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Volumn 34, Issue 1, 2014, Pages 84-95

Temporal production of the signaling lipid phosphatidic acid by phospholipase D2 determines the output of extracellular signal-regulated kinase signaling in cancer cells

Author keywords

[No Author keywords available]

Indexed keywords

EPIDERMAL GROWTH FACTOR; MITOGEN ACTIVATED PROTEIN KINASE; PHOSPHATIDIC ACID; PHOSPHOLIPASE D2; TRANSCRIPTION FACTOR ELK 1; TRANSCRIPTION FACTOR FRA 1;

EID: 84891437205     PISSN: 02707306     EISSN: 10985549     Source Type: Journal    
DOI: 10.1128/MCB.00987-13     Document Type: Article
Times cited : (94)

References (80)
  • 1
    • 33646061961 scopus 로고    scopus 로고
    • Signaling functions of phosphatidic acid
    • Wang X, Devaiah SP, Zhang W, Welti R. 2006. Signaling functions of phosphatidic acid. Prog. Lipid Res. 45:250-278. http://dx.doi.org/10.1016/j.plipres.2006.01.005.
    • (2006) Prog. Lipid Res. , vol.45 , pp. 250-278
    • Wang, X.1    Devaiah, S.P.2    Zhang, W.3    Welti, R.4
  • 2
    • 34447580192 scopus 로고    scopus 로고
    • PA promoted to manager
    • Hancock JF. 2007. PA promoted to manager. Nat. Cell Biol. 9:615-617. http://dx.doi.org/10.1038/ncb0607-615.
    • (2007) Nat. Cell Biol. , vol.9 , pp. 615-617
    • Hancock, J.F.1
  • 3
    • 79959457450 scopus 로고    scopus 로고
    • Regulation of phospholipid synthesis in the yeast Saccharomyces cerevisiae
    • Carman GM, Han GS. 2011. Regulation of phospholipid synthesis in the yeast Saccharomyces cerevisiae. Annu. Rev. Biochem. 80:859-883. http://dx.doi.org/10.1146/annurev-biochem-060409-092229.
    • (2011) Annu. Rev. Biochem. , vol.80 , pp. 859-883
    • Carman, G.M.1    Han, G.S.2
  • 4
    • 68949149746 scopus 로고    scopus 로고
    • Phosphatidic acid signaling regulation of Ras superfamily of small guanosine triphosphatases
    • Zhang Y, Du G. 2009. Phosphatidic acid signaling regulation of Ras superfamily of small guanosine triphosphatases. Biochim. Biophys. Acta 1791:850-855. http://dx.doi.org/10.1016/j.bbalip.2009.05.013.
    • (2009) Biochim. Biophys. Acta , vol.1791 , pp. 850-855
    • Zhang, Y.1    Du, G.2
  • 5
    • 80054069569 scopus 로고    scopus 로고
    • Phospholipase D: enzymology, functionality, and chemical modulation
    • Selvy PE, Lavieri RR, Lindsley CW, Brown HA. 2011. Phospholipase D: enzymology, functionality, and chemical modulation. Chem. Rev. 111: 6064-6119. http://dx.doi.org/10.1021/cr200296t.
    • (2011) Chem. Rev. , vol.111 , pp. 6064-6119
    • Selvy, P.E.1    Lavieri, R.R.2    Lindsley, C.W.3    Brown, H.A.4
  • 6
    • 80054080494 scopus 로고    scopus 로고
    • Regulation and functions of diacylglycerol kinases
    • Shulga YV, Topham MK, Epand RM. 2011. Regulation and functions of diacylglycerol kinases. Chem. Rev. 111:6186-6208. http://dx.doi.org/10.1021/cr1004106.
    • (2011) Chem. Rev. , vol.111 , pp. 6186-6208
    • Shulga, Y.V.1    Topham, M.K.2    Epand, R.M.3
  • 7
    • 84855356842 scopus 로고    scopus 로고
    • Mammalian phospholipase D physiological and pathological roles
    • Peng X, Frohman MA. 2012. Mammalian phospholipase D physiological and pathological roles. Acta Physiol. 204:219-226. http://dx.doi.org/10.1111/j.1748-1716.2011.02298.x.
    • (2012) Acta Physiol , vol.204 , pp. 219-226
    • Peng, X.1    Frohman, M.A.2
  • 8
    • 33646336602 scopus 로고    scopus 로고
    • MAPK signal specificity: the right place at the right time
    • Murphy LO, Blenis J. 2006. MAPK signal specificity: the right place at the right time. Trends Biochem. Sci. 31:268-275. http://dx.doi.org/10.1016/j.tibs.2006.03.009.
    • (2006) Trends Biochem. Sci. , vol.31 , pp. 268-275
    • Murphy, L.O.1    Blenis, J.2
  • 9
    • 34248575149 scopus 로고    scopus 로고
    • Integrating signals from RTKs to ERK/MAPK
    • McKay MM, Morrison DK. 2007. Integrating signals from RTKs to ERK/MAPK. Oncogene 26:3113-3121. http://dx.doi.org/10.1038/sj.onc.1210394.
    • (2007) Oncogene , vol.26 , pp. 3113-3121
    • McKay, M.M.1    Morrison, D.K.2
  • 10
    • 23844494402 scopus 로고    scopus 로고
    • The duration, magnitude and compartmentalization of ERK MAP kinase activity: mechanisms for providing signaling specificity
    • Ebisuya M, Kondoh K, Nishida E. 2005. The duration, magnitude and compartmentalization of ERK MAP kinase activity: mechanisms for providing signaling specificity. J. Cell Sci. 118:2997-3002. http://dx.doi.org/10.1242/jcs.02505.
    • (2005) J. Cell Sci. , vol.118 , pp. 2997-3002
    • Ebisuya, M.1    Kondoh, K.2    Nishida, E.3
  • 11
    • 65949119310 scopus 로고    scopus 로고
    • How ERK1/2 activation controls cell proliferation and cell death: is subcellular localization the answer?
    • Mebratu Y, Tesfaigzi Y. 2009. How ERK1/2 activation controls cell proliferation and cell death: is subcellular localization the answer? Cell Cycle 8:1168-1175. http://dx.doi.org/10.4161/cc.8.8.8147.
    • (2009) Cell Cycle , vol.8 , pp. 1168-1175
    • Mebratu, Y.1    Tesfaigzi, Y.2
  • 12
    • 34447568476 scopus 로고    scopus 로고
    • Phospholipase D2-generated phosphatidic acid couples EGFR stimulation to Ras activation by Sos
    • Zhao C, Du G, Skowronek K, Frohman MA, Bar-Sagi D. 2007. Phospholipase D2-generated phosphatidic acid couples EGFR stimulation to Ras activation by Sos. Nat. Cell Biol. 9:706-712. http://dx.doi.org/10.1038/ncb1594.
    • (2007) Nat. Cell Biol. , vol.9 , pp. 706-712
    • Zhao, C.1    Du, G.2    Skowronek, K.3    Frohman, M.A.4    Bar-Sagi, D.5
  • 13
    • 0033534687 scopus 로고    scopus 로고
    • Phospholipase D and its product, phosphatidic acid, mediate agonist-dependent Raf-1 translocation to the plasma membrane and the activation of the MAP kinase pathway
    • Rizzo MA, Shome K, Vasudevan C, Stolz DB, Sung T-C, Frohman MA, Watkins SC, Romero G. 1999. Phospholipase D and its product, phosphatidic acid, mediate agonist-dependent Raf-1 translocation to the plasma membrane and the activation of the MAP kinase pathway. J. Biol. Chem. 274:1131-1139. http://dx.doi.org/10.1074/jbc.274.2.1131.
    • (1999) J. Biol. Chem. , vol.274 , pp. 1131-1139
    • Rizzo, M.A.1    Shome, K.2    Vasudevan, C.3    Stolz, D.B.4    Sung, T.-C.5    Frohman, M.A.6    Watkins, S.C.7    Romero, G.8
  • 14
    • 34447579251 scopus 로고    scopus 로고
    • The lymphocyte function-associated antigen-1 receptor costimulates plasma membrane Ras via phospholipase D2
    • Mor A, Campi G, Du G, Zheng Y, Foster DA, Dustin ML, Philips MR. 2007. The lymphocyte function-associated antigen-1 receptor costimulates plasma membrane Ras via phospholipase D2. Nat. Cell Biol. 9:713-719. http://dx.doi.org/10.1038/ncb1592.
    • (2007) Nat. Cell Biol. , vol.9 , pp. 713-719
    • Mor, A.1    Campi, G.2    Du, G.3    Zheng, Y.4    Foster, D.A.5    Dustin, M.L.6    Philips, M.R.7
  • 15
    • 34248583886 scopus 로고    scopus 로고
    • MAP kinase signalling pathways in cancer
    • Dhillon AS, Hagan S, Rath O, Kolch W. 2007. MAP kinase signalling pathways in cancer. Oncogene 26:3279-3290. http://dx.doi.org/10.1038/sj.onc.1210421.
    • (2007) Oncogene , vol.26 , pp. 3279-3290
    • Dhillon, A.S.1    Hagan, S.2    Rath, O.3    Kolch, W.4
  • 16
    • 34248591612 scopus 로고    scopus 로고
    • Targeting the Raf-MEK-ERK mitogen-activated protein kinase cascade for the treatment of cancer
    • Roberts PJ, Der CJ. 2007. Targeting the Raf-MEK-ERK mitogen-activated protein kinase cascade for the treatment of cancer. Oncogene 26:3291-3310. http://dx.doi.org/10.1038/sj.onc.1210422.
    • (2007) Oncogene , vol.26 , pp. 3291-3310
    • Roberts, P.J.1    Der, C.J.2
  • 18
    • 33645274673 scopus 로고    scopus 로고
    • Analyzing phosphoinositides and their interacting proteins
    • Rusten TE, Stenmark H. 2006. Analyzing phosphoinositides and their interacting proteins. Nat. Methods 3:251-258. http://dx.doi.org/10.1038/nmeth867.
    • (2006) Nat. Methods , vol.3 , pp. 251-258
    • Rusten, T.E.1    Stenmark, H.2
  • 19
    • 70649093097 scopus 로고    scopus 로고
    • Lipidomics: a mass spectrometry based systems level analysis of cellular lipids
    • Ivanova PT, Milne SB, Myers DS, Brown HA. 2009. Lipidomics: a mass spectrometry based systems level analysis of cellular lipids. Curr. Opin. Chem. Biol. 13:526-531. http://dx.doi.org/10.1016/j.cbpa.2009.08.011.
    • (2009) Curr. Opin. Chem. Biol. , vol.13 , pp. 526-531
    • Ivanova, P.T.1    Milne, S.B.2    Myers, D.S.3    Brown, H.A.4
  • 21
    • 0033571069 scopus 로고    scopus 로고
    • Phosphatidic acid, a key intermediate in lipid metabolism
    • Athenstaedt K, Daum G. 1999. Phosphatidic acid, a key intermediate in lipid metabolism. Eur. J. Biochem. 266:1-16. http://dx.doi.org/10.1046/j.1432-1327.1999.00822.x.
    • (1999) Eur. J. Biochem. , vol.266 , pp. 1-16
    • Athenstaedt, K.1    Daum, G.2
  • 22
    • 0037177352 scopus 로고    scopus 로고
    • Visualizing cellular phosphoinositide pools with GFP-fused protein-modules
    • Balla T, Varnai P. 2002. Visualizing cellular phosphoinositide pools with GFP-fused protein-modules. Sci. STKE 2002(125):pl3. http://dx.doi.org/10.1126/scisignal.1252002pl3.
    • (2002) Sci. STKE , vol.2002
    • Balla, T.1    Varnai, P.2
  • 24
    • 62149152761 scopus 로고    scopus 로고
    • 5-Fluoro-2-indolyl des-chlorohalopemide (FIPI), a phospholipase D pharmacological inhibitor that alters cell spreading and inhibits chemotaxis
    • Su W, Yeku O, Olepu S, Genna A, Park JS, Ren H, Du G, Gelb MH, Morris AJ, Frohman MA. 2009. 5-Fluoro-2-indolyl des-chlorohalopemide (FIPI), a phospholipase D pharmacological inhibitor that alters cell spreading and inhibits chemotaxis. Mol. Pharmacol. 75:437-446. http://dx.doi.org/10.1124/mol.108.053298.
    • (2009) Mol. Pharmacol. , vol.75 , pp. 437-446
    • Su, W.1    Yeku, O.2    Olepu, S.3    Genna, A.4    Park, J.S.5    Ren, H.6    Du, G.7    Gelb, M.H.8    Morris, A.J.9    Frohman, M.A.10
  • 26
    • 0034630158 scopus 로고    scopus 로고
    • A comparison of the activity, sequence specificity, and CRM1-dependence of different nuclear export signals
    • Henderson BR, Eleftheriou A. 2000. A comparison of the activity, sequence specificity, and CRM1-dependence of different nuclear export signals. Exp. Cell Res. 256:213-224. http://dx.doi.org/10.1006/excr.2000.4825.
    • (2000) Exp. Cell Res. , vol.256 , pp. 213-224
    • Henderson, B.R.1    Eleftheriou, A.2
  • 28
    • 62449309815 scopus 로고    scopus 로고
    • A lipid-signaled myosin phosphatase surge disperses cortical contractile force early in cell spreading
    • Du G, Frohman MA. 2009. A lipid-signaled myosin phosphatase surge disperses cortical contractile force early in cell spreading. Mol. Biol. Cell 20:200-208. http://dx.doi.org/10.1091/mbc. E08-06-0555.
    • (2009) Mol. Biol. Cell , vol.20 , pp. 200-208
    • Du, G.1    Frohman, M.A.2
  • 29
    • 1542283816 scopus 로고    scopus 로고
    • Phospholipase D2 localizes to the plasma membrane and regulates angiotensin II receptor endocytosis
    • Du G, Huang P, Liang BT, Frohman MA. 2004. Phospholipase D2 localizes to the plasma membrane and regulates angiotensin II receptor endocytosis. Mol. Biol. Cell 15:1024-1030. http://dx.doi.org/10.1091/mbc. E03-09-0673.
    • (2004) Mol. Biol. Cell , vol.15 , pp. 1024-1030
    • Du, G.1    Huang, P.2    Liang, B.T.3    Frohman, M.A.4
  • 30
    • 29044435623 scopus 로고    scopus 로고
    • RhoA-mediated phospholipase D1 signaling is not required for the formation of stress fibers and focal adhesions
    • Su W, Chardin P, Yamazaki M, Kanaho Y, Du G. 2006. RhoA-mediated phospholipase D1 signaling is not required for the formation of stress fibers and focal adhesions. Cell. Signal. 18:469-478. http://dx.doi.org/10.1016/j.cellsig.2005.05.027.
    • (2006) Cell. Signal. , vol.18 , pp. 469-478
    • Su, W.1    Chardin, P.2    Yamazaki, M.3    Kanaho, Y.4    Du, G.5
  • 31
    • 67649198206 scopus 로고    scopus 로고
    • Phospholipase D1 regulates lymphocyte adhesion via upregulation of Rap1 at the plasma membrane
    • Mor A, Wynne JP, Ahearn IM, Dustin ML, Du G, Philips MR. 2009. Phospholipase D1 regulates lymphocyte adhesion via upregulation of Rap1 at the plasma membrane. Mol. Cell. Biol. 29:3297-3306. http://dx.doi.org/10.1128/MCB.00366-09.
    • (2009) Mol. Cell. Biol. , vol.29 , pp. 3297-3306
    • Mor, A.1    Wynne, J.P.2    Ahearn, I.M.3    Dustin, M.L.4    Du, G.5    Philips, M.R.6
  • 33
    • 0041671075 scopus 로고    scopus 로고
    • Regulation of phospholipase D1 subcellular cycling through coordination of multiple membrane association motifs
    • Du G, Altshuller YM, Vitale N, Huang P, Chasserot-Golaz S, Morris AJ, Bader MF, Frohman MA. 2003. Regulation of phospholipase D1 subcellular cycling through coordination of multiple membrane association motifs. J. Cell Biol. 162:305-315. http://dx.doi.org/10.1083/jcb.200302033.
    • (2003) J. Cell Biol. , vol.162 , pp. 305315
    • Du, G.1    Altshuller, Y.M.2    Vitale, N.3    Huang, P.4    Chasserot-Golaz, S.5    Morris, A.J.6    Bader, M.F.7    Frohman, M.A.8
  • 34
    • 17644418754 scopus 로고    scopus 로고
    • Full deacylation of polyethylenimine dramatically boosts its gene delivery efficiency and specificity to mouse lung
    • Thomas M, Lu JJ, Ge Q, Zhang C, Chen J, Klibanov AM. 2005. Full deacylation of polyethylenimine dramatically boosts its gene delivery efficiency and specificity to mouse lung. Proc. Natl. Acad. Sci. U. S. A. 102: 5679-5684. http://dx.doi.org/10.1073/pnas.0502067102.
    • (2005) Proc. Natl. Acad. Sci. U. S. A. , vol.102 , pp. 56795684
    • Thomas, M.1    Lu, J.J.2    Ge, Q.3    Zhang, C.4    Chen, J.5    Klibanov, A.M.6
  • 36
    • 23644456957 scopus 로고    scopus 로고
    • Peroxiredoxin II functions as a signal terminator for H2O2-activated phospholipase D1
    • Xiao N, Du G, Frohman MA. 2005. Peroxiredoxin II functions as a signal terminator for H2O2-activated phospholipase D1. FEBS J. 272:3929-3937. http://dx.doi.org/10.1111/j.1742-4658.2005.04809.x.
    • (2005) FEBS J , vol.272 , pp. 39293937
    • Xiao, N.1    Du, G.2    Frohman, M.A.3
  • 37
    • 0034798755 scopus 로고    scopus 로고
    • G-protein-coupled receptor regulation of phospholipase D
    • Du G, Morris AJ, Sciorra VA, Frohman MA. 2002. G-protein-coupled receptor regulation of phospholipase D. Methods Enzymol. 345:265-274. http://dx.doi.org/10.1016/S0076-6879(02)45022-7.
    • (2002) Methods Enzymol , vol.345 , pp. 265274
    • Du, G.1    Morris, A.J.2    Sciorra, V.A.3    Frohman, M.A.4
  • 38
    • 1642546271 scopus 로고    scopus 로고
    • Positive and negative regulation of a SNARE protein by control of intracellular localization
    • Nakanishi H, de los Santos P, Neiman AM. 2004. Positive and negative regulation of a SNARE protein by control of intracellular localization. Mol. Biol. Cell 15:1802-1815. http://dx.doi.org/10.1091/mbc. E03-11-0798.
    • (2004) Mol. Biol. Cell , vol.15 , pp. 18021815
    • Nakanishi, H.1    de los Santos, P.2    Neiman, A.M.3
  • 39
    • 35348819374 scopus 로고    scopus 로고
    • In vitro fusion catalyzed by the sporulation-specific t-SNARE light-chain Spo20p is stimulated by phosphatidic acid
    • Liu S, Wilson KA, Rice-Stitt T, Neiman AM, McNew JA. 2007. In vitro fusion catalyzed by the sporulation-specific t-SNARE light-chain Spo20p is stimulated by phosphatidic acid. Traffic 8:1630-1643. http://dx.doi.org/10.1111/j.1600-0854.2007.00628.x.
    • (2007) Traffic , vol.8 , pp. 16301643
    • Liu, S.1    Wilson, K.A.2    Rice-Stitt, T.3    Neiman, A.M.4    McNew, J.A.5
  • 40
    • 0033635117 scopus 로고    scopus 로고
    • Dual requirement for rho and protein kinase C in direct activation of phospholipase D1 through G protein-coupled receptor signaling
    • Du G, Altshuller YM, Kim Y, Han JM, Ryu SH, Morris AJ, Frohman MA. 2000. Dual requirement for rho and protein kinase C in direct activation of phospholipase D1 through G protein-coupled receptor signaling. Mol. Biol. Cell 11:4359-4368. http://dx.doi.org/10.1091/mbc.11.12.4359.
    • (2000) Mol. Biol. Cell , vol.11 , pp. 43594368
    • Du, G.1    Altshuller, Y.M.2    Kim, Y.3    Han, J.M.4    Ryu, S.H.5    Morris, A.J.6    Frohman, M.A.7
  • 41
    • 0034604717 scopus 로고    scopus 로고
    • The recruitment of Raf-1 to membranes is mediated by direct interaction with phosphatidic acid and is independent of association with Ras
    • Rizzo MA, Shome K, Watkins SC, Romero G. 2000. The recruitment of Raf-1 to membranes is mediated by direct interaction with phosphatidic acid and is independent of association with Ras. J. Biol. Chem. 275:23911-23918. http://dx.doi.org/10.1074/jbc. M001553200.
    • (2000) J. Biol. Chem. , vol.275 , pp. 2391123918
    • Rizzo, M.A.1    Shome, K.2    Watkins, S.C.3    Romero, G.4
  • 42
    • 23644455714 scopus 로고    scopus 로고
    • Phospholipase D: a lipid centric review
    • Jenkins GM, Frohman MA. 2005. Phospholipase D: a lipid centric review. Cell. Mol. Life Sci. 62:2305-2316. http://dx.doi.org/10.1007/s00018-005-5195-z.
    • (2005) Cell. Mol. Life Sci. , vol.62 , pp. 23052316
    • Jenkins, G.M.1    Frohman, M.A.2
  • 43
    • 0031105873 scopus 로고    scopus 로고
    • Phospholipase D2, a distinct phospholipase D isoform with novel regulatory properties that provokes cytoskeletal reorganization
    • Colley WC, Sung TC, Roll R, Jenco J, Hammond SM, Altshuller Y, Bar-Sagi D, Morris AJ, Frohman MA. 1997. Phospholipase D2, a distinct phospholipase D isoform with novel regulatory properties that provokes cytoskeletal reorganization. Curr. Biol. 7:191-201. http://dx.doi.org/10.1016/S0960-9822(97)70090-3.
    • (1997) Curr. Biol. , vol.7 , pp. 191201
    • Colley, W.C.1    Sung, T.C.2    Roll, R.3    Jenco, J.4    Hammond, S.M.5    Altshuller, Y.6    Bar-Sagi, D.7    Morris, A.J.8    Frohman, M.A.9
  • 44
    • 0035976615 scopus 로고    scopus 로고
    • Phosphatidic acid-mediated mitogenic activation ofmTORsignaling
    • Fang Y, Vilella-Bach M, Bachmann R, Flanigan A, Chen J. 2001. Phosphatidic acid-mediated mitogenic activation ofmTORsignaling. Science 294:1942-1945. http://dx.doi.org/10.1126/science.1066015.
    • (2001) Science , vol.294 , pp. 19421945
    • Fang, Y.1    Vilella-Bach, M.2    Bachmann, R.3    Flanigan, A.4    Chen, J.5
  • 46
    • 84867815687 scopus 로고    scopus 로고
    • Novel model for basaloid triple-negative breast cancer: behavior in vivo and response to therapy
    • Volk-Draper LD, Rajput S, Hall KL, Wilber A, Ran S. 2012. Novel model for basaloid triple-negative breast cancer: behavior in vivo and response to therapy. Neoplasia 14:926-942. http://dx.doi.org/10.1593/neo.12956.
    • (2012) Neoplasia , vol.14 , pp. 926-942
    • Volk-Draper, L.D.1    Rajput, S.2    Hall, K.L.3    Wilber, A.4    Ran, S.5
  • 47
    • 79960015997 scopus 로고    scopus 로고
    • Identification of human triple-negative breast cancer subtypes and preclinical models for selection of targeted therapies
    • Lehmann BD, Bauer JA, Chen X, Sanders ME, Chakravarthy AB, Shyr Y, Pietenpol JA. 2011. Identification of human triple-negative breast cancer subtypes and preclinical models for selection of targeted therapies. J. Clin. Invest. 121:2750-2767. http://dx.doi.org/10.1172/JCI45014.
    • (2011) J. Clin. Invest. , vol.121 , pp. 2750-2767
    • Lehmann, B.D.1    Bauer, J.A.2    Chen, X.3    Sanders, M.E.4    Chakravarthy, A.B.5    Shyr, Y.6    Pietenpol, J.A.7
  • 48
    • 0033544953 scopus 로고    scopus 로고
    • Dynamin is required for the activation of mitogen-activated protein (MAP) kinase by MAP kinase kinase
    • Kranenburg O, Verlaan I, Moolenaar WH. 1999. Dynamin is required for the activation of mitogen-activated protein (MAP) kinase by MAP kinase kinase. J. Biol. Chem. 274:35301-35304. http://dx.doi.org/10.1074/jbc.274.50.35301.
    • (1999) J. Biol. Chem. , vol.274 , pp. 35301-35304
    • Kranenburg, O.1    Verlaan, I.2    Moolenaar, W.H.3
  • 49
    • 0030461226 scopus 로고    scopus 로고
    • Control of EGF receptor signaling by clathrin-mediated endocytosis
    • Vieira AV, Lamaze C, Schmid SL. 1996. Control of EGF receptor signaling by clathrin-mediated endocytosis. Science 274:2086-2089. http://dx.doi.org/10.1126/science.274.5295.2086.
    • (1996) Science , vol.274 , pp. 2086-2089
    • Vieira, A.V.1    Lamaze, C.2    Schmid, S.L.3
  • 50
    • 0035159121 scopus 로고    scopus 로고
    • Role for phospholipase D in receptormediated endocytosis
    • Shen Y, Xu L, Foster DA. 2001. Role for phospholipase D in receptormediated endocytosis. Mol. Cell. Biol. 21:595-602. http://dx.doi.org/10.1128/MCB.21.2.595-602.2001.
    • (2001) Mol. Cell. Biol. , vol.21 , pp. 595-602
    • Shen, Y.1    Xu, L.2    Foster, D.A.3
  • 51
    • 0029125757 scopus 로고
    • Integration of MAP kinase signal transduction pathways at the serum response element
    • Whitmarsh AJ, Shore P, Sharrocks AD, Davis RJ. 1995. Integration of MAP kinase signal transduction pathways at the serum response element. Science 269:403-407. http://dx.doi.org/10.1126/science.7618106.
    • (1995) Science , vol.269 , pp. 403-407
    • Whitmarsh, A.J.1    Shore, P.2    Sharrocks, A.D.3    Davis, R.J.4
  • 52
    • 0036051342 scopus 로고    scopus 로고
    • Molecular interpretation of ERK signal duration by immediate early gene products
    • Murphy LO, Smith S, Chen RH, Fingar DC, Blenis J. 2002. Molecular interpretation of ERK signal duration by immediate early gene products. Nat. Cell Biol. 4:556-564. http://dx.doi.org/10.1038/ncb822.
    • (2002) Nat. Cell Biol. , vol.4 , pp. 556-564
    • Murphy, L.O.1    Smith, S.2    Chen, R.H.3    Fingar, D.C.4    Blenis, J.5
  • 53
    • 0028787249 scopus 로고
    • The Mos/MAP kinase pathway stabilizes c-Fos by phosphorylation and augments its transforming activity in NIH 3T3 cells
    • Okazaki K, Sagata N. 1995. The Mos/MAP kinase pathway stabilizes c-Fos by phosphorylation and augments its transforming activity in NIH 3T3 cells. EMBO J. 14:5048-5059.
    • (1995) EMBO J , vol.14 , pp. 5048-5059
    • Okazaki, K.1    Sagata, N.2
  • 54
    • 34347345040 scopus 로고    scopus 로고
    • Ubiquitin-independent proteasomal degradation of Fra-1 is antagonized by Erk1/2 pathway-mediated phosphorylation of a unique C-terminal destabilizer
    • Basbous J, Chalbos D, Hipskind R, Jariel-Encontre I, Piechaczyk M. 2007. Ubiquitin-independent proteasomal degradation of Fra-1 is antagonized by Erk1/2 pathway-mediated phosphorylation of a unique C-terminal destabilizer. Mol. Cell. Biol. 27:3936-3950. http://dx.doi.org/10.1128/MCB.01776-06.
    • (2007) Mol. Cell. Biol. , vol.27 , pp. 3936-3950
    • Basbous, J.1    Chalbos, D.2    Hipskind, R.3    Jariel-Encontre, I.4    Piechaczyk, M.5
  • 55
    • 78149273391 scopus 로고    scopus 로고
    • Heterogeneity of phosphatidic acid levels and distribution at the plasma membrane in living cells as visualized by a Foster resonance energy transfer (FRET) biosensor
    • Nishioka T, Frohman MA, Matsuda M, Kiyokawa E. 2010. Heterogeneity of phosphatidic acid levels and distribution at the plasma membrane in living cells as visualized by a Foster resonance energy transfer (FRET) biosensor. J. Biol. Chem. 285:35979-35987. http://dx.doi.org/10.1074/jbc. M110.153007.
    • (2010) J. Biol. Chem. , vol.285 , pp. 35979-35987
    • Nishioka, T.1    Frohman, M.A.2    Matsuda, M.3    Kiyokawa, E.4
  • 56
    • 77955289201 scopus 로고    scopus 로고
    • Epidermal growth factor receptor activation remodels the plasma membrane lipid environment to induce nanocluster formation
    • Ariotti N, Liang H, Xu Y, Zhang Y, Yonekubo Y, Inder K, Du G, Parton RG, Hancock JF, Plowman SJ. 2010. Epidermal growth factor receptor activation remodels the plasma membrane lipid environment to induce nanocluster formation. Mol. Cell. Biol. 30:3795-3804. http://dx.doi.org/10.1128/MCB.01615-09.
    • (2010) Mol. Cell. Biol. , vol.30 , pp. 3795-3804
    • Ariotti, N.1    Liang, H.2    Xu, Y.3    Zhang, Y.4    Yonekubo, Y.5    Inder, K.6    Du, G.7    Parton, R.G.8    Hancock, J.F.9    Plowman, S.J.10
  • 58
    • 33745801153 scopus 로고    scopus 로고
    • Lipid rafts: contentious only from simplistic standpoints
    • Hancock JF. 2006. Lipid rafts: contentious only from simplistic standpoints. Nat. Rev. Mol. Cell Biol. 7:456-462. http://dx.doi.org/10.1038/nrm1925.
    • (2006) Nat. Rev. Mol. Cell Biol. , vol.7 , pp. 456-462
    • Hancock, J.F.1
  • 59
    • 48449092211 scopus 로고    scopus 로고
    • Using plasma membrane nanoclusters to build better signaling circuits
    • Harding AS, Hancock JF. 2008. Using plasma membrane nanoclusters to build better signaling circuits. Trends Cell Biol. 18:364-371. http://dx.doi.org/10.1016/j.tcb.2008.05.006.
    • (2008) Trends Cell Biol , vol.18 , pp. 364-371
    • Harding, A.S.1    Hancock, J.F.2
  • 60
    • 84858796808 scopus 로고    scopus 로고
    • Ras trafficking, localization and compartmentalized signalling
    • Prior IA, Hancock JF. 2012. Ras trafficking, localization and compartmentalized signalling. Semin. Cell Dev. Biol. 23:145-153. http://dx.doi.org/10.1016/j.semcdb.2011.09.002.
    • (2012) Semin. Cell Dev. Biol. , vol.23 , pp. 145-153
    • Prior, I.A.1    Hancock, J.F.2
  • 61
    • 33644856168 scopus 로고    scopus 로고
    • Distinct utilization of effectors and biological outcomes resulting from site-specific Ras activation: Ras functions in lipid rafts and Golgi complex are dispensable for proliferation and transformation
    • Matallanas D, Sanz-Moreno V, Arozarena I, Calvo F, Agudo-Ibanez L, Santos E, Berciano MT, Crespo P. 2006. Distinct utilization of effectors and biological outcomes resulting from site-specific Ras activation: Ras functions in lipid rafts and Golgi complex are dispensable for proliferation and transformation. Mol. Cell. Biol. 26:100-116. http://dx.doi.org/10.1128/MCB.26.1.100-116.2006.
    • (2006) Mol. Cell. Biol. , vol.26 , pp. 100-116
    • Matallanas, D.1    Sanz-Moreno, V.2    Arozarena, I.3    Calvo, F.4    Agudo-Ibanez, L.5    Santos, E.6    Berciano, M.T.7    Crespo, P.8
  • 62
    • 79952263402 scopus 로고    scopus 로고
    • Compartmentalized Ras proteins transform NIH 3T3 cells with different efficiencies
    • Cheng CM, Li H, Gasman S, Huang J, SchiffR, Chang EC. 2011. Compartmentalized Ras proteins transform NIH 3T3 cells with different efficiencies. Mol. Cell. Biol. 31:983-997. http://dx.doi.org/10.1128/MCB.00137-10.
    • (2011) Mol. Cell. Biol. , vol.31 , pp. 983-997
    • Cheng, C.M.1    Li, H.2    Gasman, S.3    Huang, J.4    Schiff, R.5    Chang, E.C.6
  • 63
    • 4344682999 scopus 로고    scopus 로고
    • Sef is a spatial regulator for Ras/MAP kinase signaling
    • Torii S, Kusakabe M, Yamamoto T, Maekawa M, Nishida E. 2004. Sef is a spatial regulator for Ras/MAP kinase signaling. Dev. Cell 7:33-44. http://dx.doi.org/10.1016/j.devcel.2004.05.019.
    • (2004) Dev. Cell , vol.7 , pp. 33-44
    • Torii, S.1    Kusakabe, M.2    Yamamoto, T.3    Maekawa, M.4    Nishida, E.5
  • 64
    • 27644575157 scopus 로고    scopus 로고
    • Coordinating ERK/MAPK signalling through scaffolds and inhibitors
    • Kolch W. 2005. Coordinating ERK/MAPK signalling through scaffolds and inhibitors. Nat. Rev. Mol. Cell Biol. 6:827-837. http://dx.doi.org/10.1038/nrm1743.
    • (2005) Nat. Rev. Mol. Cell Biol. , vol.6 , pp. 827-837
    • Kolch, W.1
  • 65
    • 61349129180 scopus 로고    scopus 로고
    • Role of phosphatidic acid in the coupling of the ERK cascade
    • Kraft CA, Garrido JL, Fluharty E, Leiva-Vega L, Romero G. 2008. Role of phosphatidic acid in the coupling of the ERK cascade. J. Biol. Chem. 283:36636-36645. http://dx.doi.org/10.1074/jbc. M804633200.
    • (2008) J. Biol. Chem. , vol.283 , pp. 36636-36645
    • Kraft, C.A.1    Garrido, J.L.2    Fluharty, E.3    Leiva-Vega, L.4    Romero, G.5
  • 66
    • 0034695165 scopus 로고    scopus 로고
    • Overexpression of phospholipase D1 in human breast cancer tissues
    • Noh D, Ahn S, Lee R, Park I, Kim J, Suh P, Ryu S, Lee K, Han J. 2000. Overexpression of phospholipase D1 in human breast cancer tissues. Cancer Lett. 161:207-214. http://dx.doi.org/10.1016/S0304-3835(00)00612-1.
    • (2000) Cancer Lett , vol.161 , pp. 207-214
    • Noh, D.1    Ahn, S.2    Lee, R.3    Park, I.4    Kim, J.5    Suh, P.6    Ryu, S.7    Lee, K.8    Han, J.9
  • 67
    • 0032945387 scopus 로고    scopus 로고
    • Phospholipase D activity in human gastric carcinoma
    • Uchida N, Okamura S, Kuwano H. 1999. Phospholipase D activity in human gastric carcinoma. Anticancer Res. 19:671-675.
    • (1999) Anticancer Res , vol.19 , pp. 671-675
    • Uchida, N.1    Okamura, S.2    Kuwano, H.3
  • 71
    • 38449089669 scopus 로고    scopus 로고
    • Expression of phospholipase D2 in human colorectal carcinoma
    • Saito M, Iwadate M, Higashimoto M, Ono K, Takebayashi Y, Takenoshita S. 2007. Expression of phospholipase D2 in human colorectal carcinoma. Oncol. Rep. 18:1329-1334. http://www.spandidos-publications.com/or/18/5/1329/download.
    • (2007) Oncol. Rep. , vol.18 , pp. 1329-1334
    • Saito, M.1    Iwadate, M.2    Higashimoto, M.3    Ono, K.4    Takebayashi, Y.5    Takenoshita, S.6
  • 72
    • 33744943819 scopus 로고    scopus 로고
    • Phospholipase D couples survival and migration signals in stress response of human cancer cells
    • Zheng Y, Rodrik V, Toschi A, Shi M, Hui L, Shen Y, Foster DA. 2006. Phospholipase D couples survival and migration signals in stress response of human cancer cells. J. Biol. Chem. 281:15862-15868. http://dx.doi.org/10.1074/jbc. M600660200.
    • (2006) J. Biol. Chem. , vol.281 , pp. 15862-15868
    • Zheng, Y.1    Rodrik, V.2    Toschi, A.3    Shi, M.4    Hui, L.5    Shen, Y.6    Foster, D.A.7
  • 74
    • 37249034085 scopus 로고    scopus 로고
    • Suppression of TGF-beta signaling by phospholipase D
    • Gadir N, Lee E, Garcia A, Toschi A, Foster DA. 2007. Suppression of TGF-beta signaling by phospholipase D. Cell Cycle 6:2840-2845. http://dx.doi.org/10.4161/cc.6.22.4921.
    • (2007) Cell Cycle , vol.6 , pp. 2840-2845
    • Gadir, N.1    Lee, E.2    Garcia, A.3    Toschi, A.4    Foster, D.A.5
  • 75
    • 36048979906 scopus 로고    scopus 로고
    • Phospholipase D provides a survival signal in human cancer cells with activated H-Ras or K-Ras
    • Shi M, Zheng Y, Garcia A, Xu L, Foster DA. 2007. Phospholipase D provides a survival signal in human cancer cells with activated H-Ras or K-Ras. Cancer Lett. 258:268-275. http://dx.doi.org/10.1016/j.canlet.2007.09.003.
    • (2007) Cancer Lett , vol.258 , pp. 268-275
    • Shi, M.1    Zheng, Y.2    Garcia, A.3    Xu, L.4    Foster, D.A.5
  • 76
    • 0038339003 scopus 로고    scopus 로고
    • Phospholipase D confers rapamycin resistance in human breast cancer cells
    • Chen Y, Zheng Y, Foster DA. 2003. Phospholipase D confers rapamycin resistance in human breast cancer cells. Oncogene 22:3937-3942. http://dx.doi.org/10.1038/sj.onc.1206565.
    • (2003) Oncogene , vol.22 , pp. 3937-3942
    • Chen, Y.1    Zheng, Y.2    Foster, D.A.3
  • 77
    • 0034053818 scopus 로고    scopus 로고
    • Changes in phospholipase D isoform activity and expression in multidrug-resistant human cancer cells
    • Fiucci G, Czarny M, Lavie Y, Zhao D, Berse B, Blusztajn JK, Liscovitch M. 2000. Changes in phospholipase D isoform activity and expression in multidrug-resistant human cancer cells. Int. J. Cancer 85:882-888. http://onlinelibrary.wiley.com/doi/10.1002/(SICI)1097-0215(20000315)85:6 %3C882::AID-IJC24%3E3.0.CO;2-E/full.
    • (2000) Int. J. Cancer , vol.85 , pp. 882-888
    • Fiucci, G.1    Czarny, M.2    Lavie, Y.3    Zhao, D.4    Berse, B.5    Blusztajn, J.K.6    Liscovitch, M.7
  • 79
    • 68949103681 scopus 로고    scopus 로고
    • Phosphatidic acid signaling to mTOR: signals for the survival of human cancer cells
    • Foster DA. 2009. Phosphatidic acid signaling to mTOR: signals for the survival of human cancer cells. Biochim. Biophys. Acta 1791:949-955. http://dx.doi.org/10.1016/j.bbalip.2009.02.009.
    • (2009) Biochim. Biophys. Acta , vol.1791 , pp. 949-955
    • Foster, D.A.1
  • 80
    • 68949157098 scopus 로고    scopus 로고
    • Inter-regulatory dynamics of phospholipase D and the actin cytoskeleton
    • Rudge SA, Wakelam MJ. 2009. Inter-regulatory dynamics of phospholipase D and the actin cytoskeleton. Biochim. Biophys. Acta 1791:856-861. http://dx.doi.org/10.1016/j.bbalip.2009.04.008.
    • (2009) Biochim. Biophys. Acta , vol.1791 , pp. 856-861
    • Rudge, S.A.1    Wakelam, M.J.2


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