TORC1-regulated protein kinase Npr1 phosphorylates Orm to stimulate complex sphingolipid synthesis.
Identifieur interne : 000F69 ( Main/Exploration ); précédent : 000F68; suivant : 000F70TORC1-regulated protein kinase Npr1 phosphorylates Orm to stimulate complex sphingolipid synthesis.
Auteurs : Mitsugu Shimobayashi [Suisse] ; Wolfgang Oppliger ; Suzette Moes ; Paul Jenö ; Michael N. HallSource :
- Molecular biology of the cell [ 1939-4586 ] ; 2013.
Descripteurs français
- KwdFr :
- Facteurs de transcription (antagonistes et inhibiteurs), Facteurs de transcription (métabolisme), Homéostasie (MeSH), Membrane cellulaire (métabolisme), Phosphorylation (MeSH), Protein kinases (métabolisme), Protéines de Saccharomyces cerevisiae (antagonistes et inhibiteurs), Protéines de Saccharomyces cerevisiae (métabolisme), Saccharomyces cerevisiae (métabolisme), Serine C-palmitoyltransferase (génétique), Sphingolipides (biosynthèse), Systèmes de transport d'acides aminés (métabolisme).
- MESH :
- antagonistes et inhibiteurs : Facteurs de transcription, Protéines de Saccharomyces cerevisiae.
- biosynthèse : Sphingolipides.
- génétique : Serine C-palmitoyltransferase.
- métabolisme : Facteurs de transcription, Membrane cellulaire, Protein kinases, Protéines de Saccharomyces cerevisiae, Saccharomyces cerevisiae, Systèmes de transport d'acides aminés.
- Homéostasie, Phosphorylation.
English descriptors
- KwdEn :
- Amino Acid Transport Systems (metabolism), Cell Membrane (metabolism), Homeostasis (MeSH), Phosphorylation (MeSH), Protein Kinases (metabolism), Saccharomyces cerevisiae (metabolism), Saccharomyces cerevisiae Proteins (antagonists & inhibitors), Saccharomyces cerevisiae Proteins (metabolism), Serine C-Palmitoyltransferase (genetics), Sphingolipids (biosynthesis), Transcription Factors (antagonists & inhibitors), Transcription Factors (metabolism).
- MESH :
- chemical , antagonists & inhibitors : Saccharomyces cerevisiae Proteins, Transcription Factors.
- chemical , biosynthesis : Sphingolipids.
- chemical , genetics : Serine C-Palmitoyltransferase.
- chemical , metabolism : Amino Acid Transport Systems, Protein Kinases, Saccharomyces cerevisiae Proteins, Transcription Factors.
- metabolism : Cell Membrane, Saccharomyces cerevisiae.
- Homeostasis, Phosphorylation.
Abstract
The evolutionarily conserved Orm1 and Orm2 proteins mediate sphingolipid homeostasis. However, the homologous Orm proteins and the signaling pathways modulating their phosphorylation and function are incompletely characterized. Here we demonstrate that inhibition of nutrient-sensitive target of rapamycin complex 1 (TORC1) stimulates Orm phosphorylation and synthesis of complex sphingolipids in Saccharomyces cerevisiae. TORC1 inhibition activates the kinase Npr1 that directly phosphorylates and activates the Orm proteins. Npr1-phosphorylated Orm1 and Orm2 stimulate de novo synthesis of complex sphingolipids downstream of serine palmitoyltransferase. Complex sphingolipids in turn stimulate plasma membrane localization and activity of the nutrient scavenging general amino acid permease 1. Thus activation of Orm and complex sphingolipid synthesis upon TORC1 inhibition is a physiological response to starvation.
DOI: 10.1091/mbc.E12-10-0753
PubMed: 23363605
PubMed Central: PMC3596256
Affiliations:
Links toward previous steps (curation, corpus...)
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Hall</name></author></analytic><series><title level="j">Molecular biology of the cell</title><idno type="eISSN">1939-4586</idno><imprint><date when="2013" type="published">2013</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Amino Acid Transport Systems (metabolism)</term><term>Cell Membrane (metabolism)</term><term>Homeostasis (MeSH)</term><term>Phosphorylation (MeSH)</term><term>Protein Kinases (metabolism)</term><term>Saccharomyces cerevisiae (metabolism)</term><term>Saccharomyces cerevisiae Proteins (antagonists & inhibitors)</term><term>Saccharomyces cerevisiae Proteins (metabolism)</term><term>Serine C-Palmitoyltransferase (genetics)</term><term>Sphingolipids (biosynthesis)</term><term>Transcription Factors (antagonists & inhibitors)</term><term>Transcription Factors (metabolism)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Facteurs de transcription (antagonistes et inhibiteurs)</term><term>Facteurs de transcription (métabolisme)</term><term>Homéostasie (MeSH)</term><term>Membrane cellulaire (métabolisme)</term><term>Phosphorylation (MeSH)</term><term>Protein kinases (métabolisme)</term><term>Protéines de Saccharomyces cerevisiae (antagonistes et inhibiteurs)</term><term>Protéines de Saccharomyces cerevisiae (métabolisme)</term><term>Saccharomyces cerevisiae (métabolisme)</term><term>Serine C-palmitoyltransferase (génétique)</term><term>Sphingolipides (biosynthèse)</term><term>Systèmes de transport d'acides aminés (métabolisme)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="antagonists & inhibitors" xml:lang="en"><term>Saccharomyces cerevisiae Proteins</term><term>Transcription Factors</term></keywords><keywords scheme="MESH" type="chemical" qualifier="biosynthesis" xml:lang="en"><term>Sphingolipids</term></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Serine C-Palmitoyltransferase</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Amino Acid Transport Systems</term><term>Protein Kinases</term><term>Saccharomyces cerevisiae Proteins</term><term>Transcription Factors</term></keywords><keywords scheme="MESH" qualifier="antagonistes et inhibiteurs" xml:lang="fr"><term>Facteurs de transcription</term><term>Protéines de Saccharomyces cerevisiae</term></keywords><keywords scheme="MESH" qualifier="biosynthèse" xml:lang="fr"><term>Sphingolipides</term></keywords><keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Serine C-palmitoyltransferase</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Cell Membrane</term><term>Saccharomyces cerevisiae</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Facteurs de transcription</term><term>Membrane cellulaire</term><term>Protein kinases</term><term>Protéines de Saccharomyces cerevisiae</term><term>Saccharomyces cerevisiae</term><term>Systèmes de transport d'acides aminés</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Homeostasis</term><term>Phosphorylation</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Homéostasie</term><term>Phosphorylation</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">The evolutionarily conserved Orm1 and Orm2 proteins mediate sphingolipid homeostasis. However, the homologous Orm proteins and the signaling pathways modulating their phosphorylation and function are incompletely characterized. Here we demonstrate that inhibition of nutrient-sensitive target of rapamycin complex 1 (TORC1) stimulates Orm phosphorylation and synthesis of complex sphingolipids in Saccharomyces cerevisiae. TORC1 inhibition activates the kinase Npr1 that directly phosphorylates and activates the Orm proteins. Npr1-phosphorylated Orm1 and Orm2 stimulate de novo synthesis of complex sphingolipids downstream of serine palmitoyltransferase. Complex sphingolipids in turn stimulate plasma membrane localization and activity of the nutrient scavenging general amino acid permease 1. Thus activation of Orm and complex sphingolipid synthesis upon TORC1 inhibition is a physiological response to starvation.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">23363605</PMID><DateCompleted><Year>2013</Year><Month>09</Month><Day>13</Day></DateCompleted><DateRevised><Year>2018</Year><Month>11</Month><Day>13</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1939-4586</ISSN><JournalIssue CitedMedium="Internet"><Volume>24</Volume><Issue>6</Issue><PubDate><Year>2013</Year><Month>Mar</Month></PubDate></JournalIssue><Title>Molecular biology of the cell</Title><ISOAbbreviation>Mol Biol Cell</ISOAbbreviation></Journal><ArticleTitle>TORC1-regulated protein kinase Npr1 phosphorylates Orm to stimulate complex sphingolipid synthesis.</ArticleTitle><Pagination><MedlinePgn>870-81</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1091/mbc.E12-10-0753</ELocationID><Abstract><AbstractText>The evolutionarily conserved Orm1 and Orm2 proteins mediate sphingolipid homeostasis. However, the homologous Orm proteins and the signaling pathways modulating their phosphorylation and function are incompletely characterized. Here we demonstrate that inhibition of nutrient-sensitive target of rapamycin complex 1 (TORC1) stimulates Orm phosphorylation and synthesis of complex sphingolipids in Saccharomyces cerevisiae. TORC1 inhibition activates the kinase Npr1 that directly phosphorylates and activates the Orm proteins. Npr1-phosphorylated Orm1 and Orm2 stimulate de novo synthesis of complex sphingolipids downstream of serine palmitoyltransferase. Complex sphingolipids in turn stimulate plasma membrane localization and activity of the nutrient scavenging general amino acid permease 1. 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IdType="pubmed">9475724</ArticleId></ArticleIdList></Reference><Reference><Citation>Yeast. 1998 Jul;14(10):953-61</Citation><ArticleIdList><ArticleId IdType="pubmed">9717241</ArticleId></ArticleIdList></Reference><Reference><Citation>J Biol Chem. 1998 Nov 13;273(46):30688-94</Citation><ArticleIdList><ArticleId IdType="pubmed">9804843</ArticleId></ArticleIdList></Reference><Reference><Citation>EMBO J. 1998 Dec 1;17(23):6924-31</Citation><ArticleIdList><ArticleId IdType="pubmed">9843498</ArticleId></ArticleIdList></Reference><Reference><Citation>J Bacteriol. 1999 Feb;181(4):1134-40</Citation><ArticleIdList><ArticleId IdType="pubmed">9973338</ArticleId></ArticleIdList></Reference><Reference><Citation>J Cell Biol. 1999 Sep 20;146(6):1227-38</Citation><ArticleIdList><ArticleId IdType="pubmed">10491387</ArticleId></ArticleIdList></Reference><Reference><Citation>Nature. 1999 Dec 9;402(6762):689-92</Citation><ArticleIdList><ArticleId IdType="pubmed">10604478</ArticleId></ArticleIdList></Reference><Reference><Citation>Proc Natl Acad Sci U S A. 1999 Dec 21;96(26):14866-70</Citation><ArticleIdList><ArticleId IdType="pubmed">10611304</ArticleId></ArticleIdList></Reference><Reference><Citation>Genes Dev. 1999 Dec 15;13(24):3271-9</Citation><ArticleIdList><ArticleId IdType="pubmed">10617575</ArticleId></ArticleIdList></Reference><Reference><Citation>J Biol Chem. 2000 Mar 17;275(11):7597-603</Citation><ArticleIdList><ArticleId IdType="pubmed">10713067</ArticleId></ArticleIdList></Reference><Reference><Citation>EMBO J. 2000 Jun 15;19(12):2824-33</Citation><ArticleIdList><ArticleId IdType="pubmed">10856228</ArticleId></ArticleIdList></Reference><Reference><Citation>EMBO J. 2001 Jun 1;20(11):2655-65</Citation><ArticleIdList><ArticleId IdType="pubmed">11387200</ArticleId></ArticleIdList></Reference><Reference><Citation>Mol Biol Cell. 2001 Nov;12(11):3417-27</Citation><ArticleIdList><ArticleId IdType="pubmed">11694577</ArticleId></ArticleIdList></Reference><Reference><Citation>J Biol Chem. 2001 Nov 23;276(47):43939-48</Citation><ArticleIdList><ArticleId IdType="pubmed">11500493</ArticleId></ArticleIdList></Reference><Reference><Citation>Curr Genet. 2001 Dec;40(4):221-33</Citation><ArticleIdList><ArticleId IdType="pubmed">11795842</ArticleId></ArticleIdList></Reference><Reference><Citation>Methods Enzymol. 2002;351:325-38</Citation><ArticleIdList><ArticleId IdType="pubmed">12073353</ArticleId></ArticleIdList></Reference><Reference><Citation>Genetics. 2002 Aug;161(4):1453-64</Citation><ArticleIdList><ArticleId IdType="pubmed">12196392</ArticleId></ArticleIdList></Reference><Reference><Citation>Mol Cell. 2002 Sep;10(3):457-68</Citation><ArticleIdList><ArticleId IdType="pubmed">12408816</ArticleId></ArticleIdList></Reference><Reference><Citation>Mol Biol Cell. 2003 Mar;14(3):1204-20</Citation><ArticleIdList><ArticleId IdType="pubmed">12631735</ArticleId></ArticleIdList></Reference><Reference><Citation>Cell. 1989 Feb 24;56(4):527-37</Citation><ArticleIdList><ArticleId IdType="pubmed">2537149</ArticleId></ArticleIdList></Reference><Reference><Citation>Proc Natl Acad Sci U S A. 1994 Aug 16;91(17):7899-902</Citation><ArticleIdList><ArticleId IdType="pubmed">8058731</ArticleId></ArticleIdList></Reference><Reference><Citation>J Cell Biol. 1997 Jun 30;137(7):1469-82</Citation><ArticleIdList><ArticleId IdType="pubmed">9199164</ArticleId></ArticleIdList></Reference><Reference><Citation>EMBO J. 2005 Feb 23;24(4):730-41</Citation><ArticleIdList><ArticleId IdType="pubmed">15692566</ArticleId></ArticleIdList></Reference><Reference><Citation>Cell. 2006 Feb 10;124(3):471-84</Citation><ArticleIdList><ArticleId IdType="pubmed">16469695</ArticleId></ArticleIdList></Reference><Reference><Citation>Mol Biol Cell. 2006 Mar;17(3):1164-75</Citation><ArticleIdList><ArticleId IdType="pubmed">16381812</ArticleId></ArticleIdList></Reference><Reference><Citation>Mol Cell Proteomics. 2006 Apr;5(4):749-57</Citation><ArticleIdList><ArticleId IdType="pubmed">16340016</ArticleId></ArticleIdList></Reference><Reference><Citation>Oncogene. 2006 Oct 16;25(48):6392-415</Citation><ArticleIdList><ArticleId IdType="pubmed">17041625</ArticleId></ArticleIdList></Reference><Reference><Citation>Mol Biol Cell. 2007 Aug;18(8):3068-80</Citation><ArticleIdList><ArticleId IdType="pubmed">17553927</ArticleId></ArticleIdList></Reference><Reference><Citation>Nature. 2007 Jul 26;448(7152):470-3</Citation><ArticleIdList><ArticleId IdType="pubmed">17611496</ArticleId></ArticleIdList></Reference><Reference><Citation>J Biol Chem. 2007 Sep 28;282(39):28485-92</Citation><ArticleIdList><ArticleId IdType="pubmed">17686782</ArticleId></ArticleIdList></Reference><Reference><Citation>Nat Rev Mol Cell Biol. 2008 Feb;9(2):139-50</Citation><ArticleIdList><ArticleId IdType="pubmed">18216770</ArticleId></ArticleIdList></Reference><Reference><Citation>Cell Metab. 2008 Feb;7(2):148-58</Citation><ArticleIdList><ArticleId IdType="pubmed">18249174</ArticleId></ArticleIdList></Reference><Reference><Citation>Nat Genet. 2008 Aug;40(8):955-62</Citation><ArticleIdList><ArticleId IdType="pubmed">18587394</ArticleId></ArticleIdList></Reference><Reference><Citation>Rapid Commun Mass Spectrom. 2008 Dec;22(23):3743-53</Citation><ArticleIdList><ArticleId IdType="pubmed">18980262</ArticleId></ArticleIdList></Reference><Reference><Citation>J Biol Chem. 2009 Mar 20;284(12):7588-96</Citation><ArticleIdList><ArticleId IdType="pubmed">19139096</ArticleId></ArticleIdList></Reference><Reference><Citation>J Lipid Res. 2009 Jun;50(6):1237-44</Citation><ArticleIdList><ArticleId IdType="pubmed">19181628</ArticleId></ArticleIdList></Reference><Reference><Citation>Genes Dev. 2009 Aug 15;23(16):1929-43</Citation><ArticleIdList><ArticleId IdType="pubmed">19684113</ArticleId></ArticleIdList></Reference><Reference><Citation>Mol Cell. 2009 Sep 11;35(5):563-73</Citation><ArticleIdList><ArticleId IdType="pubmed">19748353</ArticleId></ArticleIdList></Reference><Reference><Citation>Nature. 2010 Feb 25;463(7284):1048-53</Citation><ArticleIdList><ArticleId IdType="pubmed">20182505</ArticleId></ArticleIdList></Reference><Reference><Citation>Curr Genet. 2010 Apr;56(2):121-37</Citation><ArticleIdList><ArticleId IdType="pubmed">20043226</ArticleId></ArticleIdList></Reference><Reference><Citation>Nat Genet. 2010 Apr;42(4):332-7</Citation><ArticleIdList><ArticleId IdType="pubmed">20228799</ArticleId></ArticleIdList></Reference><Reference><Citation>Proc Natl Acad Sci U S A. 2010 Mar 30;107(13):5851-6</Citation><ArticleIdList><ArticleId IdType="pubmed">20212121</ArticleId></ArticleIdList></Reference><Reference><Citation>Nat Genet. 2009 Jun;41(6):703-7</Citation><ArticleIdList><ArticleId IdType="pubmed">19430480</ArticleId></ArticleIdList></Reference><Reference><Citation>Mol Biol Cell. 2010 Oct 1;21(19):3475-86</Citation><ArticleIdList><ArticleId IdType="pubmed">20702584</ArticleId></ArticleIdList></Reference><Reference><Citation>Mol Biol Cell. 2010 Oct 15;21(20):3552-66</Citation><ArticleIdList><ArticleId IdType="pubmed">20739461</ArticleId></ArticleIdList></Reference><Reference><Citation>Nat Rev Drug Discov. 2011 Nov;10(11):868-80</Citation><ArticleIdList><ArticleId IdType="pubmed">22037041</ArticleId></ArticleIdList></Reference><Reference><Citation>Cell. 2011 Nov 23;147(5):1104-17</Citation><ArticleIdList><ArticleId IdType="pubmed">22118465</ArticleId></ArticleIdList></Reference><Reference><Citation>Proc Natl Acad Sci U S A. 2011 Nov 29;108(48):19222-7</Citation><ArticleIdList><ArticleId IdType="pubmed">22080611</ArticleId></ArticleIdList></Reference><Reference><Citation>Genetics. 2011 Dec;189(4):1177-201</Citation><ArticleIdList><ArticleId IdType="pubmed">22174183</ArticleId></ArticleIdList></Reference><Reference><Citation>Nat Cell Biol. 2012 May;14(5):542-7</Citation><ArticleIdList><ArticleId IdType="pubmed">22504275</ArticleId></ArticleIdList></Reference><Reference><Citation>Mol Biol Cell. 2012 Jun;23(12):2388-98</Citation><ArticleIdList><ArticleId IdType="pubmed">22535525</ArticleId></ArticleIdList></Reference><Reference><Citation>J Biol Chem. 1997 Dec 19;272(51):32566-72</Citation><ArticleIdList><ArticleId IdType="pubmed">9405471</ArticleId></ArticleIdList></Reference></ReferenceList></PubmedData></pubmed><affiliations><list><country><li>Suisse</li></country></list><tree><noCountry><name sortKey="Hall, Michael N" sort="Hall, Michael N" uniqKey="Hall M" first="Michael N" last="Hall">Michael N. Hall</name><name sortKey="Jeno, Paul" sort="Jeno, Paul" uniqKey="Jeno P" first="Paul" last="Jenö">Paul Jenö</name><name sortKey="Moes, Suzette" sort="Moes, Suzette" uniqKey="Moes S" first="Suzette" last="Moes">Suzette Moes</name><name sortKey="Oppliger, Wolfgang" sort="Oppliger, Wolfgang" uniqKey="Oppliger W" first="Wolfgang" last="Oppliger">Wolfgang Oppliger</name></noCountry><country name="Suisse"><noRegion><name sortKey="Shimobayashi, Mitsugu" sort="Shimobayashi, Mitsugu" uniqKey="Shimobayashi M" first="Mitsugu" last="Shimobayashi">Mitsugu Shimobayashi</name></noRegion></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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|texte= TORC1-regulated protein kinase Npr1 phosphorylates Orm to stimulate complex sphingolipid synthesis.
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