ISSN><JournalIssue CitedMedium="Internet"><Volume>215</Volume><Issue>6</Issue><PubDate><Year>2016</Year><Month>Dec</Month><Day>19</Day></PubDate></JournalIssue><Title>The Journal of cell biology</Title><ISOAbbreviation>J Cell Biol</ISOAbbreviation></Journal><ArticleTitle>Calcium channel regulator Mid1 links TORC2-mediated changes in mitochondrial respiration to autophagy.</ArticleTitle><Pagination><MedlinePgn>779-788</MedlinePgn></Pagination><Abstract><AbstractText>Autophagy is a catabolic process that recycles cytoplasmic contents and is crucial for cell survival during stress. The target of rapamycin (TOR) kinase regulates autophagy as part of two distinct protein complexes, TORC1 and TORC2. TORC1 negatively regulates autophagy according to nitrogen availability. In contrast, TORC2 functions as a positive regulator of autophagy during amino acid starvation, via its target kinase Ypk1, by repressing the activity of the calcium-dependent phosphatase calcineurin and promoting the general amino acid control (GAAC) response. Precisely how TORC2-Ypk1 signaling regulates calcineurin within this pathway remains unknown. Here we demonstrate that activation of calcineurin requires Mid1, an endoplasmic reticulum-localized calcium channel regulatory protein implicated in the oxidative stress response. We find that normal mitochondrial respiration is perturbed in TORC2-Ypk1-deficient cells, which results in the accumulation of mitochondrial-derived reactive oxygen species that signal to Mid1 to activate calcineurin, thereby inhibiting the GAAC response and autophagy. These findings describe a novel pathway involving TORC2, mitochondrial oxidative stress, and calcium homeostasis for autophagy regulation.</AbstractText><CopyrightInformation>© 2016 Vlahakis et al.</CopyrightInformation></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Vlahakis</LastName><ForeName>Ariadne</ForeName><Initials>A</Initials><Identifier Source="ORCID">http://orcid.org/0000-0003-3452-9925</Identifier><AffiliationInfo><Affiliation>Department of Molecular and Cellular Biology, College of Biological Sciences, University of California, Davis, Davis, CA 95616.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Lopez Muniozguren</LastName><ForeName>Nerea</ForeName><Initials>N</Initials><AffiliationInfo><Affiliation>Department of Molecular and Cellular Biology, College of Biological Sciences, University of California, Davis, Davis, CA 95616.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Powers</LastName><ForeName>Ted</ForeName><Initials>T</Initials><Identifier Source="ORCID">http://orcid.org/0000-0002-2007-3819</Identifier><AffiliationInfo><Affiliation>Department of Molecular and Cellular Biology, College of Biological Sciences, University of California, Davis, Davis, CA 95616 tpowers@ucdavis.edu.</Affiliation></AffiliationInfo></Author></AuthorList><Language>eng</Language><GrantList CompleteYN="Y"><Grant><GrantID>T32 GM007377</GrantID><Acronym>GM</Acronym><Agency>NIGMS NIH HHS</Agency><Country>United States</Country></Grant></GrantList><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2016</Year><Month>11</Month><Day>29</Day></ArticleDate></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>J Cell 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