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Regulation of Autophagy by Sphingosine Kinase 1 and Its Role in Cell Survival during Nutrient Starvation
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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.](/paper-figures/20c5b912917a4931afc1fec2a47a0caa/regulation-of-autophagy-by-sphingosine-kinase-1-and-its-role-in-cell-survival-figure-1.png)
![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.](/paper-figures/8ae365f1cd3946399de0416cee04f72d/regulation-of-autophagy-by-sphingosine-kinase-1-and-its-role-in-cell-survival-figure-2.png)







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“In yeast, dephosphorylation of Atg13 is associated with activation/assembly of the core complex that reflects the reduction of TORC1 and PKA activities.”
From Guidelines for the use and interpretation of assays for monitoring autophagy (4th edition) 1 (2021) · cites this paper as [738]
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A RAPID METHOD OF TOTAL LIPID EXTRACTION AND PURIFICATION
Bligh, E. G., & Dyer, W. J. (1959) · Canadian Journal of Biochemistry and Physiology · doi:10.1139/o59-099 · Cited by 54,751
LC3, a mammalian homologue of yeast Apg8p, is localized in autophagosome membranes after processing.
Kabeya, Y., Mizushima, N., Ueno, T., Yamamoto, A., Kirisako, T., Noda, T., Kominami, E., Ohsumi, Y., & Yoshimori, T. (2000) · The EMBO Journal · doi:10.1093/emboj/19.21.5720 · Cited by 6,605
Phosphorylation and regulation of Akt/PKB by the rictor-mTOR complex
Sarbassov, D. D., Guertin, D. A., Ali, S. M., & Sabatini, D. M. (2005) · Science · doi:10.1126/science.1106148 · Cited by 6,216
Induction of autophagy and inhibition of tumorigenesis by beclin 1
Liang, X. H., Jackson, S., Seaman, M., Brown, K., Kempkes, B., Hibshoosh, H., & Levine, B. (1999) · Nature · doi:10.1038/45257 · Cited by 3,347
The role of autophagy during the early neonatal starvation period
Kuma, A., Hatano, M., Matsui, M., Yamamoto, A., Nakaya, H., Yoshimori, T., Ohsumi, Y., Tokuhisa, T., & Mizushima, N. (2004) · Nature · doi:10.1038/nature03029 · Cited by 2,865
Promotion of tumorigenesis by heterozygous disruption of the beclin 1 autophagy gene
Qu, X., Yu, J., Bhagat, G., Furuya, N., Hibshoosh, H., Troxel, A., Rosen, J., Eskelinen, E.-L., Mizushima, N., Ohsumi, Y., et al. (2003) · Journal of Clinical Investigation · doi:10.1172/jci20039 · Cited by 2,311
Yue, Z., Jin, S., Yang, C., Levine, A. J., & Heintz, N. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2436255100 · Cited by 2,116
Phosphatidic Acid-Mediated Mitogenic Activation of mTOR Signaling
Fang, Y., Vilella-Bach, M., Bachmann, R., Flanigan, A., & Chen, J. (2001) · Science · doi:10.1126/science.1066015 · Cited by 1,055
Beclin–phosphatidylinositol 3‐kinase complex functions at the trans‐Golgi network
Kihara, A., Kabeya, Y., Ohsumi, Y., & Yoshimori, T. (2001) · The EMBO Reports · doi:10.1093/embo-reports/kve061 · Cited by 813
Research works printed but not linked: 71
- Seglen, 1992, Experientia, 48, 158, 10.1007/BF01923509 · DOI
- Dunn, 1994, Trends Cell Biol., 4, 139, 10.1016/0962-8924(94)90069-8 · DOI
- Klionsky, 2000, Science, 290, 1717, 10.1126/science.290.5497.1717 · DOI
- Klionsky, 1999, Annu. Rev. Cell Dev. Biol., 15, 1, 10.1146/annurev.cellbio.15.1.1 · DOI
- Klionsky, 2003, Dev. Cell, 5, 539, 10.1016/S1534-5807(03)00296-X · DOI
- Scott, 2004, Dev. Cell, 7, 167, 10.1016/j.devcel.2004.07.009 · DOI
- Lum, 2005, Cell, 120, 237, 10.1016/j.cell.2004.11.046 · DOI · Paper page
- Boya, 2005, Mol. Cell. Biol., 25, 1025, 10.1128/MCB.25.3.1025-1040.2005 · DOI
- Schweichel, 1973, Teratology, 7, 253, 10.1002/tera.1420070306 · DOI · Paper page
- Clarke, 1990, Anat. Embryol., 181, 195, 10.1007/BF00174615 · DOI · Paper page
- Bursch, 2001, Cell Death Differ., 8, 569, 10.1038/sj.cdd.4400852 · DOI
- Lockshin, 2004, Int. J. Biochem. Cell Biol., 36, 2405, 10.1016/j.biocel.2004.04.011 · DOI
- Shimizu, 2004, Nat. Cell Biol., 6, 1221, 10.1038/ncb1192 · DOI · Paper page
- Yu, 2004, Science, 304, 1500, 10.1126/science.1096645 · DOI
- Edinger, 2004, Curr. Opin. Cell Biol., 16, 663, 10.1016/j.ceb.2004.09.011 · DOI
- Baehrecke, 2005, Nat. Rev. Mol. Cell. Biol., 6, 505, 10.1038/nrm1666 · DOI
- Golstein, 2005, Cell Death Differ., 12, 1490, 10.1038/sj.cdd.4401607 · DOI
- Levine, 2005, J. Clin. Invest., 115, 2679, 10.1172/JCI26390 · DOI
- Ogier-Denis, 2003, Biochim. Biophys. Acta, 1603, 113
- Gozuacik, 2004, Oncogene, 23, 2891, 10.1038/sj.onc.1207521 · DOI
- Arico, 2001, J. Biol. Chem., 276, 35243, 10.1074/jbc.C100319200 · DOI
- Blommaart, 1995, J. Biol. Chem., 270, 2320, 10.1074/jbc.270.5.2320 · DOI · Paper page
- Noda, 1998, J. Biol. Chem., 273, 3963, 10.1074/jbc.273.7.3963 · DOI
- Alva, 2004, Cell Death Differ., 11, 1046, 10.1038/sj.cdd.4401445 · DOI
- Kondo, 2005, Nat. Rev. Cancer, 5, 726, 10.1038/nrc1692 · DOI
- Bursch, 1996, Carcinogenesis, 17, 1595, 10.1093/carcin/17.8.1595 · DOI
- Scarlatti, 2004, J. Biol. Chem., 279, 18384, 10.1074/jbc.M313561200 · DOI · Paper page
- Daido, 2004, Cancer Res., 64, 4286, 10.1158/0008-5472.CAN-03-3084 · DOI
- Mathias, 1998, Biochem. J., 335, 465, 10.1042/bj3350465 · DOI
- Hannun, 2001, Biochemistry, 40, 4893, 10.1021/bi002836k · DOI
- Spiegel, 2003, Nat. Rev. Mol. Cell. Biol., 4, 397, 10.1038/nrm1103 · DOI
- Levade, 2002, Neurochem. Res., 27, 601, 10.1023/A:1020215815013 · DOI
- Ogretmen, 2004, Nat. Rev. Cancer, 4, 604, 10.1038/nrc1411 · DOI
- Cuvillier, 1996, Nature, 381, 800, 10.1038/381800a0 · DOI
- Pitson, 2000, J. Biol. Chem., 275, 33945, 10.1074/jbc.M006176200 · DOI
- Liang, 2001, Cancer Res., 61, 3443
- Bektas, 2005, Oncogene, 24, 178, 10.1038/sj.onc.1208019 · DOI
- Pattingre, 2004, Methods Enzymol., 390, 17, 10.1016/S0076-6879(04)90002-X · DOI · Paper page
- Perry, 1999, Trends Biochem. Sci., 24, 226, 10.1016/S0968-0004(99)01407-3 · DOI
- Bligh, 1959, Can. J. Biochem. Physiol., 37, 911, 10.1139/y59-099 · DOI · Paper page
- Ames, 1960, J. Biol. Chem., 235, 769, 10.1016/S0021-9258(19)67936-6 · DOI
- Granata, 2004, FASEB J., 18, 1456, 10.1096/fj.04-1618fje · DOI
- Gijsbers, 2001, Biochim. Biophys. Acta, 1532, 37, 10.1016/S1388-1981(01)00111-1 · DOI
- Vessey, 2005, Anal. Biochem., 337, 136, 10.1016/j.ab.2004.10.032 · DOI
- O'Luanaigh, 2002, Mol. Biol. Cell, 13, 3730, 10.1091/mbc.e02-04-0213 · DOI
- Seglen, 1982, Proc. Natl. Acad. Sci. U. S. A., 79, 1889, 10.1073/pnas.79.6.1889 · DOI
- Burnett, 1998, Proc. Natl. Acad. Sci. U. S. A., 95, 1432, 10.1073/pnas.95.4.1432 · DOI
- Gingras, 1998, Genes Dev., 12, 502, 10.1101/gad.12.4.502 · DOI
- Chen, 2005, Oncogene, 24, 672, 10.1038/sj.onc.1208099 · DOI
- Fang, 2003, Curr. Biol., 13, 2037, 10.1016/j.cub.2003.11.021 · DOI
- Nava, 2002, Exp. Cell Res., 281, 115, 10.1006/excr.2002.5658 · DOI
- Tanida, 1999, Mol. Biol. Cell, 10, 1367, 10.1091/mbc.10.5.1367 · DOI
- Tanida, 2001, J. Biol. Chem., 276, 1701, 10.1074/jbc.C000752200 · DOI
- Spiegel, 2002, J. Biol. Chem., 277, 25851, 10.1074/jbc.R200007200 · DOI
- Van Brocklyn, 1998, J. Cell Biol., 142, 229, 10.1083/jcb.142.1.229 · DOI
- Haussinger, 1999, Gastroenterology, 116, 921, 10.1016/S0016-5085(99)70076-4 · DOI
- Pattingre, 2003, J. Biol. Chem., 278, 16667, 10.1074/jbc.M210998200 · DOI
- Meijer, 2004, Int. J. Biochem. Cell Biol., 36, 2445, 10.1016/j.biocel.2004.02.002 · DOI
- Lanterman, 1998, Biochem. J., 332, 525, 10.1042/bj3320525 · DOI
- Levine, 2005, Cell, 120, 159
- Shang, 2005, J. Biol. Chem., 280, 34644, 10.1074/jbc.M506466200 · DOI
- Yamamoto, 2002, Eur. J. Biochem., 269, 139, 10.1046/j.0014-2956.2002.00029.x · DOI
- Shohat, 2002, Eur. Cytokine Netw., 13, 398
- Martinet, 2002, Arterioscler. Thromb. Vasc. Biol., 22, 2023, 10.1161/01.ATV.0000041843.44312.12 · DOI
- Pelled, 2002, J. Biol. Chem., 277, 1957, 10.1074/jbc.M104677200 · DOI
- Inbal, 2002, J. Cell Biol., 157, 455, 10.1083/jcb.200109094 · DOI
- Thorburn, 2005, Mol. Biol. Cell, 16, 1189, 10.1091/mbc.e04-10-0906 · DOI
- Pattingre, 2005, Cell, 122, 927, 10.1016/j.cell.2005.07.002 · DOI · Paper page
- Le Stunff, 2002, J. Cell Biol., 158, 1039, 10.1083/jcb.200203123 · DOI
- Reiss, 2004, J. Biol. Chem., 279, 1281, 10.1074/jbc.M309646200 · DOI
- Gottlieb, 1999, Mol. Cell. Biol. Res. Commun., 1, 66, 10.1006/mcbr.1999.0109 · DOI
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Metadata
- 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
- Cited by
- 225
- References
- 9
- Language
- en
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