RapamycinFungusV1, Main, Exploration, bibRecord, 001595

Regulation of ceramide biosynthesis by TOR complex 2.

Identifieur interne : 001595 ( Main/Exploration ); précédent : 001594; suivant : 001596

Regulation of ceramide biosynthesis by TOR complex 2.

Auteurs : Sofia Aronova [États-Unis] ; Karen Wedaman ; Pavel A. Aronov ; Kristin Fontes ; Karmela Ramos ; Bruce D. Hammock ; Ted Powers

Source :

Cell metabolism [ 1550-4131 ] ; 2008.

RBID : pubmed:18249174

Descripteurs français

KwdFr :
- Céramides (biosynthèse), Levures (MeSH), Oxidoreductases (métabolisme), Phosphatidylinositol 3-kinases (physiologie), Protein kinases (métabolisme), Protéines de Saccharomyces cerevisiae (métabolisme), Protéines de Saccharomyces cerevisiae (physiologie), Protéines du cycle cellulaire (physiologie), Protéines fongiques (métabolisme), Transduction du signal (MeSH).
MESH :
- biosynthèse : Céramides.
- métabolisme : Oxidoreductases, Protein kinases, Protéines de Saccharomyces cerevisiae, Protéines fongiques.
- physiologie : Phosphatidylinositol 3-kinases, Protéines de Saccharomyces cerevisiae, Protéines du cycle cellulaire.
- Levures, Transduction du signal.

English descriptors

KwdEn :
- Cell Cycle Proteins (physiology), Ceramides (biosynthesis), Fungal Proteins (metabolism), Oxidoreductases (metabolism), Phosphatidylinositol 3-Kinases (physiology), Protein Kinases (metabolism), Saccharomyces cerevisiae Proteins (metabolism), Saccharomyces cerevisiae Proteins (physiology), Signal Transduction (MeSH), Yeasts (MeSH).
MESH :
- chemical , biosynthesis : Ceramides.
- chemical , metabolism : Fungal Proteins, Oxidoreductases, Protein Kinases, Saccharomyces cerevisiae Proteins.
- chemical , physiology : Cell Cycle Proteins, Phosphatidylinositol 3-Kinases, Saccharomyces cerevisiae Proteins.
- Signal Transduction, Yeasts.

Abstract

Ceramides and sphingoid long-chain bases (LCBs) are precursors to more complex sphingolipids and play distinct signaling roles crucial for cell growth and survival. Conserved reactions within the sphingolipid biosynthetic pathway are responsible for the formation of these intermediates. Components of target of rapamycin complex 2 (TORC2) have been implicated in the biosynthesis of sphingolipids in S. cerevisiae; however, the precise step regulated by this complex remains unknown. Here we demonstrate that yeast cells deficient in TORC2 activity are impaired for de novo ceramide biosynthesis both in vivo and in vitro. We find that TORC2 regulates this step in part by activating the AGC kinase Ypk2 and that this step is antagonized by the Ca2+/calmodulin-dependent phosphatase calcineurin. Because Ypk2 is activated independently by LCBs, the direct precursors to ceramides, our data suggest a model wherein TORC2 signaling is coupled with LCB levels to control Ypk2 activity and, ultimately, regulate ceramide formation.

DOI: 10.1016/j.cmet.2007.11.015
PubMed: 18249174
PubMed Central: PMC3882310

Affiliations:

Links toward previous steps (curation, corpus...)

to stream Main, to step Corpus: 001640
to stream Main, to step Curation: 001640

Le document en format XML

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<term>Phosphatidylinositol 3-Kinases (physiology)</term>
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<term>Saccharomyces cerevisiae Proteins (metabolism)</term>
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<term>Protéines fongiques (métabolisme)</term>
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<front><div type="abstract" xml:lang="en">Ceramides and sphingoid long-chain bases (LCBs) are precursors to more complex sphingolipids and play distinct signaling roles crucial for cell growth and survival. Conserved reactions within the sphingolipid biosynthetic pathway are responsible for the formation of these intermediates. Components of target of rapamycin complex 2 (TORC2) have been implicated in the biosynthesis of sphingolipids in S. cerevisiae; however, the precise step regulated by this complex remains unknown. Here we demonstrate that yeast cells deficient in TORC2 activity are impaired for de novo ceramide biosynthesis both in vivo and in vitro. We find that TORC2 regulates this step in part by activating the AGC kinase Ypk2 and that this step is antagonized by the Ca2+/calmodulin-dependent phosphatase calcineurin. Because Ypk2 is activated independently by LCBs, the direct precursors to ceramides, our data suggest a model wherein TORC2 signaling is coupled with LCB levels to control Ypk2 activity and, ultimately, regulate ceramide formation.</div>
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<ReferenceList><Reference><Citation>Eukaryot Cell. 2003 Apr;2(2):284-94</Citation>
<ArticleIdList><ArticleId IdType="pubmed">12684378</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Curr Genet. 2001 Dec;40(4):221-33</Citation>
<ArticleIdList><ArticleId IdType="pubmed">11795842</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Biochim Biophys Acta. 2007 Mar;1771(3):421-31</Citation>
<ArticleIdList><ArticleId IdType="pubmed">16997623</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Sci Aging Knowledge Environ. 2003 Oct 1;2003(39):PE27</Citation>
<ArticleIdList><ArticleId IdType="pubmed">14523222</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Biochem J. 2006 Feb 1;393(Pt 3):733-40</Citation>
<ArticleIdList><ArticleId IdType="pubmed">16201964</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Biochim Biophys Acta. 2006 Dec;1758(12):1893-901</Citation>
<ArticleIdList><ArticleId IdType="pubmed">16938269</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>Mol Cell Biol. 2005 Aug;25(16):7239-48</Citation>
<ArticleIdList><ArticleId IdType="pubmed">16055732</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Biochim Biophys Acta. 2006 Dec;1758(12):1995-2015</Citation>
<ArticleIdList><ArticleId IdType="pubmed">17084809</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Anal Biochem. 2001 Nov 15;298(2):283-92</Citation>
<ArticleIdList><ArticleId IdType="pubmed">11700984</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Biol Chem. 1995 Oct 27;270(43):25905-14</Citation>
<ArticleIdList><ArticleId IdType="pubmed">7592778</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Mol Cell Biol. 2007 Jan;27(2):633-50</Citation>
<ArticleIdList><ArticleId IdType="pubmed">17101780</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Biol Chem. 2004 Nov 5;279(45):46527-35</Citation>
<ArticleIdList><ArticleId IdType="pubmed">15326168</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Genetics. 1989 May;122(1):19-27</Citation>
<ArticleIdList><ArticleId IdType="pubmed">2659436</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Ann N Y Acad Sci. 2000 Apr;905:54-60</Citation>
<ArticleIdList><ArticleId IdType="pubmed">10818441</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 Cell Biol. 2006 Aug;26(15):5861-75</Citation>
<ArticleIdList><ArticleId IdType="pubmed">16847337</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Biochem Cell Biol. 2004 Feb;82(1):45-61</Citation>
<ArticleIdList><ArticleId IdType="pubmed">15052327</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Biochim Biophys Acta. 2002 Dec 30;1585(2-3):163-71</Citation>
<ArticleIdList><ArticleId IdType="pubmed">12531550</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Biol Chem. 2005 Jun 17;280(24):22679-87</Citation>
<ArticleIdList><ArticleId IdType="pubmed">15840588</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Cell Signal. 2006 Mar;18(3):267-75</Citation>
<ArticleIdList><ArticleId IdType="pubmed">16126370</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Mol Cell Biol. 2001 Jan;21(1):109-25</Citation>
<ArticleIdList><ArticleId IdType="pubmed">11113186</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Rapid Commun Mass Spectrom. 2005;19(10):1257-62</Citation>
<ArticleIdList><ArticleId IdType="pubmed">15838927</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Biol Chem. 1997 Nov 21;272(47):29704-10</Citation>
<ArticleIdList><ArticleId IdType="pubmed">9368039</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Biol Chem. 2006 Nov 3;281(44):33000-7</Citation>
<ArticleIdList><ArticleId IdType="pubmed">16959779</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Genetics. 1998 Jan;148(1):99-112</Citation>
<ArticleIdList><ArticleId IdType="pubmed">9475724</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Genetics. 1996 Jun;143(2):723-39</Citation>
<ArticleIdList><ArticleId IdType="pubmed">8725222</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Biol Chem. 1997 Nov 28;272(48):30196-200</Citation>
<ArticleIdList><ArticleId IdType="pubmed">9374502</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Mol Cell Biol. 2006 Jun;26(12):4729-45</Citation>
<ArticleIdList><ArticleId IdType="pubmed">16738335</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>J Biol Chem. 2002 Jul 19;277(29):25847-50</Citation>
<ArticleIdList><ArticleId IdType="pubmed">12011103</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Yeast. 1992 Feb;8(2):79-82</Citation>
<ArticleIdList><ArticleId IdType="pubmed">1561838</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Crit Rev Oncol Hematol. 2007 Aug;63(2):150-9</Citation>
<ArticleIdList><ArticleId IdType="pubmed">17560117</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Prog Lipid Res. 2006 Nov;45(6):447-65</Citation>
<ArticleIdList><ArticleId IdType="pubmed">16730802</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>EMBO J. 2004 Oct 1;23(19):3747-57</Citation>
<ArticleIdList><ArticleId IdType="pubmed">15372071</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Mol Cell Biol. 2000 Jun;20(12):4411-9</Citation>
<ArticleIdList><ArticleId IdType="pubmed">10825204</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Biol Chem. 1997 Dec 19;272(51):32566-72</Citation>
<ArticleIdList><ArticleId IdType="pubmed">9405471</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Cell. 2006 Feb 10;124(3):471-84</Citation>
<ArticleIdList><ArticleId IdType="pubmed">16469695</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Genetics. 2000 Dec;156(4):1519-29</Citation>
<ArticleIdList><ArticleId IdType="pubmed">11102354</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Methods Enzymol. 1993;217:270-9</Citation>
<ArticleIdList><ArticleId IdType="pubmed">8474334</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Mol Cell. 2002 Sep;10(3):457-68</Citation>
<ArticleIdList><ArticleId IdType="pubmed">12408816</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Biochem J. 2006 Feb 15;394(Pt 1):237-42</Citation>
<ArticleIdList><ArticleId IdType="pubmed">16225461</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>FEBS Lett. 2000 Jun 30;476(1-2):55-7</Citation>
<ArticleIdList><ArticleId IdType="pubmed">10878250</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Yeast. 1998 Mar 15;14(4):311-21</Citation>
<ArticleIdList><ArticleId IdType="pubmed">9559540</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Biochim Biophys Acta. 1999 Jun 10;1438(3):305-21</Citation>
<ArticleIdList><ArticleId IdType="pubmed">10366774</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Curr Genet. 2005 May;47(5):273-88</Citation>
<ArticleIdList><ArticleId IdType="pubmed">15809876</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>Yeast. 2002 May;19(7):573-86</Citation>
<ArticleIdList><ArticleId IdType="pubmed">11967828</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Biol Chem. 2004 Apr 9;279(15):14752-62</Citation>
<ArticleIdList><ArticleId IdType="pubmed">14736892</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. 2003 Sep 26;278(39):37083-91</Citation>
<ArticleIdList><ArticleId IdType="pubmed">12869556</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Biol Chem. 1998 Jul 31;273(31):19437-42</Citation>
<ArticleIdList><ArticleId IdType="pubmed">9677363</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Science. 1996 Dec 13;274(5294):1855-9</Citation>
<ArticleIdList><ArticleId IdType="pubmed">8943189</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 Biochem Mol Biol. 2006 Mar 31;39(2):113-31</Citation>
<ArticleIdList><ArticleId IdType="pubmed">16584625</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Biol Chem. 2004 Apr 30;279(18):18688-93</Citation>
<ArticleIdList><ArticleId IdType="pubmed">14976195</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Biol Chem. 1995 Dec 22;270(51):30701-8</Citation>
<ArticleIdList><ArticleId IdType="pubmed">8530509</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Methods Cell Biol. 1989;31:357-435</Citation>
<ArticleIdList><ArticleId IdType="pubmed">2476649</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>EMBO J. 2001 Dec 3;20(23):6783-92</Citation>
<ArticleIdList><ArticleId IdType="pubmed">11726514</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Biol Chem. 1998 Mar 6;273(10):5869-77</Citation>
<ArticleIdList><ArticleId IdType="pubmed">9488724</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Biochem Soc Trans. 2005 Nov;33(Pt 5):1170-3</Citation>
<ArticleIdList><ArticleId IdType="pubmed">16246074</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Biochim Biophys Acta. 2002 Jun 13;1583(1):13-25</Citation>
<ArticleIdList><ArticleId IdType="pubmed">12069845</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Mol Pharmacol. 2001 May;59(5):1249-55</Citation>
<ArticleIdList><ArticleId IdType="pubmed">11306710</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Cell Metab. 2007 Jul;6(1):1-2</Citation>
<ArticleIdList><ArticleId IdType="pubmed">17618850</ArticleId>
</ArticleIdList>
</Reference>
</ReferenceList>
</PubmedData>
</pubmed>
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	Serveur d'exploration sur la rapamycine et les champignons
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Regulation of ceramide biosynthesis by TOR complex 2.

Regulation of ceramide biosynthesis by TOR complex 2.

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