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Regulation of Autophagy by Sphingosine Kinase 1 and Its Role in Cell Survival during Nutrient Starvation

Lavieu, Grégory, Scarlatti, Francesca, Sala, Giusy, Carpentier, Stéphane, Levade, Thierry, Ghidoni, Riccardo, Botti, Joëlle, Codogno, Patrice·2006·Journal of Biological Chemistry
DOI 10.1074/jbc.m506182200
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FIGURE 1 Sphingosine kinase activity and sphingolipid levels in MCF-7 cells. A , MCF-7 cells were transfected with an empty vector (control), cDNAs encoding the wild-type SK1 (SK1 WT ) or a catalytically inactive SK1 mutant (SK1 G82D ). Left , SK activity was analyzed as described under 'Experimental Procedures.' When required 1.5 𝛍 M DMS was added at the beginning of the experiment. Middle , S1P was determined after [ 3 H]sphingosine incorporation in control cells or SK1 wt -overexpressing cells in the presence or absence of DMS. [ 3 H]Sphingosine recovery in control cells was set to 100%. Right , endogenous long-chain ceramides were quantified by the DGK assay in control cells, SK1 WT -overexpressing cells, SK G82D -expressing cells, and cells treated by C 2 -Cer (75 𝛍 M, 2 h). B , quantification of ceramide. Endogenous long-chain ceramides were quantified by the DGK assay in SK1 WT overexpressing cells cultured in complete medium at different time points. When required 3MA (10 mM) and DMS (1.5 𝛍 M) were added, and the ceramide level was analyzed after 24 h of treatment. The amount of ceramide (5.2 pmol of Cer/nmol of P i ) in MCF-7 cells cultured in complete medium was set to 100%. Values are the mean ± S.D. of three independent experiments. *, p < 0.05 versus control cells.
FIGURE 1 Sphingosine kinase activity and sphingolipid levels in MCF-7 cells. A , MCF-7 cells were transfected with an empty vector (control), cDNAs encoding the wild-type SK1 (SK1 WT ) or a catalytically inactive SK1 mutant (SK1 G82D ). Left , SK activity was analyzed as described under 'Experimental Procedures.' When required 1.5 𝛍 M DMS was added at the beginning of the experiment. Middle , S1P was determined after [ 3 H]sphingosine incorporation in control cells or SK1 wt -overexpressing cells in the presence or absence of DMS. [ 3 H]Sphingosine recovery in control cells was set to 100%. Right , endogenous long-chain ceramides were quantified by the DGK assay in control cells, SK1 WT -overexpressing cells, SK G82D -expressing cells, and cells treated by C 2 -Cer (75 𝛍 M, 2 h). B , quantification of ceramide. Endogenous long-chain ceramides were quantified by the DGK assay in SK1 WT overexpressing cells cultured in complete medium at different time points. When required 3MA (10 mM) and DMS (1.5 𝛍 M) were added, and the ceramide level was analyzed after 24 h of treatment. The amount of ceramide (5.2 pmol of Cer/nmol of P i ) in MCF-7 cells cultured in complete medium was set to 100%. Values are the mean ± S.D. of three independent experiments. *, p < 0.05 versus control cells.CC-BY · From the PDF
FIGURE 2 Sphingosine kinase 1 stimulates autophagy in MCF-7 cells. A , GFP-LC3 staining and quantitative analysis in MCF-7 transfected with an empty vector (control), in SK1 WT -overexpressing cells, in SK1 G82D -expressing cells, and in cells treated with C2-Cer (75 𝛍 M, 2 h). When required, 1.5 𝛍 M DMS was added. The bar represents 10 𝛍 m. B , degradation of [ 14 C]valine-labeled long-lived proteins was determined in control cells, in SK1 WT -overexpressing cells, and in cells treated with C 2 -Cer (75 𝛍 M) as described under 'Experimental Procedures.' When required 3MA (10 mM) and DMS (1.5 𝛍 M) were added during the chase period. Values reported are the mean ± S.D. of four independent experiments. *, p < 0.05 versus control cells.
FIGURE 2 Sphingosine kinase 1 stimulates autophagy in MCF-7 cells. A , GFP-LC3 staining and quantitative analysis in MCF-7 transfected with an empty vector (control), in SK1 WT -overexpressing cells, in SK1 G82D -expressing cells, and in cells treated with C2-Cer (75 𝛍 M, 2 h). When required, 1.5 𝛍 M DMS was added. The bar represents 10 𝛍 m. B , degradation of [ 14 C]valine-labeled long-lived proteins was determined in control cells, in SK1 WT -overexpressing cells, and in cells treated with C 2 -Cer (75 𝛍 M) as described under 'Experimental Procedures.' When required 3MA (10 mM) and DMS (1.5 𝛍 M) were added during the chase period. Values reported are the mean ± S.D. of four independent experiments. *, p < 0.05 versus control cells.CC-BY · From the PDF
FIGURE 3 Effect of fumonisin B1 (FB1) on autophagy. GFP-LC3stainingandquantitativeanalysis in SK1 WT -overexpressing cells and in cells treated with C2 -Cer (75 𝛍 M 2 h). When required, 100 𝛍 M FB1 was added. The bar represents 10 𝛍 m. Values are representative of three independent experiments. *, p < 0.05 versus C2-Cer-treated cells.
FIGURE 3 Effect of fumonisin B1 (FB1) on autophagy. GFP-LC3stainingandquantitativeanalysis in SK1 WT -overexpressing cells and in cells treated with C2 -Cer (75 𝛍 M 2 h). When required, 100 𝛍 M FB1 was added. The bar represents 10 𝛍 m. Values are representative of three independent experiments. *, p < 0.05 versus C2-Cer-treated cells.CC-BY · From the PDF
FIGURE 4 Effect of SK1 on mTOR signaling pathway and Akt/PKB activation. A , analysis of mTOR signaling. Cell lysates of control MCF-7 cells (empty vector) treated or not by 1.5 𝛍 MDMS,C2-Cer(75 𝛍 M, 2 h)-treated cells, SK1 wt -overexpressingcellstreatedornotby 1.5 𝛍 MDMS,andSK1 G82D -expressingcells were analyzed by Western blotting for p70S6K phosphorylation at Thr 389 using a phosphospecific antibody. The expression of total p70S6K was detected by using an anti-pan p70S6K antibody. Densitometry was performed on the original fluorographs, and the ratio of phospho-Thr 389 /total p70S6K in controlcellswassetto1.Thephosphorylationof4E-BP1wasevaluatedbyphosphorylationdependent band shift using anti-4E-BP1. SK1 was detected in cell lysates of SK1 wt -overexpressing cells and SK1 G82D -expressing cells by anti-FLAG. Actin was used as loading control. When required, 1.5 𝛍 M DMS was added. B , Akt/PKB activation. Cell lysates obtained as described above were analyzed by Western blotting for Akt/PKB phosphorylation at Ser 473 using a phosphospecific antibody. The expression of total Akt/PKB was detected by using an anti-pan Akt/PKB antibody. Densitometry was performed on the original fluorographs, and the ratio of phospho-Ser 473 /total Akt/PKB in control cells was set to 1. Values are the mean ± S.D. of three independent experiments. *, p < 0.05 versus control cells.
FIGURE 4 Effect of SK1 on mTOR signaling pathway and Akt/PKB activation. A , analysis of mTOR signaling. Cell lysates of control MCF-7 cells (empty vector) treated or not by 1.5 𝛍 MDMS,C2-Cer(75 𝛍 M, 2 h)-treated cells, SK1 wt -overexpressingcellstreatedornotby 1.5 𝛍 MDMS,andSK1 G82D -expressingcells were analyzed by Western blotting for p70S6K phosphorylation at Thr 389 using a phosphospecific antibody. The expression of total p70S6K was detected by using an anti-pan p70S6K antibody. Densitometry was performed on the original fluorographs, and the ratio of phospho-Thr 389 /total p70S6K in controlcellswassetto1.Thephosphorylationof4E-BP1wasevaluatedbyphosphorylationdependent band shift using anti-4E-BP1. SK1 was detected in cell lysates of SK1 wt -overexpressing cells and SK1 G82D -expressing cells by anti-FLAG. Actin was used as loading control. When required, 1.5 𝛍 M DMS was added. B , Akt/PKB activation. Cell lysates obtained as described above were analyzed by Western blotting for Akt/PKB phosphorylation at Ser 473 using a phosphospecific antibody. The expression of total Akt/PKB was detected by using an anti-pan Akt/PKB antibody. Densitometry was performed on the original fluorographs, and the ratio of phospho-Ser 473 /total Akt/PKB in control cells was set to 1. Values are the mean ± S.D. of three independent experiments. *, p < 0.05 versus control cells.CC-BY · From the PDF
Image 5
CC-BY · From the PDF
FIGURE 6 Effect of SK1 on Beclin 1 accumulation. Cell lysates of control MCF-7 cells (empty vector), C2-Cer (75 𝛍 M, 2 h)-treated cells, SK1 wt -overexpressing cells, and SK1 G82D -expressing cells were analyzed by Western blotting for Beclin 1 and actin expression. Densitometry was performed on the original fluorographs, and the Beclin 1/actin ratio in control cells was set to 1. The Western blot is representative of three independent experiments. *, p < 0.05 versus control cells.
FIGURE 6 Effect of SK1 on Beclin 1 accumulation. Cell lysates of control MCF-7 cells (empty vector), C2-Cer (75 𝛍 M, 2 h)-treated cells, SK1 wt -overexpressing cells, and SK1 G82D -expressing cells were analyzed by Western blotting for Beclin 1 and actin expression. Densitometry was performed on the original fluorographs, and the Beclin 1/actin ratio in control cells was set to 1. The Western blot is representative of three independent experiments. *, p < 0.05 versus control cells.CC-BY · From the PDF
FIGURE 7 Effect of starvation on SK activity and ceramide level in MCF7. beclin 1 cells. A , expression of Beclin1 was analyzed in control MCF-7 and MCF-7/tet-off clone (MCF-7. beclin 1 ) before and after tetracycline removal. Actin was used as a loading control. B , SK activity was analyzed as determined under 'Experimental Procedures' in MCF7. beclin 1 cells cultured in tetracycline-free complete medium (CM) and in nutrient-free medium (NF) in the presence or absence of 1.5 𝛍 M DMS for 4 h. C , quantification of ceramide. Endogenous long-chain ceramides were quantified by the DGK assay in starved MCF-7. beclin 1 cells at different time points. When required 3MA (10 mM) and DMS(1.5 𝛍 M) were added, and the ceramide level was analyzed after 24 h of treatment. Ceramide was quantified in cells transfected with SK1-siRNA 24 h post-transfection. The amount of ceramide (5.2 pmol of Cer/nmol of P i ) in control MCF-7. beclin 1 cells cultured in complete medium was set to 100%. Values are the mean ± S.D. of two independent experiments. Values are representative of three independent experiments. *, p < 0.05 versus control cells.
FIGURE 7 Effect of starvation on SK activity and ceramide level in MCF7. beclin 1 cells. A , expression of Beclin1 was analyzed in control MCF-7 and MCF-7/tet-off clone (MCF-7. beclin 1 ) before and after tetracycline removal. Actin was used as a loading control. B , SK activity was analyzed as determined under 'Experimental Procedures' in MCF7. beclin 1 cells cultured in tetracycline-free complete medium (CM) and in nutrient-free medium (NF) in the presence or absence of 1.5 𝛍 M DMS for 4 h. C , quantification of ceramide. Endogenous long-chain ceramides were quantified by the DGK assay in starved MCF-7. beclin 1 cells at different time points. When required 3MA (10 mM) and DMS(1.5 𝛍 M) were added, and the ceramide level was analyzed after 24 h of treatment. Ceramide was quantified in cells transfected with SK1-siRNA 24 h post-transfection. The amount of ceramide (5.2 pmol of Cer/nmol of P i ) in control MCF-7. beclin 1 cells cultured in complete medium was set to 100%. Values are the mean ± S.D. of two independent experiments. Values are representative of three independent experiments. *, p < 0.05 versus control cells.CC-BY · From the PDF
FIGURE 8 SK1-induced autophagy protects cells from apoptosis during starvation. In A : Upper panel , GFP-LC3 staining and quantitative analysis in MCF-7. beclin 1 cells transfected with control siRNA, Atg7-siRNA, or SK1-siRNA and incubated in complete medium or in nutrient-free (NF) mediumfor48h.Whenrequired1.5 𝛍 MDMSor10 mM 3MA were added to control cells (control siRNA). The bar represents 10 𝛍 m. Lower panel , Atg7 and actin were detected by Western blot in cells transfected with control siRNA or Atg7-siRNA ( left ). SK1 RT-PCR in cells transfected with control siRNA, SK1-siRNA ( right panel ). Glyceraldehyde-3phosphate dehydrogenase ( GAPDH ) was used as a control. B : Left , MCF-7. beclin 1 cells transfected withcontrol siRNA, Atg7-siRNA, or SK1-siRNA were incubated in nutrient-free medium for 48 h. Cell viability was determined by the trypan blue exclusion test. Cell viability in complete medium was set to 100%. When required, DMS (1.5 𝛍 M) or 3MA (10 mM) were added to control cells (control siRNA). z-VAD-fmk (40 𝛍 M) was added 1 h before starvation and was present throughout the incubation period in nutrient-free ( NF ) medium. Right , analysis of PARP cleavage in MCF-7. beclin 1 cells transfected with control siRNA, Atg7-siRNA, SK1-siRNA, and in MCF-7. beclin 1 cells treated by 1.5 𝛍 M DMS or 10 mM 3MA. z-VAD-fmk (40 𝛍 M) was added 1 h before starvation and was present throughout the incubation period in nutrient-free ( NF ) medium. Values are representative of three independent experiments. *, p < 0.05 versus control cells in nutrient-free medium.
FIGURE 8 SK1-induced autophagy protects cells from apoptosis during starvation. In A : Upper panel , GFP-LC3 staining and quantitative analysis in MCF-7. beclin 1 cells transfected with control siRNA, Atg7-siRNA, or SK1-siRNA and incubated in complete medium or in nutrient-free (NF) mediumfor48h.Whenrequired1.5 𝛍 MDMSor10 mM 3MA were added to control cells (control siRNA). The bar represents 10 𝛍 m. Lower panel , Atg7 and actin were detected by Western blot in cells transfected with control siRNA or Atg7-siRNA ( left ). SK1 RT-PCR in cells transfected with control siRNA, SK1-siRNA ( right panel ). Glyceraldehyde-3phosphate dehydrogenase ( GAPDH ) was used as a control. B : Left , MCF-7. beclin 1 cells transfected withcontrol siRNA, Atg7-siRNA, or SK1-siRNA were incubated in nutrient-free medium for 48 h. Cell viability was determined by the trypan blue exclusion test. Cell viability in complete medium was set to 100%. When required, DMS (1.5 𝛍 M) or 3MA (10 mM) were added to control cells (control siRNA). z-VAD-fmk (40 𝛍 M) was added 1 h before starvation and was present throughout the incubation period in nutrient-free ( NF ) medium. Right , analysis of PARP cleavage in MCF-7. beclin 1 cells transfected with control siRNA, Atg7-siRNA, SK1-siRNA, and in MCF-7. beclin 1 cells treated by 1.5 𝛍 M DMS or 10 mM 3MA. z-VAD-fmk (40 𝛍 M) was added 1 h before starvation and was present throughout the incubation period in nutrient-free ( NF ) medium. Values are representative of three independent experiments. *, p < 0.05 versus control cells in nutrient-free medium.CC-BY · From the PDF
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Research works printed but not linked: 71

  1. Seglen, 1992, Experientia, 48, 158, 10.1007/BF01923509 · DOI
  2. Dunn, 1994, Trends Cell Biol., 4, 139, 10.1016/0962-8924(94)90069-8 · DOI
  3. Klionsky, 2000, Science, 290, 1717, 10.1126/science.290.5497.1717 · DOI
  4. Klionsky, 1999, Annu. Rev. Cell Dev. Biol., 15, 1, 10.1146/annurev.cellbio.15.1.1 · DOI
  5. Klionsky, 2003, Dev. Cell, 5, 539, 10.1016/S1534-5807(03)00296-X · DOI
  6. Scott, 2004, Dev. Cell, 7, 167, 10.1016/j.devcel.2004.07.009 · DOI
  7. Lum, 2005, Cell, 120, 237, 10.1016/j.cell.2004.11.046 · DOI · Paper page
  8. Boya, 2005, Mol. Cell. Biol., 25, 1025, 10.1128/MCB.25.3.1025-1040.2005 · DOI
  9. Schweichel, 1973, Teratology, 7, 253, 10.1002/tera.1420070306 · DOI · Paper page
  10. Clarke, 1990, Anat. Embryol., 181, 195, 10.1007/BF00174615 · DOI · Paper page
  11. Bursch, 2001, Cell Death Differ., 8, 569, 10.1038/sj.cdd.4400852 · DOI
  12. Lockshin, 2004, Int. J. Biochem. Cell Biol., 36, 2405, 10.1016/j.biocel.2004.04.011 · DOI
  13. Shimizu, 2004, Nat. Cell Biol., 6, 1221, 10.1038/ncb1192 · DOI · Paper page
  14. Yu, 2004, Science, 304, 1500, 10.1126/science.1096645 · DOI
  15. Edinger, 2004, Curr. Opin. Cell Biol., 16, 663, 10.1016/j.ceb.2004.09.011 · DOI
  16. Baehrecke, 2005, Nat. Rev. Mol. Cell. Biol., 6, 505, 10.1038/nrm1666 · DOI
  17. Golstein, 2005, Cell Death Differ., 12, 1490, 10.1038/sj.cdd.4401607 · DOI
  18. Levine, 2005, J. Clin. Invest., 115, 2679, 10.1172/JCI26390 · DOI
  19. Ogier-Denis, 2003, Biochim. Biophys. Acta, 1603, 113
  20. Gozuacik, 2004, Oncogene, 23, 2891, 10.1038/sj.onc.1207521 · DOI
  21. Arico, 2001, J. Biol. Chem., 276, 35243, 10.1074/jbc.C100319200 · DOI
  22. Blommaart, 1995, J. Biol. Chem., 270, 2320, 10.1074/jbc.270.5.2320 · DOI · Paper page
  23. Noda, 1998, J. Biol. Chem., 273, 3963, 10.1074/jbc.273.7.3963 · DOI
  24. Alva, 2004, Cell Death Differ., 11, 1046, 10.1038/sj.cdd.4401445 · DOI
  25. Kondo, 2005, Nat. Rev. Cancer, 5, 726, 10.1038/nrc1692 · DOI
  26. Bursch, 1996, Carcinogenesis, 17, 1595, 10.1093/carcin/17.8.1595 · DOI
  27. Scarlatti, 2004, J. Biol. Chem., 279, 18384, 10.1074/jbc.M313561200 · DOI · Paper page
  28. Daido, 2004, Cancer Res., 64, 4286, 10.1158/0008-5472.CAN-03-3084 · DOI
  29. Mathias, 1998, Biochem. J., 335, 465, 10.1042/bj3350465 · DOI
  30. Hannun, 2001, Biochemistry, 40, 4893, 10.1021/bi002836k · DOI
  31. Spiegel, 2003, Nat. Rev. Mol. Cell. Biol., 4, 397, 10.1038/nrm1103 · DOI
  32. Levade, 2002, Neurochem. Res., 27, 601, 10.1023/A:1020215815013 · DOI
  33. Ogretmen, 2004, Nat. Rev. Cancer, 4, 604, 10.1038/nrc1411 · DOI
  34. Cuvillier, 1996, Nature, 381, 800, 10.1038/381800a0 · DOI
  35. Pitson, 2000, J. Biol. Chem., 275, 33945, 10.1074/jbc.M006176200 · DOI
  36. Liang, 2001, Cancer Res., 61, 3443
  37. Bektas, 2005, Oncogene, 24, 178, 10.1038/sj.onc.1208019 · DOI
  38. Pattingre, 2004, Methods Enzymol., 390, 17, 10.1016/S0076-6879(04)90002-X · DOI · Paper page
  39. Perry, 1999, Trends Biochem. Sci., 24, 226, 10.1016/S0968-0004(99)01407-3 · DOI
  40. Bligh, 1959, Can. J. Biochem. Physiol., 37, 911, 10.1139/y59-099 · DOI · Paper page
  41. Ames, 1960, J. Biol. Chem., 235, 769, 10.1016/S0021-9258(19)67936-6 · DOI
  42. Granata, 2004, FASEB J., 18, 1456, 10.1096/fj.04-1618fje · DOI
  43. Gijsbers, 2001, Biochim. Biophys. Acta, 1532, 37, 10.1016/S1388-1981(01)00111-1 · DOI
  44. Vessey, 2005, Anal. Biochem., 337, 136, 10.1016/j.ab.2004.10.032 · DOI
  45. O'Luanaigh, 2002, Mol. Biol. Cell, 13, 3730, 10.1091/mbc.e02-04-0213 · DOI
  46. Seglen, 1982, Proc. Natl. Acad. Sci. U. S. A., 79, 1889, 10.1073/pnas.79.6.1889 · DOI
  47. Burnett, 1998, Proc. Natl. Acad. Sci. U. S. A., 95, 1432, 10.1073/pnas.95.4.1432 · DOI
  48. Gingras, 1998, Genes Dev., 12, 502, 10.1101/gad.12.4.502 · DOI
  49. Chen, 2005, Oncogene, 24, 672, 10.1038/sj.onc.1208099 · DOI
  50. Fang, 2003, Curr. Biol., 13, 2037, 10.1016/j.cub.2003.11.021 · DOI
  51. Nava, 2002, Exp. Cell Res., 281, 115, 10.1006/excr.2002.5658 · DOI
  52. Tanida, 1999, Mol. Biol. Cell, 10, 1367, 10.1091/mbc.10.5.1367 · DOI
  53. Tanida, 2001, J. Biol. Chem., 276, 1701, 10.1074/jbc.C000752200 · DOI
  54. Spiegel, 2002, J. Biol. Chem., 277, 25851, 10.1074/jbc.R200007200 · DOI
  55. Van Brocklyn, 1998, J. Cell Biol., 142, 229, 10.1083/jcb.142.1.229 · DOI
  56. Haussinger, 1999, Gastroenterology, 116, 921, 10.1016/S0016-5085(99)70076-4 · DOI
  57. Pattingre, 2003, J. Biol. Chem., 278, 16667, 10.1074/jbc.M210998200 · DOI
  58. Meijer, 2004, Int. J. Biochem. Cell Biol., 36, 2445, 10.1016/j.biocel.2004.02.002 · DOI
  59. Lanterman, 1998, Biochem. J., 332, 525, 10.1042/bj3320525 · DOI
  60. Levine, 2005, Cell, 120, 159
  61. Shang, 2005, J. Biol. Chem., 280, 34644, 10.1074/jbc.M506466200 · DOI
  62. Yamamoto, 2002, Eur. J. Biochem., 269, 139, 10.1046/j.0014-2956.2002.00029.x · DOI
  63. Shohat, 2002, Eur. Cytokine Netw., 13, 398
  64. Martinet, 2002, Arterioscler. Thromb. Vasc. Biol., 22, 2023, 10.1161/01.ATV.0000041843.44312.12 · DOI
  65. Pelled, 2002, J. Biol. Chem., 277, 1957, 10.1074/jbc.M104677200 · DOI
  66. Inbal, 2002, J. Cell Biol., 157, 455, 10.1083/jcb.200109094 · DOI
  67. Thorburn, 2005, Mol. Biol. Cell, 16, 1189, 10.1091/mbc.e04-10-0906 · DOI
  68. Pattingre, 2005, Cell, 122, 927, 10.1016/j.cell.2005.07.002 · DOI · Paper page
  69. Le Stunff, 2002, J. Cell Biol., 158, 1039, 10.1083/jcb.200203123 · DOI
  70. Reiss, 2004, J. Biol. Chem., 279, 1281, 10.1074/jbc.M309646200 · DOI
  71. Gottlieb, 1999, Mol. Cell. Biol. Res. Commun., 1, 66, 10.1006/mcbr.1999.0109 · DOI

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Authors
Lavieu, G., Scarlatti, F., Sala, G., Carpentier, S., Levade, T., Ghidoni, R., Botti, J., & Codogno, P.
Venue
Journal of Biological Chemistry
Publisher
Elsevier BV
Published
2006-03
Volume
281
Issue
13
Pages
8518-8527
ISSN
0021-9258
DOI
10.1074/jbc.m506182200
Cited by
225
References
9
Language
en
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CoChat. (2026). Citation check: Regulation of Autophagy by Sphingosine Kinase 1 and Its Role in Cell Survival during Nutrient Starvation. https://app.cochat.ai/papers/10.1074/jbc.m506182200
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Lavieu, G., Scarlatti, F., Sala, G., Carpentier, S., Levade, T., Ghidoni, R., Botti, J., & Codogno, P. (2006). Regulation of Autophagy by Sphingosine Kinase 1 and Its Role in Cell Survival during Nutrient Starvation. Journal of Biological Chemistry. https://doi.org/10.1074/jbc.m506182200