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nature portfolio research grants obtained permissions reprints privacy policy advertising nature 451 nature 426 nature ceramide-synthase-6–generated c16-ceramide social media c18-ceramide–induced lethal autophagy regulates n-stearoyl-sphinganine er-stress-response pathways drp1-dependent mitochondrial fission atg4b–lc3 complex reveals article initially published fumonisin b1-independent manner mammalian development normal development gfp-lc3 transgenic hepatocytes endogenous c18-ceramide generation springerlink instant access author correspondence ceramide-activated protein kinase anchoring lc3b-ii autophagolysosomes permissions c18-ceramide–dependent mitophagy c18-pyridinium ceramide treatment radiation-induced apoptosis sphingolipid-protein binding molecular biology anti-tumoral action ceramide targets autophagosomes er stress privacy molecular life sciences ceramide synthase activity ampk-dependent activation besim ogretmen impaired ceramide binding human cancer cells cell death differ personal data bcl-2 family proteins competing financial interests induces lethal mitophagy hyl-2 ceramide synthase stimulates mitochondrial turnover structural basis cationic pyridinium-ceramide

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         headline:Ceramide targets autophagosomes to mitochondria and induces lethal mitophagy
         description:C18-ceramide mediates lethal autophagy by anchoring LC3B-II (lipidated LC3) to mitochondrial membranes during mitochondrial fission and thereby recruiting autophagosomes. Mechanisms by which autophagy promotes cell survival or death are unclear. We provide evidence that C18-pyridinium ceramide treatment or endogenous C18-ceramide generation by ceramide synthase 1 (CerS1) expression mediates autophagic cell death, independent of apoptosis in human cancer cells. C18-ceramide–induced lethal autophagy was regulated via microtubule-associated protein 1 light chain 3 β-lipidation, forming LC3B-II, and selective targeting of mitochondria by LC3B-II–containing autophagolysosomes (mitophagy) through direct interaction between ceramide and LC3B-II upon Drp1-dependent mitochondrial fission, leading to inhibition of mitochondrial function and oxygen consumption. Accordingly, expression of mutant LC3B with impaired ceramide binding, as predicted by molecular modeling, prevented CerS1-mediated mitochondrial targeting, recovering oxygen consumption. Moreover, knockdown of CerS1 abrogated sodium selenite–induced mitophagy, and stable LC3B knockdown protected against CerS1- and C18-ceramide–dependent mitophagy and blocked tumor suppression in vivo. Thus, these data suggest a new receptor function of ceramide for anchoring LC3B-II autophagolysosomes to mitochondrial membranes, defining a key mechanism for the induction of lethal mitophagy.
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      description:C18-ceramide mediates lethal autophagy by anchoring LC3B-II (lipidated LC3) to mitochondrial membranes during mitochondrial fission and thereby recruiting autophagosomes. Mechanisms by which autophagy promotes cell survival or death are unclear. We provide evidence that C18-pyridinium ceramide treatment or endogenous C18-ceramide generation by ceramide synthase 1 (CerS1) expression mediates autophagic cell death, independent of apoptosis in human cancer cells. C18-ceramide–induced lethal autophagy was regulated via microtubule-associated protein 1 light chain 3 β-lipidation, forming LC3B-II, and selective targeting of mitochondria by LC3B-II–containing autophagolysosomes (mitophagy) through direct interaction between ceramide and LC3B-II upon Drp1-dependent mitochondrial fission, leading to inhibition of mitochondrial function and oxygen consumption. Accordingly, expression of mutant LC3B with impaired ceramide binding, as predicted by molecular modeling, prevented CerS1-mediated mitochondrial targeting, recovering oxygen consumption. Moreover, knockdown of CerS1 abrogated sodium selenite–induced mitophagy, and stable LC3B knockdown protected against CerS1- and C18-ceramide–dependent mitophagy and blocked tumor suppression in vivo. Thus, these data suggest a new receptor function of ceramide for anchoring LC3B-II autophagolysosomes to mitochondrial membranes, defining a key mechanism for the induction of lethal mitophagy.
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      name:Hollings Cancer Center, Medical University of South Carolina, Charleston, USA
      name:Department of Biochemistry and Molecular Biology, Medical University of South Carolina, Charleston, USA
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      name:Department of Biochemistry and Molecular Biology, Medical University of South Carolina, Charleston, USA
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