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Volumn 24, Issue 6, 2013, Pages 272-278

Phosphatidic acid and lipid-sensing by mTOR

Author keywords

DG kinase; LPAAT; MTOR; Phosphatidic acid; Phospholipase D

Indexed keywords

DIACYLGLYCEROL KINASE; ESSENTIAL AMINO ACID; GLUCOSE; LYSOPHOSPHATIDIC ACID; MAMMALIAN TARGET OF RAPAMYCIN; PHOSPHATIDIC ACID; PHOSPHATIDYLCHOLINE; PHOSPHOLIPASE;

EID: 84878252749     PISSN: 10432760     EISSN: 18793061     Source Type: Journal    
DOI: 10.1016/j.tem.2013.02.003     Document Type: Review
Times cited : (91)

References (74)
  • 1
    • 63749105226 scopus 로고    scopus 로고
    • MTOR and the control of whole body metabolism
    • Polak P., Hall M.N. mTOR and the control of whole body metabolism. Curr. Opin. Cell Biol. 2009, 21:209-218.
    • (2009) Curr. Opin. Cell Biol. , vol.21 , pp. 209-218
    • Polak, P.1    Hall, M.N.2
  • 2
    • 32044465506 scopus 로고    scopus 로고
    • TOR signaling in growth and metabolism
    • Wullschleger S., et al. TOR signaling in growth and metabolism. Cell 2006, 124:471-484.
    • (2006) Cell , vol.124 , pp. 471-484
    • Wullschleger, S.1
  • 3
    • 78649348967 scopus 로고    scopus 로고
    • Regulation of the mTOR complex 1 pathway by nutrients, growth factors, and stress
    • Sengupta S., et al. Regulation of the mTOR complex 1 pathway by nutrients, growth factors, and stress. Mol. Cell 2010, 40:310-322.
    • (2010) Mol. Cell , vol.40 , pp. 310-322
    • Sengupta, S.1
  • 4
    • 65649128580 scopus 로고    scopus 로고
    • Amino acid regulation of TOR complex 1
    • Avruch J., et al. Amino acid regulation of TOR complex 1. Am. J. Physiol. Endocrinol. Metab. 2009, 296:E592-E602.
    • (2009) Am. J. Physiol. Endocrinol. Metab. , vol.296
    • Avruch, J.1
  • 5
    • 0035976615 scopus 로고    scopus 로고
    • Phosphatidic acid-mediated mitogenic activation of mTOR signaling
    • Fang Y., et al. Phosphatidic acid-mediated mitogenic activation of mTOR signaling. Science 2001, 294:1942-1945.
    • (2001) Science , vol.294 , pp. 1942-1945
    • Fang, Y.1
  • 6
    • 33846438568 scopus 로고    scopus 로고
    • Regulation of mTOR by phosphatidic acid?
    • Foster D.A. Regulation of mTOR by phosphatidic acid?. Cancer Res. 2007, 67:1-4.
    • (2007) Cancer Res. , vol.67 , pp. 1-4
    • Foster, D.A.1
  • 7
    • 54149107123 scopus 로고    scopus 로고
    • MTOR signaling: PLD takes center stage
    • Sun Y., Chen J. mTOR signaling: PLD takes center stage. Cell Cycle 2008, 7:3118-3123.
    • (2008) Cell Cycle , vol.7 , pp. 3118-3123
    • Sun, Y.1    Chen, J.2
  • 8
    • 62849111751 scopus 로고    scopus 로고
    • Regulation of mTORC1 and mTORC2 complex assembly by phosphatidic acid: competition with rapamycin
    • Toschi A., et al. Regulation of mTORC1 and mTORC2 complex assembly by phosphatidic acid: competition with rapamycin. Mol. Cell. Biol. 2009, 29:1411-1420.
    • (2009) Mol. Cell. Biol. , vol.29 , pp. 1411-1420
    • Toschi, A.1
  • 9
    • 84859778293 scopus 로고    scopus 로고
    • MTOR signaling in growth control and disease
    • Laplante M., Sabatini D.M. mTOR signaling in growth control and disease. Cell 2012, 149:274-293.
    • (2012) Cell , vol.149 , pp. 274-293
    • Laplante, M.1    Sabatini, D.M.2
  • 10
    • 68949103681 scopus 로고    scopus 로고
    • Phosphatidic acid signaling to mTOR: signals for the survival of human cancer cells
    • Foster D.A. Phosphatidic acid signaling to mTOR: signals for the survival of human cancer cells. Biochim. Biophys. Acta 2009, 1791:949-955.
    • (2009) Biochim. Biophys. Acta , vol.1791 , pp. 949-955
    • Foster, D.A.1
  • 11
    • 0028845640 scopus 로고
    • What is the restriction point?
    • Zetterberg A., et al. What is the restriction point?. Curr. Opin. Cell Biol. 1995, 7:835-842.
    • (1995) Curr. Opin. Cell Biol. , vol.7 , pp. 835-842
    • Zetterberg, A.1
  • 12
    • 79960048104 scopus 로고    scopus 로고
    • Regulation of G1 cell cycle progression: distinguishing the restriction point from a nutrient-sensing cell growth checkpoint(s)
    • Foster D., et al. Regulation of G1 cell cycle progression: distinguishing the restriction point from a nutrient-sensing cell growth checkpoint(s). Genes Cancer 2010, 1:1124-1131.
    • (2010) Genes Cancer , vol.1 , pp. 1124-1131
    • Foster, D.1
  • 13
    • 0345732640 scopus 로고    scopus 로고
    • MTOR controls cell cycle progression through its cell growth effectors S6K1 and 4E-BP1/eukaryotic translation initiation factor 4E
    • Fingar D.C., et al. mTOR controls cell cycle progression through its cell growth effectors S6K1 and 4E-BP1/eukaryotic translation initiation factor 4E. Mol. Cell. Biol. 2004, 24:200-216.
    • (2004) Mol. Cell. Biol. , vol.24 , pp. 200-216
    • Fingar, D.C.1
  • 14
    • 39149089610 scopus 로고    scopus 로고
    • Defective TGF-beta signaling sensitizes human cancer cells to rapamycin
    • Gadir N., et al. Defective TGF-beta signaling sensitizes human cancer cells to rapamycin. Oncogene 2008, 27:1055-1062.
    • (2008) Oncogene , vol.27 , pp. 1055-1062
    • Gadir, N.1
  • 15
    • 84858604270 scopus 로고    scopus 로고
    • Metabolic reprogramming: a cancer hallmark even Warburg did not anticipate
    • Ward P.S., et al. Metabolic reprogramming: a cancer hallmark even Warburg did not anticipate. Cancer Cell 2012, 21:297-308.
    • (2012) Cancer Cell , vol.21 , pp. 297-308
    • Ward, P.S.1
  • 16
    • 84859489680 scopus 로고    scopus 로고
    • Molecular damage in cancer: an argument for mTOR-driven aging
    • Blagosklonny M.V. Molecular damage in cancer: an argument for mTOR-driven aging. Aging 2011, 3:1130-1141.
    • (2011) Aging , vol.3 , pp. 1130-1141
    • Blagosklonny, M.V.1
  • 17
    • 78751699575 scopus 로고    scopus 로고
    • Activating mutations of TOR (target of rapamycin)
    • Hardt M., et al. Activating mutations of TOR (target of rapamycin). Genes Cells 2011, 16:141-151.
    • (2011) Genes Cells , vol.16 , pp. 141-151
    • Hardt, M.1
  • 18
    • 84861444859 scopus 로고    scopus 로고
    • Regulation of glucose transport by insulin: traffic control of GLUT4
    • Leto D., Saltiel A.R. Regulation of glucose transport by insulin: traffic control of GLUT4. Nat. Rev. Mol. Cell Biol. 2012, 13:383-396.
    • (2012) Nat. Rev. Mol. Cell Biol. , vol.13 , pp. 383-396
    • Leto, D.1    Saltiel, A.R.2
  • 19
    • 0001221508 scopus 로고
    • On respiratory impairment in cancer cells
    • Warburg O. On respiratory impairment in cancer cells. Science 1956, 124:269-270.
    • (1956) Science , vol.124 , pp. 269-270
    • Warburg, O.1
  • 20
    • 84868019043 scopus 로고    scopus 로고
    • Cancer cell metabolism: one hallmark, many faces
    • Cantor J.R., Sabatini D.M. Cancer cell metabolism: one hallmark, many faces. Cancer Discov. 2012, 2:881-898.
    • (2012) Cancer Discov. , vol.2 , pp. 881-898
    • Cantor, J.R.1    Sabatini, D.M.2
  • 21
    • 0038339003 scopus 로고    scopus 로고
    • Phospholipase D confers rapamycin resistance in human breast cancer cells
    • Chen Y., et al. Phospholipase D confers rapamycin resistance in human breast cancer cells. Oncogene 2003, 22:3937-3942.
    • (2003) Oncogene , vol.22 , pp. 3937-3942
    • Chen, Y.1
  • 22
    • 84862166355 scopus 로고    scopus 로고
    • The phospholipase D1 pathway modulates macroautophagy
    • Dall'Armi C., et al. The phospholipase D1 pathway modulates macroautophagy. Nat. Commun. 2010, 1:142.
    • (2010) Nat. Commun. , vol.1 , pp. 142
    • Dall'Armi, C.1
  • 23
    • 84868121895 scopus 로고    scopus 로고
    • Redundant functions of phospholipases D1 and D2 in platelet alpha-granule release
    • Thielmann I., et al. Redundant functions of phospholipases D1 and D2 in platelet alpha-granule release. J. Thromb. Haemost. 2012, 10.1111/j.1538-7836.2012.04924.x.
    • (2012) J. Thromb. Haemost.
    • Thielmann, I.1
  • 24
    • 33751348056 scopus 로고    scopus 로고
    • Ablation in mice of the mTORC components raptor, rictor, or mLST8 reveals that mTORC2 is required for signaling to Akt-FOXO and PKCα, but not S6K1
    • Guertin D., et al. Ablation in mice of the mTORC components raptor, rictor, or mLST8 reveals that mTORC2 is required for signaling to Akt-FOXO and PKCα, but not S6K1. Dev. Cell 2006, 11:859-871.
    • (2006) Dev. Cell , vol.11 , pp. 859-871
    • Guertin, D.1
  • 25
    • 6344245674 scopus 로고    scopus 로고
    • Disruption of the mouse mTOR gene leads to early postimplantation lethality and prohibits embryonic stem cell development
    • Gangloff Y.G., et al. Disruption of the mouse mTOR gene leads to early postimplantation lethality and prohibits embryonic stem cell development. Mol. Cell. Biol. 2004, 24:9508-9516.
    • (2004) Mol. Cell. Biol. , vol.24 , pp. 9508-9516
    • Gangloff, Y.G.1
  • 26
    • 0033571069 scopus 로고    scopus 로고
    • Phosphatidic acid, a key intermediate in lipid metabolism
    • Athenstaedt K., Daum G. Phosphatidic acid, a key intermediate in lipid metabolism. Eur. J. Biochem. 1999, 266:1-16.
    • (1999) Eur. J. Biochem. , vol.266 , pp. 1-16
    • Athenstaedt, K.1    Daum, G.2
  • 27
    • 67349112100 scopus 로고    scopus 로고
    • Glycerol-3-phosphate acyltransferases: rate limiting enzymes of triacylglycerol biosynthesis
    • Wendel A.A., et al. Glycerol-3-phosphate acyltransferases: rate limiting enzymes of triacylglycerol biosynthesis. Biochim. Biophys. Acta 2009, 1791:501-506.
    • (2009) Biochim. Biophys. Acta , vol.1791 , pp. 501-506
    • Wendel, A.A.1
  • 28
    • 83055173170 scopus 로고    scopus 로고
    • Diacylglycerol kinase ζ: at the crossroads of lipid signaling and protein complex organization
    • Rincon E., et al. Diacylglycerol kinase ζ: at the crossroads of lipid signaling and protein complex organization. Prog. Lipid Res. 2012, 51:1-10.
    • (2012) Prog. Lipid Res. , vol.51 , pp. 1-10
    • Rincon, E.1
  • 29
    • 38149018650 scopus 로고    scopus 로고
    • Diacylglycerol kinases: at the hub of cell signalling
    • Merida I., et al. Diacylglycerol kinases: at the hub of cell signalling. Biochem. J. 2008, 409:1-18.
    • (2008) Biochem. J. , vol.409 , pp. 1-18
    • Merida, I.1
  • 30
    • 33750813851 scopus 로고    scopus 로고
    • Identification of a novel human lysophosphatidic acid acyltransferase, LPAAT-theta, which activates mTOR pathway
    • Tang W., et al. Identification of a novel human lysophosphatidic acid acyltransferase, LPAAT-theta, which activates mTOR pathway. J. Biochem. Mol. Biol. 2006, 39:626-635.
    • (2006) J. Biochem. Mol. Biol. , vol.39 , pp. 626-635
    • Tang, W.1
  • 31
    • 15444378732 scopus 로고    scopus 로고
    • Modulation of the mammalian target of rapamycin pathway by diacylglycerol kinase-produced phosphatidic acid
    • Avila-Flores A., et al. Modulation of the mammalian target of rapamycin pathway by diacylglycerol kinase-produced phosphatidic acid. J. Biol. Chem. 2005, 280:10091-10099.
    • (2005) J. Biol. Chem. , vol.280 , pp. 10091-10099
    • Avila-Flores, A.1
  • 32
    • 79955061238 scopus 로고    scopus 로고
    • Diacylglycerol kinase inhibitor R59022-induced autophagy and apoptosis in the neuronal cell line NG108-15
    • Takita T., et al. Diacylglycerol kinase inhibitor R59022-induced autophagy and apoptosis in the neuronal cell line NG108-15. Arch. Biochem. Biophys. 2011, 509:197-201.
    • (2011) Arch. Biochem. Biophys. , vol.509 , pp. 197-201
    • Takita, T.1
  • 33
    • 79954618943 scopus 로고    scopus 로고
    • Negative regulation of mTOR activation by diacylglycerol kinases
    • Gorentla B., et al. Negative regulation of mTOR activation by diacylglycerol kinases. Blood 2011, 117:4022-4031.
    • (2011) Blood , vol.117 , pp. 4022-4031
    • Gorentla, B.1
  • 34
    • 1542323186 scopus 로고    scopus 로고
    • Inhibition of lysophosphatidic acid acyltransferase beta disrupts proliferative and survival signals in normal cells and induces apoptosis of tumor cells
    • Coon M., et al. Inhibition of lysophosphatidic acid acyltransferase beta disrupts proliferative and survival signals in normal cells and induces apoptosis of tumor cells. Mol. Cancer Ther. 2003, 2:1067-1078.
    • (2003) Mol. Cancer Ther. , vol.2 , pp. 1067-1078
    • Coon, M.1
  • 35
    • 84864003561 scopus 로고    scopus 로고
    • PERK utilizes intrinsic lipid kinase activity to generate phosphatidic acid, mediate Akt activation, and promote adipocyte differentiation
    • Bobrovnikova-Marjon E., et al. PERK utilizes intrinsic lipid kinase activity to generate phosphatidic acid, mediate Akt activation, and promote adipocyte differentiation. Mol. Cell. Biol. 2012, 32:2268-2278.
    • (2012) Mol. Cell. Biol. , vol.32 , pp. 2268-2278
    • Bobrovnikova-Marjon, E.1
  • 36
    • 84856111924 scopus 로고    scopus 로고
    • The unfolded protein response: controlling cell fate decisions under ER stress and beyond
    • Hetz C. The unfolded protein response: controlling cell fate decisions under ER stress and beyond. Nat. Rev. Mol. Cell Biol. 2012, 13:89-102.
    • (2012) Nat. Rev. Mol. Cell Biol. , vol.13 , pp. 89-102
    • Hetz, C.1
  • 37
    • 40649104735 scopus 로고    scopus 로고
    • Loss of the tuberous sclerosis complex tumor suppressors triggers the unfolded protein response to regulate insulin signaling and apoptosis
    • Ozcan U., et al. Loss of the tuberous sclerosis complex tumor suppressors triggers the unfolded protein response to regulate insulin signaling and apoptosis. Mol. Cell 2008, 29:541-551.
    • (2008) Mol. Cell , vol.29 , pp. 541-551
    • Ozcan, U.1
  • 38
    • 37449024702 scopus 로고    scopus 로고
    • The biology of cancer: metabolic reprogramming fuels cell growth and proliferation
    • DeBerardinis R.J., et al. The biology of cancer: metabolic reprogramming fuels cell growth and proliferation. Cell Metab. 2008, 7:11-20.
    • (2008) Cell Metab. , vol.7 , pp. 11-20
    • DeBerardinis, R.J.1
  • 39
    • 43749083041 scopus 로고    scopus 로고
    • Brick by brick: metabolism and tumor cell growth
    • DeBerardinis R.J., et al. Brick by brick: metabolism and tumor cell growth. Curr. Opin. Genet. Dev. 2008, 18:54-61.
    • (2008) Curr. Opin. Genet. Dev. , vol.18 , pp. 54-61
    • DeBerardinis, R.J.1
  • 40
    • 77957907225 scopus 로고    scopus 로고
    • Phospholipase D-mTOR requirement for the Warburg effect in human cancer cells
    • Toschi A., et al. Phospholipase D-mTOR requirement for the Warburg effect in human cancer cells. Cancer Lett. 2010, 299:72-79.
    • (2010) Cancer Lett. , vol.299 , pp. 72-79
    • Toschi, A.1
  • 41
    • 40749163248 scopus 로고    scopus 로고
    • The M2 splice isoform of pyruvate kinase is important for cancer metabolism and tumour growth
    • Christofk H.R., et al. The M2 splice isoform of pyruvate kinase is important for cancer metabolism and tumour growth. Nature 2008, 452:230-233.
    • (2008) Nature , vol.452 , pp. 230-233
    • Christofk, H.R.1
  • 42
    • 77449131347 scopus 로고    scopus 로고
    • Tyrosine phosphorylation inhibits PKM2 to promote the Warburg effect and tumor growth
    • Hitosugi T., et al. Tyrosine phosphorylation inhibits PKM2 to promote the Warburg effect and tumor growth. Sci. Signal. 2009, 2:ra73.
    • (2009) Sci. Signal. , vol.2
    • Hitosugi, T.1
  • 43
    • 66249108601 scopus 로고    scopus 로고
    • Understanding the Warburg effect: the metabolic requirements of cell proliferation
    • Vander Heiden M.G., et al. Understanding the Warburg effect: the metabolic requirements of cell proliferation. Science 2009, 324:1029-1033.
    • (2009) Science , vol.324 , pp. 1029-1033
    • Vander Heiden, M.G.1
  • 44
    • 80051923932 scopus 로고    scopus 로고
    • Functional genomics reveal that the serine synthesis pathway is essential in breast cancer
    • Possemato R., et al. Functional genomics reveal that the serine synthesis pathway is essential in breast cancer. Nature 2011, 476:346-350.
    • (2011) Nature , vol.476 , pp. 346-350
    • Possemato, R.1
  • 45
    • 80052751477 scopus 로고    scopus 로고
    • Pyruvate kinase triggers a metabolic feedback loop that controls redox metabolism in respiring cells
    • Gruning N.M., et al. Pyruvate kinase triggers a metabolic feedback loop that controls redox metabolism in respiring cells. Cell Metab. 2011, 14:415-427.
    • (2011) Cell Metab. , vol.14 , pp. 415-427
    • Gruning, N.M.1
  • 46
    • 60749121730 scopus 로고    scopus 로고
    • Dietary n-6 and n-3 polyunsaturated fatty acids: from biochemistry to clinical implications in cardiovascular prevention
    • Russo G.L. Dietary n-6 and n-3 polyunsaturated fatty acids: from biochemistry to clinical implications in cardiovascular prevention. Biochem. Pharmacol. 2009, 77:937-946.
    • (2009) Biochem. Pharmacol. , vol.77 , pp. 937-946
    • Russo, G.L.1
  • 47
    • 0026906553 scopus 로고
    • The essential fatty acids
    • Sardesai V.M. The essential fatty acids. Nutr. Clin. Pract. 1992, 7:179-186.
    • (1992) Nutr. Clin. Pract. , vol.7 , pp. 179-186
    • Sardesai, V.M.1
  • 48
    • 84863115883 scopus 로고    scopus 로고
    • Glycerolipid signals alter mTOR complex 2 (mTORC2) to diminish insulin signaling
    • Zhang C., et al. Glycerolipid signals alter mTOR complex 2 (mTORC2) to diminish insulin signaling. Proc. Natl. Acad. Sci. U.S.A. 2012, 109:1667-1672.
    • (2012) Proc. Natl. Acad. Sci. U.S.A. , vol.109 , pp. 1667-1672
    • Zhang, C.1
  • 49
    • 80051917141 scopus 로고    scopus 로고
    • Phosphatidic acid activates mammalian target of rapamycin complex 1 (mTORC1) kinase by displacing FK506 binding protein 38 (FKBP38) and exerting an allosteric effect
    • Yoon M.S., et al. Phosphatidic acid activates mammalian target of rapamycin complex 1 (mTORC1) kinase by displacing FK506 binding protein 38 (FKBP38) and exerting an allosteric effect. J. Biol. Chem. 2011, 286:29568-29574.
    • (2011) J. Biol. Chem. , vol.286 , pp. 29568-29574
    • Yoon, M.S.1
  • 50
    • 79960387847 scopus 로고    scopus 로고
    • Phospholipase D mediates nutrient input to mammalian target of rapamycin complex 1 (mTORC1)
    • Xu L., et al. Phospholipase D mediates nutrient input to mammalian target of rapamycin complex 1 (mTORC1). J. Biol. Chem. 2011, 286:25477-25486.
    • (2011) J. Biol. Chem. , vol.286 , pp. 25477-25486
    • Xu, L.1
  • 51
    • 84855731134 scopus 로고    scopus 로고
    • Class III PI-3-kinase activates phospholipase D in an amino acid-sensing mTORC1 pathway
    • Yoon M.S., et al. Class III PI-3-kinase activates phospholipase D in an amino acid-sensing mTORC1 pathway. J. Cell Biol. 2011, 195:435-447.
    • (2011) J. Cell Biol. , vol.195 , pp. 435-447
    • Yoon, M.S.1
  • 52
    • 38549134335 scopus 로고    scopus 로고
    • Structural characterization of the interaction of mTOR with phosphatidic acid and a novel class of inhibitor: compelling evidence for a central role of the FRB domain in small molecule-mediated regulation of mTOR
    • Veverka V., et al. Structural characterization of the interaction of mTOR with phosphatidic acid and a novel class of inhibitor: compelling evidence for a central role of the FRB domain in small molecule-mediated regulation of mTOR. Oncogene 2008, 27:585-595.
    • (2008) Oncogene , vol.27 , pp. 585-595
    • Veverka, V.1
  • 53
    • 84862555250 scopus 로고    scopus 로고
    • The FKBP-rapamycin binding domain of human TOR undergoes strong conformational changes in the presence of membrane mimetics with and without the regulator phosphatidic acid
    • Rodriguez Camargo D.C., et al. The FKBP-rapamycin binding domain of human TOR undergoes strong conformational changes in the presence of membrane mimetics with and without the regulator phosphatidic acid. Biochemistry 2012, 51:4909-4921.
    • (2012) Biochemistry , vol.51 , pp. 4909-4921
    • Rodriguez Camargo, D.C.1
  • 54
    • 33644503868 scopus 로고    scopus 로고
    • Identification of pathways regulating cell size and cell-cycle progression by RNAi
    • Bjorklund M., et al. Identification of pathways regulating cell size and cell-cycle progression by RNAi. Nature 2006, 439:1009-1013.
    • (2006) Nature , vol.439 , pp. 1009-1013
    • Bjorklund, M.1
  • 55
    • 78649808161 scopus 로고    scopus 로고
    • Phospholipase D controls Dictyostelium development by regulating G protein signaling
    • Ray S., et al. Phospholipase D controls Dictyostelium development by regulating G protein signaling. Cell. Signal. 2011, 23:335-343.
    • (2011) Cell. Signal. , vol.23 , pp. 335-343
    • Ray, S.1
  • 56
    • 84856704227 scopus 로고    scopus 로고
    • TOR complex 2 (TORC2) in Dictyostelium suppresses phagocytic nutrient capture independently of TORC1-mediated nutrient sensing
    • Rosel D., et al. TOR complex 2 (TORC2) in Dictyostelium suppresses phagocytic nutrient capture independently of TORC1-mediated nutrient sensing. J. Cell Sci. 2012, 125:37-48.
    • (2012) J. Cell Sci. , vol.125 , pp. 37-48
    • Rosel, D.1
  • 57
    • 0242664746 scopus 로고    scopus 로고
    • Functional analysis of a phosphatidic acid binding domain in human Raf-1 kinase: mutations in the phosphatidate binding domain lead to tail and trunk abnormalities in developing zebrafish embryos
    • Ghosh S., et al. Functional analysis of a phosphatidic acid binding domain in human Raf-1 kinase: mutations in the phosphatidate binding domain lead to tail and trunk abnormalities in developing zebrafish embryos. J. Biol. Chem. 2003, 278:45690-45696.
    • (2003) J. Biol. Chem. , vol.278 , pp. 45690-45696
    • Ghosh, S.1
  • 58
    • 0034651872 scopus 로고    scopus 로고
    • An EGF receptor/Ral-GTPase signaling cascade regulates c-Src activity and substrate specificity
    • Goi T., et al. An EGF receptor/Ral-GTPase signaling cascade regulates c-Src activity and substrate specificity. EMBO J. 2000, 19:623-630.
    • (2000) EMBO J. , vol.19 , pp. 623-630
    • Goi, T.1
  • 59
    • 0028818914 scopus 로고
    • Involvement of Ral GTPase in v-Src-induced phospholipase D activation
    • Jiang H., et al. Involvement of Ral GTPase in v-Src-induced phospholipase D activation. Nature 1995, 378:409-412.
    • (1995) Nature , vol.378 , pp. 409-412
    • Jiang, H.1
  • 60
    • 58049216316 scopus 로고    scopus 로고
    • RalA functions as an indispensable signal mediator for the nutrient-sensing system
    • Maehama T., et al. RalA functions as an indispensable signal mediator for the nutrient-sensing system. J. Biol. Chem. 2008, 283:35053-35059.
    • (2008) J. Biol. Chem. , vol.283 , pp. 35053-35059
    • Maehama, T.1
  • 61
    • 84859018387 scopus 로고    scopus 로고
    • Phospholipase D and mTORC1: nutrients are what bring them together
    • Wiczer B.M., Thomas G. Phospholipase D and mTORC1: nutrients are what bring them together. Sci. Signal. 2012, 5:pe13.
    • (2012) Sci. Signal. , vol.5
    • Wiczer, B.M.1    Thomas, G.2
  • 62
    • 0037436828 scopus 로고    scopus 로고
    • Phospholipase D prevents apoptosis in v-Src-transformed rat fibroblasts and MDA-MB-231 breast cancer cells
    • Zhong M., et al. Phospholipase D prevents apoptosis in v-Src-transformed rat fibroblasts and MDA-MB-231 breast cancer cells. Biochem. Biophys. Res. Commun. 2003, 302:615-619.
    • (2003) Biochem. Biophys. Res. Commun. , vol.302 , pp. 615-619
    • Zhong, M.1
  • 63
    • 13244289821 scopus 로고    scopus 로고
    • Alternative phospholipase D/mTOR survival signal in human breast cancer cells
    • Chen Y., et al. Alternative phospholipase D/mTOR survival signal in human breast cancer cells. Oncogene 2005, 24:672-679.
    • (2005) Oncogene , vol.24 , pp. 672-679
    • Chen, Y.1
  • 64
    • 23844465938 scopus 로고    scopus 로고
    • Survival signals generated by estrogen and phospholipase D in MCF-7 breast cancer cells are dependent on Myc
    • Rodrik V., et al. Survival signals generated by estrogen and phospholipase D in MCF-7 breast cancer cells are dependent on Myc. Mol. Cell. Biol. 2005, 25:7917-7925.
    • (2005) Mol. Cell. Biol. , vol.25 , pp. 7917-7925
    • Rodrik, V.1
  • 65
    • 33749337752 scopus 로고    scopus 로고
    • Myc stabilization in response to estrogen and phospholipase D in MCF-7 breast cancer cells
    • Rodrik V., et al. Myc stabilization in response to estrogen and phospholipase D in MCF-7 breast cancer cells. FEBS Lett. 2006, 580:5647-5652.
    • (2006) FEBS Lett. , vol.580 , pp. 5647-5652
    • Rodrik, V.1
  • 66
    • 27744539859 scopus 로고    scopus 로고
    • MTOR-dependent suppression of protein phosphatase 2A is critical for phospholipase D survival signals in human breast cancer cells
    • Hui L., et al. mTOR-dependent suppression of protein phosphatase 2A is critical for phospholipase D survival signals in human breast cancer cells. J. Biol. Chem. 2005, 280:35829-35835.
    • (2005) J. Biol. Chem. , vol.280 , pp. 35829-35835
    • Hui, L.1
  • 67
    • 33744943819 scopus 로고    scopus 로고
    • Phospholipase D couples survival and migration signals in stress response of human cancer cells
    • Zheng Y., et al. Phospholipase D couples survival and migration signals in stress response of human cancer cells. J. Biol. Chem. 2006, 281:15862-15868.
    • (2006) J. Biol. Chem. , vol.281 , pp. 15862-15868
    • Zheng, Y.1
  • 68
    • 36048979906 scopus 로고    scopus 로고
    • Phospholipase D provides a survival signal in human cancer cells with activated H-Ras or K-Ras
    • Shi M., et al. Phospholipase D provides a survival signal in human cancer cells with activated H-Ras or K-Ras. Cancer Lett. 2007, 258:268-275.
    • (2007) Cancer Lett. , vol.258 , pp. 268-275
    • Shi, M.1
  • 69
    • 48249084606 scopus 로고    scopus 로고
    • Honokiol suppresses survival signals mediated by Ras-dependent phospholipase D activity in human cancer cells
    • Garcia A., et al. Honokiol suppresses survival signals mediated by Ras-dependent phospholipase D activity in human cancer cells. Clin. Cancer Res. 2008, 14:4267-4274.
    • (2008) Clin. Cancer Res. , vol.14 , pp. 4267-4274
    • Garcia, A.1
  • 70
    • 34447256138 scopus 로고    scopus 로고
    • Honokiol, a natural biphenyl, inhibits in vitro and in vivo growth of breast cancer through induction of apoptosis and cell cycle arrest
    • Wolf I., et al. Honokiol, a natural biphenyl, inhibits in vitro and in vivo growth of breast cancer through induction of apoptosis and cell cycle arrest. Int. J. Oncol. 2007, 30:1529-1537.
    • (2007) Int. J. Oncol. , vol.30 , pp. 1529-1537
    • Wolf, I.1
  • 71
    • 77956730942 scopus 로고    scopus 로고
    • Design, synthesis, and biological evaluation of halogenated N-(2-(4-oxo-1-phenyl-1,3,8-triazaspiro[4.5]decan-8-yl)ethyl)benzamides: discovery of an isoform-selective small molecule phospholipase D2 inhibitor
    • Lavieri R.R., et al. Design, synthesis, and biological evaluation of halogenated N-(2-(4-oxo-1-phenyl-1,3,8-triazaspiro[4.5]decan-8-yl)ethyl)benzamides: discovery of an isoform-selective small molecule phospholipase D2 inhibitor. J. Med. Chem. 2010, 53:6706-6719.
    • (2010) J. Med. Chem. , vol.53 , pp. 6706-6719
    • Lavieri, R.R.1
  • 72
    • 61849108279 scopus 로고    scopus 로고
    • Design and synthesis of isoform-selective phospholipase D (PLD) inhibitors. Part I: Impact of alternative halogenated privileged structures for PLD1 specificity
    • Lewis J.A., et al. Design and synthesis of isoform-selective phospholipase D (PLD) inhibitors. Part I: Impact of alternative halogenated privileged structures for PLD1 specificity. Bioorg. Med. Chem. Lett. 2009, 19:1916-1920.
    • (2009) Bioorg. Med. Chem. Lett. , vol.19 , pp. 1916-1920
    • Lewis, J.A.1
  • 73
    • 63149128774 scopus 로고    scopus 로고
    • Design and synthesis of isoform-selective phospholipase D (PLD) inhibitors. Part II. Identification of the 1,3,8-triazaspiro[4,5]decan-4-one privileged structure that engenders PLD2 selectivity
    • Lavieri R., et al. Design and synthesis of isoform-selective phospholipase D (PLD) inhibitors. Part II. Identification of the 1,3,8-triazaspiro[4,5]decan-4-one privileged structure that engenders PLD2 selectivity. Bioorg. Med. Chem. Lett. 2009, 19:2240-2243.
    • (2009) Bioorg. Med. Chem. Lett. , vol.19 , pp. 2240-2243
    • Lavieri, R.1
  • 74
    • 34748912615 scopus 로고    scopus 로고
    • Fatty acid synthase and the lipogenic phenotype in cancer pathogenesis
    • Menendez J.A., Lupu R. Fatty acid synthase and the lipogenic phenotype in cancer pathogenesis. Nat. Rev. Cancer 2007, 7:763-777.
    • (2007) Nat. Rev. Cancer , vol.7 , pp. 763-777
    • Menendez, J.A.1    Lupu, R.2


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