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Volumn 289, Issue 3, 2014, Pages 1551-1563

The role of diacylglycerol kinase ζ and phosphatidic acid in the mechanical activation of mammalian target of rapamycin (mTOR) signaling and skeletal muscle hypertrophy

Author keywords

[No Author keywords available]

Indexed keywords

DIACYLGLYCEROL KINASE; FUNDAMENTAL COMPONENT; MAMMALIAN TARGET; MAMMALIAN TARGET OF RAPAMYCIN (MTOR); MECHANICAL ACTIVATION; MECHANICAL STIMULATION; MECHANICAL STIMULUS; PHOSPHATIDIC ACIDS;

EID: 84892657844     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M113.531392     Document Type: Article
Times cited : (123)

References (56)
  • 1
    • 79952970526 scopus 로고    scopus 로고
    • Strength training as a countermeasure to aging muscle and chronic disease
    • Hurley, B. F., Hanson, E. D., and Sheaff, A. K. (2011) Strength training as a countermeasure to aging muscle and chronic disease. Sports Med. 41, 289-306
    • (2011) Sports Med. , vol.41 , pp. 289-306
    • Hurley, B.F.1    Hanson, E.D.2    Sheaff, A.K.3
  • 4
    • 79960925868 scopus 로고    scopus 로고
    • Mechanotransduction and the regulation of mTORC1 signaling in skeletal muscle
    • Hornberger, T. A. (2011) Mechanotransduction and the regulation of mTORC1 signaling in skeletal muscle. Int. J. Biochem. Cell Biol. 43, 1267-1276
    • (2011) Int. J. Biochem. Cell Biol. , vol.43 , pp. 1267-1276
    • Hornberger, T.A.1
  • 5
    • 0034980336 scopus 로고    scopus 로고
    • Comparison of five retrovirus vectors containing the human IL-2 receptor γ chain gene for their ability to restore T and B lymphocytes in the X-linked severe combined immunodeficiency mouse model
    • DOI 10.1006/mthe.2001.0292
    • Avilés Mendoza, G. J., Seidel, N. E., Otsu, M., Anderson, S. M., Simon-Stoos, K., Herrera, A., Hoogstraten-Miller, S., Malech, H. L., Candotti, F., Puck, J. M., and Bodine, D. M. (2001) Comparison of five retrovirus vectors containing the human IL-2 receptor γ chain gene for their ability to restore T and B lymphocytes in the X-linked severe combined immunodeficiency mouse model. Mol. Ther. 3, 565-573 (Pubitemid 32509851)
    • (2001) Molecular Therapy , vol.3 , Issue.4 , pp. 565-573
    • Aviles Mendoza, G.J.1    Seidel, N.E.2    Otsu, M.3    Anderson, S.M.4    Simon-Stoos, K.5    Herrera, A.6    Hoogstraten-Miller, S.7    Malech, H.L.8    Candotti, F.9    Puck, J.M.10    Bodine, D.M.11
  • 6
    • 77956677109 scopus 로고    scopus 로고
    • Aphosphatidylinositol 3-kinase/ protein kinase B-independent activation of mammalian target of rapamycin signaling is sufficient to induce skeletal muscle hypertrophy
    • Goodman, C. A., Miu, M. H., Frey, J. W., Mabrey, D. M., Lincoln, H. C., Ge, Y., Chen, J., and Hornberger, T. A. (2010) Aphosphatidylinositol 3-kinase/ protein kinase B-independent activation of mammalian target of rapamycin signaling is sufficient to induce skeletal muscle hypertrophy. Mol. Biol. Cell 21, 3258-3268
    • (2010) Mol. Biol. Cell , vol.21 , pp. 3258-3268
    • Goodman, C.A.1    Miu, M.H.2    Frey, J.W.3    Mabrey, D.M.4    Lincoln, H.C.5    Ge, Y.6    Chen, J.7    Hornberger, T.A.8
  • 7
    • 3042820402 scopus 로고    scopus 로고
    • Mechanical stimuli regulate rapamycin-sensitive signalling by a phosphoinositide 3-kinase-, protein kinase B- and growth factor-independent mechanism
    • DOI 10.1042/BJ20040274
    • Hornberger, T. A., Stuppard, R., Conley, K. E., Fedele, M. J., Fiorotto, M. L., Chin, E. R., and Esser, K. A. (2004) Mechanical stimuli regulate rapamycin-sensitive signalling by a phosphoinositide 3-kinase-, protein kinase B-, and growth factor-independent mechanism. Biochem. J. 380, 795-804 (Pubitemid 38850521)
    • (2004) Biochemical Journal , vol.380 , Issue.3 , pp. 795-804
    • Hornberger, T.A.1    Stuppard, R.2    Conley, K.E.3    Fedele, M.J.4    Fiorotto, M.L.5    Chin, E.R.6    Esser, K.A.7
  • 8
    • 67651096033 scopus 로고    scopus 로고
    • The role of phosphoinositide 3-kinase and phosphatidic acid in the regulation of mammalian target of rapamycin following eccentric contractions
    • O'Neil, T. K., Duffy, L. R., Frey, J. W., and Hornberger, T. A. (2009) The role of phosphoinositide 3-kinase and phosphatidic acid in the regulation of mammalian target of rapamycin following eccentric contractions. J. Physiol. 587, 3691-3701
    • (2009) J. Physiol. , vol.587 , pp. 3691-3701
    • O'Neil, T.K.1    Duffy, L.R.2    Frey, J.W.3    Hornberger, T.A.4
  • 9
    • 33645659052 scopus 로고    scopus 로고
    • Mechanical stimuli and nutrients regulate rapamycin-sensitive signaling through distinct mechanisms in skeletal muscle
    • Hornberger, T. A., and Chien, S. (2006) Mechanical stimuli and nutrients regulate rapamycin-sensitive signaling through distinct mechanisms in skeletal muscle. J. Cell Biochem. 97, 1207-1216
    • (2006) J. Cell Biochem. , vol.97 , pp. 1207-1216
    • Hornberger, T.A.1    Chien, S.2
  • 10
    • 33645241260 scopus 로고    scopus 로고
    • The role of phospholipase D and phosphatidic acid in the mechanical activation of mTOR signaling in skeletal muscle
    • Hornberger, T. A., Chu, W. K., Mak, Y. W., Hsiung, J. W., Huang, S. A., and Chien, S. (2006) The role of phospholipase D and phosphatidic acid in the mechanical activation of mTOR signaling in skeletal muscle. Proc. Natl. Acad. Sci. U.S.A. 103, 4741-4746
    • (2006) Proc. Natl. Acad. Sci. U.S.A. , vol.103 , pp. 4741-4746
    • Hornberger, T.A.1    Chu, W.K.2    Mak, Y.W.3    Hsiung, J.W.4    Huang, S.A.5    Chien, S.6
  • 11
    • 84867525052 scopus 로고    scopus 로고
    • Mechanical stimulation induces mTOR signaling via an ERK-independent mechanism. Implications for a direct activation of mTOR by phosphatidic acid
    • You, J. S., Frey, J. W., and Hornberger, T. A. (2012) Mechanical stimulation induces mTOR signaling via an ERK-independent mechanism. Implications for a direct activation of mTOR by phosphatidic acid. PloS ONE 7, e47258
    • (2012) PloS ONE , vol.7
    • You, J.S.1    Frey, J.W.2    Hornberger, T.A.3
  • 12
    • 0024434397 scopus 로고
    • Exercise-induced translocation of protein kinase C and production of diacylglycerol and phosphatidic acid in rat skeletal muscle in vivo. Relationship to changes in glucose transport
    • Cleland, P. J., Appleby, G. J., Rattigan, S., and Clark, M. G. (1989) Exerciseinduced translocation of protein kinaseCand production of diacylglycerol and phosphatidic acid in rat skeletal muscle in vivo. Relationship to changes in glucose transport. J. Biol. Chem. 264, 17704-17711 (Pubitemid 19279231)
    • (1989) Journal of Biological Chemistry , vol.264 , Issue.30 , pp. 17704-17711
    • Cleland, P.J.F.1    Appleby, G.J.2    Rattigan, S.3    Clark, M.G.4
  • 13
    • 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., Sun, Y., Arauz, E., Jiang, Y., and Chen, J. (2011) 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. 286, 29568-29574
    • (2011) J. Biol. Chem. , vol.286 , pp. 29568-29574
    • Yoon, M.S.1    Sun, Y.2    Arauz, E.3    Jiang, Y.4    Chen, J.5
  • 14
    • 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
    • DOI 10.1038/sj.onc.1210693, PII 1210693
    • Veverka, V., Crabbe, T., Bird, I., Lennie, G., Muskett, F. W., Taylor, R. J., and Carr, M. D. (2008) 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 27, 585-595 (Pubitemid 351158903)
    • (2008) Oncogene , vol.27 , Issue.5 , pp. 585-595
    • Veverka, V.1    Crabbe, T.2    Bird, I.3    Lennie, G.4    Muskett, F.W.5    Taylor, R.J.6    Carr, M.D.7
  • 15
    • 0029055145 scopus 로고
    • Identification of an 11-kDa FKBP12-rapamycin-binding domain within the 289- kDa FKBP12-rapamycin-associated protein and characterization of a critical serine residue
    • Chen, J., Zheng, X. F., Brown, E. J., and Schreiber, S. L. (1995) Identification of an 11-kDa FKBP12-rapamycin-binding domain within the 289- kDa FKBP12-rapamycin-associated protein and characterization of a critical serine residue. Proc. Natl. Acad. Sci. U.S.A. 92, 4947-4951
    • (1995) Proc. Natl. Acad. Sci. U.S.A. , vol.92 , pp. 4947-4951
    • Chen, J.1    Zheng, X.F.2    Brown, E.J.3    Schreiber, S.L.4
  • 16
    • 77953091045 scopus 로고    scopus 로고
    • Structure of the human mTOR complex i and its implications for rapamycin inhibition
    • Yip, C. K., Murata, K., Walz, T., Sabatini, D. M., and Kang, S. A. (2010) Structure of the human mTOR complex I and its implications for rapamycin inhibition. Mol. Cell 38, 768-774
    • (2010) Mol. Cell , vol.38 , pp. 768-774
    • Yip, C.K.1    Murata, K.2    Walz, T.3    Sabatini, D.M.4    Kang, S.A.5
  • 17
    • 62849111751 scopus 로고    scopus 로고
    • Regulation ofmTORC1andmTORC2complex assembly by phosphatidic acid. Competition with rapamycin
    • Toschi, A., Lee, E., Xu, L., Garcia, A., Gadir, N., and Foster, D. A. (2009) Regulation ofmTORC1andmTORC2complex assembly by phosphatidic acid. Competition with rapamycin. Mol. Cell. Biol. 29, 1411-1420
    • (2009) Mol. Cell. Biol. , vol.29 , pp. 1411-1420
    • Toschi, A.1    Lee, E.2    Xu, L.3    Garcia, A.4    Gadir, N.5    Foster, D.A.6
  • 18
    • 0035976615 scopus 로고    scopus 로고
    • Phosphatidic acid-mediated mitogenic activation of mTOR signaling
    • DOI 10.1126/science.1066015
    • Fang, Y., Vilella-Bach, M., Bachmann, R., Flanigan, A., and Chen, J. (2001) Phosphatidic acid-mediated mitogenic activation of mTOR signaling. Science 294, 1942-1945 (Pubitemid 33101594)
    • (2001) Science , vol.294 , Issue.5548 , pp. 1942-1945
    • Fang, Y.1    Vilella-Bach, M.2    Bachmann, R.3    Flanigan, A.4    Chen, J.5
  • 19
    • 62149152761 scopus 로고    scopus 로고
    • 5-Fluoro-2-indolyl deschlorohalopemide (FIPI), a phospholipase D pharmacological inhibitor that alters cell spreading and inhibits chemotaxis
    • Su, W., Yeku, O., Olepu, S., Genna, A., Park, J. S., Ren, H., Du, G., Gelb, M. H., Morris, A. J., and Frohman, M. A. (2009) 5-Fluoro-2-indolyl deschlorohalopemide (FIPI), a phospholipase D pharmacological inhibitor that alters cell spreading and inhibits chemotaxis. Mol. Pharmacol. 75, 437-446
    • (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
  • 20
    • 72449211906 scopus 로고    scopus 로고
    • Reversible bleb formation in mast cells stimulated with antigen is Ca2+/calmodulin-dependent and bleb size is regulated by ARF6
    • Yanase, Y., Carvou, N., Frohman, M. A., and Cockcroft, S. (2010) Reversible bleb formation in mast cells stimulated with antigen is Ca2+/calmodulin-dependent and bleb size is regulated by ARF6. Biochem. J. 425, 179-193
    • (2010) Biochem. J. , vol.425 , pp. 179-193
    • Yanase, Y.1    Carvou, N.2    Frohman, M.A.3    Cockcroft, S.4
  • 21
    • 84871887002 scopus 로고    scopus 로고
    • Molecular mechanisms of N-formyl-methionyl-leucyl-phenylalanine-induced superoxide generation and degranulation in mouse neutrophils. Phospholipase D is dispensable
    • Sato, T., Hongu, T., Sakamoto, M., Funakoshi, Y., and Kanaho, Y. (2013) Molecular mechanisms of N-formyl-methionyl-leucyl-phenylalanine-induced superoxide generation and degranulation in mouse neutrophils. Phospholipase D is dispensable. Mol. Cell. Biol. 33, 136-145
    • (2013) Mol. Cell. Biol. , vol.33 , pp. 136-145
    • Sato, T.1    Hongu, T.2    Sakamoto, M.3    Funakoshi, Y.4    Kanaho, Y.5
  • 22
    • 0032514484 scopus 로고    scopus 로고
    • Protein kinase C regulates the nuclear localization of diacylglycerol kinase-ζ
    • DOI 10.1038/29337
    • Topham, M. K., Bunting, M., Zimmerman, G. A., McIntyre, T. M., Blackshear, P. J., and Prescott, S. M. (1998) Protein kinase C regulates the nuclear localization of diacylglycerol kinase-ζ. Nature 394, 697-700 (Pubitemid 28389799)
    • (1998) Nature , vol.394 , Issue.6694 , pp. 697-700
    • Topham, M.K.1    Bunting, M.2    Zimmerman, G.A.3    McIntyre, T.M.4    Blackshear, P.J.5    Prescott, S.M.6
  • 24
    • 84884254389 scopus 로고    scopus 로고
    • Eccentric contractions increase the phosphorylation of tuberous sclerosis complex-2 (TSC2) and alter the targeting of TSC2 and the mechanistic target of rapamycin to the lysosome
    • Jacobs, B. L., You, J. S., Frey, J. W., Goodman, C. A., Gundermann, D. M., and Hornberger, T. A. (2013) Eccentric contractions increase the phosphorylation of tuberous sclerosis complex-2 (TSC2) and alter the targeting of TSC2 and the mechanistic target of rapamycin to the lysosome. J. Physiol. 591, 4611-4620
    • (2013) J. Physiol. , vol.591 , pp. 4611-4620
    • Jacobs, B.L.1    You, J.S.2    Frey, J.W.3    Goodman, C.A.4    Gundermann, D.M.5    Hornberger, T.A.6
  • 26
    • 84886444687 scopus 로고    scopus 로고
    • Smad3 induces atrogin-1, inhibits mTOR and protein synthesis, and promotes muscle atrophy in vivo
    • Goodman, C. A., McNally, R. M., Hoffmann, F. M., and Hornberger, T. A. (2013) Smad3 induces atrogin-1, inhibits mTOR and protein synthesis, and promotes muscle atrophy in vivo. Mol. Endocrinol. 27, 1946-1957
    • (2013) Mol. Endocrinol. , vol.27 , pp. 1946-1957
    • Goodman, C.A.1    McNally, R.M.2    Hoffmann, F.M.3    Hornberger, T.A.4
  • 27
    • 84875972792 scopus 로고    scopus 로고
    • Phosphorylation of lipin 1 and charge on the phosphatidic acid head group control its phosphatidic acid phosphatase activity and membrane association
    • Eaton, J. M., Mullins, G. R., Brindley, D. N., and Harris, T. E. (2013) Phosphorylation of lipin 1 and charge on the phosphatidic acid head group control its phosphatidic acid phosphatase activity and membrane association. J. Biol. Chem. 288, 9933-9945
    • (2013) J. Biol. Chem. , vol.288 , pp. 9933-9945
    • Eaton, J.M.1    Mullins, G.R.2    Brindley, D.N.3    Harris, T.E.4
  • 28
    • 33846975789 scopus 로고    scopus 로고
    • Insulin controls subcellular localization and multisite phosphorylation of the phosphatidic acid phosphatase, lipin 1
    • DOI 10.1074/jbc.M609537200
    • Harris, T. E., Huffman, T. A., Chi, A., Shabanowitz, J., Hunt, D. F., Kumar, A., and Lawrence, J. C., Jr. (2007) Insulin controls subcellular localization and multisite phosphorylation of the phosphatidic acid phosphatase, lipin 1. J. Biol. Chem. 282, 277-286 (Pubitemid 47076630)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.1 , pp. 277-286
    • Harris, T.E.1    Huffman, T.A.2    Chi, A.3    Shabanowitz, J.4    Hunt, D.F.5    Kumar, A.6    Lawrence Jr., J.C.7
  • 29
    • 84055178474 scopus 로고    scopus 로고
    • Regulation and function of ribosomal protein S6 kinase (S6K) within mTOR signalling networks
    • Magnuson, B., Ekim, B., and Fingar, D. C. (2012) Regulation and function of ribosomal protein S6 kinase (S6K) within mTOR signalling networks. Biochem. J. 441, 1-21
    • (2012) Biochem. J. , vol.441 , pp. 1-21
    • Magnuson, B.1    Ekim, B.2    Fingar, D.C.3
  • 30
    • 78650510609 scopus 로고    scopus 로고
    • MTOR. from growth signal integration to cancer, diabetes, and ageing
    • Zoncu, R., Efeyan, A., and Sabatini, D. M. (2011) mTOR. From growth signal integration to cancer, diabetes, and ageing. Nat. Rev. Mol. Cell Biol. 12, 21-35
    • (2011) Nat. Rev. Mol. Cell Biol. , vol.12 , pp. 21-35
    • Zoncu, R.1    Efeyan, A.2    Sabatini, D.M.3
  • 31
    • 0037178786 scopus 로고    scopus 로고
    • MTOR interacts with raptor to form a nutrient-sensitive complex that signals to the cell growth machinery
    • DOI 10.1016/S0092-8674(02)00808-5
    • Kim, D. H., Sarbassov, D. D., Ali, S. M., King, J. E., Latek, R. R., Erdjument-Bromage, H., Tempst, P., and Sabatini, D. M. (2002) mTOR interacts with raptor to form a nutrient-sensitive complex that signals to the cell growth machinery. Cell 110, 163-175 (Pubitemid 34876545)
    • (2002) Cell , vol.110 , Issue.2 , pp. 163-175
    • Kim, D.-H.1    Sarbassov, D.D.2    Ali, S.M.3    King, J.E.4    Latek, R.R.5    Erdjument-Bromage, H.6    Tempst, P.7    Sabatini, D.M.8
  • 32
    • 0029993846 scopus 로고    scopus 로고
    • Contribution of phosphoinositides and phosphatidylcholines to the production of phosphatidic acid upon concanavalin A stimulation of rat thymocytes
    • el Bawab, S., Macovschi, O., Thevenon, C., Goncalves, A., Némoz, G., Lagarde, M., and Prigent, A. F. (1996) Contribution of phosphoinositides and phosphatidylcholines to the production of phosphatidic acid upon concanavalin A stimulation of rat thymocytes. J. Lipid Res. 37, 2098-2108 (Pubitemid 26357321)
    • (1996) Journal of Lipid Research , vol.37 , Issue.10 , pp. 2098-2108
    • El Bawab, S.1    Macovschi, O.2    Thevenon, C.3    Goncalves, A.4    Nemoz, G.5    Lagarde, M.6    Prigent, A.-F.7
  • 33
    • 0027521065 scopus 로고
    • Mechanical stretch rapidly activates multiple signal transduction pathways in cardiac myocytes: Potential involvement of an autocrine/paracrine mechanism
    • Sadoshima, J., and Izumo, S. (1993) Mechanical stretch rapidly activates multiple signal transduction pathways in cardiac myocytes. Potential involvement of an autocrine/paracrine mechanism. EMBOJ. 12, 1681-1692 (Pubitemid 23112823)
    • (1993) EMBO Journal , vol.12 , Issue.4 , pp. 1681-1692
    • Sadoshima, J.-I.1    Izumo, S.2
  • 34
    • 0033954192 scopus 로고    scopus 로고
    • Selectivity of the diacylglycerol kinase inhibitor 3-{2-(4-[bis-(4- fluorophenyl)methylene]-1-piperidinyl)ethyl}-2,3-dihydro-2-thioxo-4(1H) quinazolinone (R59949) among diacylglycerol kinase subtypes
    • DOI 10.1016/S0006-2952(99)00395-0, PII S0006295299003950
    • Jiang, Y., Sakane, F., Kanoh, H., and Walsh, J. P. (2000) Selectivity of the diacylglycerol kinase inhibitor 3-[2-(4-[bis-(4-fluorophenyl)methylene]- 1-piperidinyl)ethyl]-2, 3-dihydro-2-thioxo-4(1H)quinazolinone (R59949) among diacylglycerol kinase subtypes. Biochem. Pharmacol. 59, 763-772 (Pubitemid 30081699)
    • (2000) Biochemical Pharmacology , vol.59 , Issue.7 , pp. 763-772
    • Jiang, Y.1    Sakane, F.2    Kanoh, H.3    Walsh, J.P.4
  • 36
    • 0033749209 scopus 로고    scopus 로고
    • Properties and functions of diacylglycerol kinases
    • van Blitterswijk, W. J., and Houssa, B. (2000) Properties and functions of diacylglycerol kinases. Cell. Signal. 12, 595-605
    • (2000) Cell. Signal. , vol.12 , pp. 595-605
    • Van Blitterswijk, W.J.1    Houssa, B.2
  • 37
    • 15444378732 scopus 로고    scopus 로고
    • Modulation of the mammalian target of rapamycin pathway by diacylglycerol kinase-produced phosphatidic acid
    • DOI 10.1074/jbc.M412296200
    • Avila-Flores, A., Santos, T., Rincón, E., and Mérida, I. (2005) Modulation of the mammalian target of rapamycin pathway by diacylglycerol kinaseproduced phosphatidic acid. J. Biol. Chem. 280, 10091-10099 (Pubitemid 40395861)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.11 , pp. 10091-10099
    • Avila-Flores, A.1    Santos, T.2    Rincon, E.3    Merida, I.4
  • 38
    • 79954618943 scopus 로고    scopus 로고
    • Negative regulation of mTOR activation by diacylglycerol kinases
    • Gorentla, B. K., Wan, C. K., and Zhong, X. P. (2011) Negative regulation of mTOR activation by diacylglycerol kinases. Blood 117, 4022-4031
    • (2011) Blood , vol.117 , pp. 4022-4031
    • Gorentla, B.K.1    Wan, C.K.2    Zhong, X.P.3
  • 39
    • 0142070928 scopus 로고    scopus 로고
    • 2+- and phospholipase D-dependent and -independent pathways activate mTOR signaling
    • DOI 10.1016/S0014-5793(03)00816-0
    • Ballou, L. M., Jiang, Y. P., Du, G., Frohman, M. A., and Lin, R. Z. (2003) Ca2+- and phospholipase D-dependent and -independent pathways activate mTOR signaling. FEBS Lett. 550, 51-56 (Pubitemid 37281356)
    • (2003) FEBS Letters , vol.550 , Issue.1-3 , pp. 51-56
    • Ballou, L.M.1    Jiang, Y.-P.2    Du, G.3    Frohman, M.A.4    Lin, R.Z.5
  • 40
    • 40549088524 scopus 로고    scopus 로고
    • PLD regulates myoblast differentiation through the mTOR-IGF2 pathway
    • DOI 10.1242/jcs.022566
    • Yoon, M. S., and Chen, J. (2008) PLD regulates myoblast differentiation through the mTOR-IGF2 pathway. J. Cell Sci. 121, 282-289 (Pubitemid 351356699)
    • (2008) Journal of Cell Science , vol.121 , Issue.3 , pp. 282-289
    • Yoon, M.-S.1    Chen, J.2
  • 41
    • 84855731134 scopus 로고    scopus 로고
    • Class III PI-3-kinase activates phospholipase D in an amino acid-sensing mTORC1 pathway
    • Yoon, M. S., Du, G., Backer, J. M., Frohman, M. A., and Chen, J. (2011) Class III PI-3-kinase activates phospholipase D in an amino acid-sensing mTORC1 pathway. J. Cell Biol. 195, 435-447
    • (2011) J. Cell Biol. , vol.195 , pp. 435-447
    • Yoon, M.S.1    Du, G.2    Backer, J.M.3    Frohman, M.A.4    Chen, J.5
  • 43
    • 77951768486 scopus 로고    scopus 로고
    • Ragulator-Rag complex targets mTORC1 to the lysosomal surface and is necessary for its activation by amino acids
    • Sancak, Y., Bar-Peled, L., Zoncu, R., Markhard, A. L., Nada, S., and Sabatini, D. M. (2010) Ragulator-Rag complex targets mTORC1 to the lysosomal surface and is necessary for its activation by amino acids. Cell 141, 290-303
    • (2010) Cell , vol.141 , pp. 290-303
    • Sancak, Y.1    Bar-Peled, L.2    Zoncu, R.3    Markhard, A.L.4    Nada, S.5    Sabatini, D.M.6
  • 44
    • 18244362311 scopus 로고    scopus 로고
    • Novel role of the small GTPase Rheb: Its implication in endocytic pathway independent of the activation of mammalian target of rapamycin
    • DOI 10.1093/jb/mvi046
    • Saito, K., Araki, Y., Kontani, K., Nishina, H., and Katada, T. (2005) Novel role of the small GTPase Rheb. Its implication in endocytic pathway independent of the activation of mammalian target of rapamycin. J. Biochem. 137, 423-430 (Pubitemid 40628451)
    • (2005) Journal of Biochemistry , vol.137 , Issue.3 , pp. 423-430
    • Saito, K.1    Araki, Y.2    Kontani, K.3    Nishina, H.4    Katada, T.5
  • 45
    • 84899471750 scopus 로고    scopus 로고
    • The mechanical activation ofmTORsignaling.Anemerging role for late endosome/lysosomal targeting
    • doi: 10.1007/s10974-013-9367-4
    • Jacobs, B. L., Goodman, C. A., and Hornberger, T. A. (2013) The mechanical activation ofmTORsignaling.Anemerging role for late endosome/lysosomal targeting. J. Muscle Res. Cell Motil. doi: 10.1007/s10974-013-9367-4
    • (2013) J. Muscle Res. Cell Motil.
    • Jacobs, B.L.1    Goodman, C.A.2    Hornberger, T.A.3
  • 46
    • 84866163429 scopus 로고    scopus 로고
    • Phosphatidic acid mediates the targeting of tBid to induce lysosomal membrane permeabilization and apoptosis
    • Zhao, K., Zhou, H., Zhao, X., Wolff, D. W., Tu, Y., Liu, H., Wei, T., and Yang, F. (2012) Phosphatidic acid mediates the targeting of tBid to induce lysosomal membrane permeabilization and apoptosis. J. Lipid Res. 53, 2102-2114
    • (2012) J. Lipid Res. , vol.53 , pp. 2102-2114
    • Zhao, K.1    Zhou, H.2    Zhao, X.3    Wolff, D.W.4    Tu, Y.5    Liu, H.6    Wei, T.7    Yang, F.8
  • 47
    • 34250665428 scopus 로고    scopus 로고
    • Proteomics identification of sorting nexin 27 as a diacyglycerol kinase ζ-associated protein: New diacylglycerol kinase roles in endocytic recycling
    • DOI 10.1074/mcp.M700047-MCP200
    • Rincón, E., Santos, T., Avila-Flores, A., Albar, J. P., Lalioti, V., Lei, C., Hong, W., and Mérida, I. (2007) Proteomics identification of sorting nexin 27 as a diacylglycerol kinase ζ-associated protein. New diacylglycerol kinase roles in endocytic recycling. Mol. Cell Proteomics 6, 1073-1087 (Pubitemid 47019408)
    • (2007) Molecular and Cellular Proteomics , vol.6 , Issue.6 , pp. 1073-1087
    • Rincon, E.1    Santos, T.2    Avila-Flores, A.3    Albar, J.P.4    Lalioti, V.5    Lei, C.6    Hong, W.7    Merida, I.8
  • 48
    • 33846834013 scopus 로고    scopus 로고
    • Targeting of diacylglycerol degradation to M1 muscarinic receptors by β-arrestins
    • DOI 10.1126/science.1134562
    • Nelson, C. D., Perry, S. J., Regier, D. S., Prescott, S. M., Topham, M. K., and Lefkowitz, R. J. (2007) Targeting of diacylglycerol degradation to M1 muscarinic receptors by β-arrestins. Science 315, 663-666 (Pubitemid 46214713)
    • (2007) Science , vol.315 , Issue.5812 , pp. 663-666
    • Nelson, C.D.1    Perry, S.J.2    Regier, D.S.3    Prescott, S.M.4    Topham, M.K.5    Lefkowitz, R.J.6
  • 50
    • 0038339003 scopus 로고    scopus 로고
    • Phospholipase D confers rapamycin resistance in human breast cancer cells
    • DOI 10.1038/sj.onc.1206565
    • Chen, Y., Zheng, Y., and Foster, D. A. (2003) Phospholipase D confers rapamycin resistance in human breast cancer cells. Oncogene 22, 3937-3942 (Pubitemid 36819667)
    • (2003) Oncogene , vol.22 , Issue.25 , pp. 3937-3942
    • Chen, Y.1    Zheng, Y.2    Foster, D.A.3
  • 51
    • 84879141330 scopus 로고    scopus 로고
    • Cluster analysis reveals differential transcript profiles associated with resistance training-induced human skeletal muscle hypertrophy
    • Thalacker-Mercer, A., Stec, M., Cui, X., Cross, J., Windham, S., and Bamman, M. (2013) Cluster analysis reveals differential transcript profiles associated with resistance training-induced human skeletal muscle hypertrophy. Physiol. Genomics 45, 499-507
    • (2013) Physiol. Genomics , vol.45 , pp. 499-507
    • Thalacker-Mercer, A.1    Stec, M.2    Cui, X.3    Cross, J.4    Windham, S.5    Bamman, M.6
  • 52
    • 33749236816 scopus 로고    scopus 로고
    • Subnuclear localization and differentiation-dependent increased expression of DGK-ζ in C2C12 mouse myoblasts
    • DOI 10.1002/jcp.20744
    • Evangelisti, C., Riccio, M., Faenza, I., Zini, N., Hozumi, Y., Goto, K., Cocco, L., and Martelli, A. M. (2006) Subnuclear localization and differentiationdependent increased expression of DGK-ζ in C2C12 mouse myoblasts. J. Cell Physiol. 209, 370-378 (Pubitemid 44484627)
    • (2006) Journal of Cellular Physiology , vol.209 , Issue.2 , pp. 370-378
    • Evangelisti, C.1    Riccio, M.2    Faenza, I.3    Zini, N.4    Hozumi, Y.5    Goto, K.6    Cocco, L.7    Martelli, A.M.8
  • 53
    • 34250320543 scopus 로고    scopus 로고
    • Morphological changes and spatial regulation of diacylglycerol kinase-ζ, syntrophins, and Rac1 during myoblast fusion
    • DOI 10.1002/cm.20204
    • Abramovici, H., and Gee, S. H. (2007) Morphological changes and spatial regulation of diacylglycerol kinase-ζ, syntrophins, and Rac1 during myoblast fusion. Cell Motil. Cytoskeleton 64, 549-567 (Pubitemid 46919607)
    • (2007) Cell Motility and the Cytoskeleton , vol.64 , Issue.7 , pp. 549-567
    • Abramovici, H.1    Gee, S.H.2
  • 55
    • 77954413330 scopus 로고    scopus 로고
    • Mammalian target of rapamycin regulates miRNA-1 and follistatin in skeletal myogenesis
    • Sun, Y., Ge, Y., Drnevich, J., Zhao, Y., Band, M., and Chen, J. (2010) Mammalian target of rapamycin regulates miRNA-1 and follistatin in skeletal myogenesis. J. Cell Biol. 189, 1157-1169
    • (2010) J. Cell Biol. , vol.189 , pp. 1157-1169
    • Sun, Y.1    Ge, Y.2    Drnevich, J.3    Zhao, Y.4    Band, M.5    Chen, J.6
  • 56
    • 70449158340 scopus 로고
    • A simple method for the isolation and purification of total lipides from animal tissues
    • Folch, J., Lees, M., and Sloane Stanley, G. H. (1957) A simple method for the isolation and purification of total lipides from animal tissues. J. Biol. Chem. 226, 497-509
    • (1957) J. Biol. Chem. , vol.226 , pp. 497-509
    • Folch, J.1    Lees, M.2    Sloane Stanley, G.H.3


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