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Volumn 289, Issue 49, 2014, Pages 34366-34377

Proteinase-activated receptor 2 (PAR2) decreases apoptosis in colonic epithelial cells

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACIDS; CELL DEATH; CHEMICAL ACTIVATION; DISEASE CONTROL;

EID: 84916917407     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M114.610485     Document Type: Article
Times cited : (48)

References (63)
  • 4
    • 4344700784 scopus 로고    scopus 로고
    • Downregulation of epithelial apoptosis and barrier repair in active Crohn's disease by tumour necrosis factor α antibody treatment
    • Zeissig, S., Bojarski, C., Buergel, N., Mankertz, J., Zeitz, M., Fromm, M., and Schulzke, J. D. (2004) Downregulation of epithelial apoptosis and barrier repair in active Crohn's disease by tumour necrosis factor α antibody treatment. Gut 53, 1295-1302
    • (2004) Gut , vol.53 , pp. 1295-1302
    • Zeissig, S.1    Bojarski, C.2    Buergel, N.3    Mankertz, J.4    Zeitz, M.5    Fromm, M.6    Schulzke, J.D.7
  • 6
    • 0035210487 scopus 로고    scopus 로고
    • Epithelial barrier defects in ulcerative colitis: Characterization and quantification by electrophysiological imaging
    • Gitter, A. H., Wullstein, F., Fromm, M., and Schulzke, J. D. (2001) Epithelial barrier defects in ulcerative colitis: characterization and quantification by electrophysiological imaging. Gastroenterology 121, 1320-1328
    • (2001) Gastroenterology , vol.121 , pp. 1320-1328
    • Gitter, A.H.1    Wullstein, F.2    Fromm, M.3    Schulzke, J.D.4
  • 10
    • 0037483705 scopus 로고    scopus 로고
    • Epidermal growth factor enemas with oral mesalamine for mild-to-moderate left-sided ulcerative colitis or proctitis
    • Sinha, A., Nightingale, J., West, K. P., Berlanga-Acosta, J., and Playford, R. J. (2003) Epidermal growth factor enemas with oral mesalamine for mild-to-moderate left-sided ulcerative colitis or proctitis. N. Engl. J. Med. 349, 350-357
    • (2003) N. Engl. J. Med. , vol.349 , pp. 350-357
    • Sinha, A.1    Nightingale, J.2    West, K.P.3    Berlanga-Acosta, J.4    Playford, R.J.5
  • 11
    • 84867027990 scopus 로고    scopus 로고
    • Mucosal healing in inflammatory bowel diseases: A systematic review
    • Neurath, M. F., and Travis, S. P. (2012) Mucosal healing in inflammatory bowel diseases: a systematic review. Gut 61, 1619-1635
    • (2012) Gut , vol.61 , pp. 1619-1635
    • Neurath, M.F.1    Travis, S.P.2
  • 16
    • 0034689003 scopus 로고    scopus 로고
    • β-arrestin-dependent endocytosis of proteinaseactivated receptor 2 is required for intracellular targeting of activated ERK1/2
    • DeFea, K. A., Zalevsky, J., Thoma, M. S., Déry, O., Mullins, R. D., and Bunnett, N. W. (2000) β-Arrestin-dependent endocytosis of proteinaseactivated receptor 2 is required for intracellular targeting of activated ERK1/2. J. Cell Biol. 148, 1267-1281
    • (2000) J. Cell Biol. , vol.148 , pp. 1267-1281
    • Defea, K.A.1    Zalevsky, J.2    Thoma, M.S.3    Déry, O.4    Mullins, R.D.5    Bunnett, N.W.6
  • 17
    • 70349324342 scopus 로고    scopus 로고
    • Agonist-biased signaling via proteinase activated receptor-2: Differential activation of calcium and mitogen- activated protein kinase pathways
    • Ramachandran, R., Mihara, K., Mathur, M., Rochdi, M. D., Bouvier, M., Defea, K., and Hollenberg, M. D. (2009) Agonist-biased signaling via proteinase activated receptor-2: differential activation of calcium and mitogen- activated protein kinase pathways. Mol. Pharmacol. 76, 791-801
    • (2009) Mol. Pharmacol. , vol.76 , pp. 791-801
    • Ramachandran, R.1    Mihara, K.2    Mathur, M.3    Rochdi, M.D.4    Bouvier, M.5    Defea, K.6    Hollenberg, M.D.7
  • 18
    • 2442692682 scopus 로고    scopus 로고
    • Proteaseactivated receptor 2 in colon cancer: Trypsin-induced MAPK phosphorylation and cell proliferation are mediated by epidermal growth factor receptor transactivation
    • Darmoul, D., Gratio, V., Devaud, H., and Laburthe, M. (2004) Proteaseactivated receptor 2 in colon cancer: trypsin-induced MAPK phosphorylation and cell proliferation are mediated by epidermal growth factor receptor transactivation. J. Biol. Chem. 279, 20927-20934
    • (2004) J. Biol. Chem. , vol.279 , pp. 20927-20934
    • Darmoul, D.1    Gratio, V.2    Devaud, H.3    Laburthe, M.4
  • 19
    • 36749006304 scopus 로고    scopus 로고
    • Differential regulation of class IA phosphoinositide 3-kinase catalytic subunits p110 α and β by protease-activated receptor 2 and β-arrestins
    • Wang, P., Kumar, P., Wang, C., and Defea, K. A. (2007) Differential regulation of class IA phosphoinositide 3-kinase catalytic subunits p110 α and β by protease-activated receptor 2 and β-arrestins. Biochem. J. 408, 221-230
    • (2007) Biochem. J. , vol.408 , pp. 221-230
    • Wang, P.1    Kumar, P.2    Wang, C.3    Defea, K.A.4
  • 20
    • 0039843091 scopus 로고    scopus 로고
    • Trafficking of proteinase-activated receptor-2 and β-arrestin-1 tagged with green fluorescent protein. β-Arrestin-dependent endocytosis of a proteinase receptor
    • Déry, O., Thoma, M. S., Wong, H., Grady, E. F., and Bunnett, N. W. (1999) Trafficking of proteinase-activated receptor-2 and β-arrestin-1 tagged with green fluorescent protein. β-Arrestin-dependent endocytosis of a proteinase receptor. J. Biol. Chem. 274, 18524-18535
    • (1999) J. Biol. Chem. , vol.274 , pp. 18524-18535
    • Déry, O.1    Thoma, M.S.2    Wong, H.3    Grady, E.F.4    Bunnett, N.W.5
  • 21
    • 84863514051 scopus 로고    scopus 로고
    • Epidermal growth factor receptor transactivation is required for proteinase-activated receptor-2-induced COX-2 expression in intestinal epithelial cells
    • Hirota, C. L., Moreau, F., Iablokov, V., Dicay, M., Renaux, B., Hollenberg, M. D., and MacNaughton, W. K. (2012) Epidermal growth factor receptor transactivation is required for proteinase-activated receptor-2-induced COX-2 expression in intestinal epithelial cells. Am. J. Physiol. Gastrointest. Liver Physiol. 303, G111-G119
    • (2012) Am. J. Physiol. Gastrointest. Liver Physiol. , vol.303 , pp. G111-G119
    • Hirota, C.L.1    Moreau, F.2    Iablokov, V.3    Dicay, M.4    Renaux, B.5    Hollenberg, M.D.6    Macnaughton, W.K.7
  • 22
    • 84863205849 scopus 로고    scopus 로고
    • NIH Image to Image J: 25 years of image analysis
    • Schneider, C. A., Rasband, W. S., and Eliceiri, K. W. (2012) NIH Image to Image J: 25 years of image analysis. Nat. Methods 9, 671-675
    • (2012) Nat. Methods , vol.9 , pp. 671-675
    • Schneider, C.A.1    Rasband, W.S.2    Eliceiri, K.W.3
  • 23
    • 84900328188 scopus 로고    scopus 로고
    • Evaluating strategies to normalise biological replicates of Western blot data
    • Degasperi, A., Birtwistle, M. R., Volinsky, N., and Rauch, J. (2014) Evaluating strategies to normalise biological replicates of Western blot data. PLoS One 10.1371/journal.pone.0087293
    • (2014) PLoS One
    • Degasperi, A.1    Birtwistle, M.R.2    Volinsky, N.3    Rauch, J.4
  • 24
    • 44949231424 scopus 로고    scopus 로고
    • Analyzing real-time PCR data by the comparative C(T) method
    • Schmittgen, T. D., and Livak, K. J. (2008) Analyzing real-time PCR data by the comparative C(T) method. Nat. Protoc. 3, 1101-1108
    • (2008) Nat. Protoc. , vol.3 , pp. 1101-1108
    • Schmittgen, T.D.1    Livak, K.J.2
  • 25
    • 0025835716 scopus 로고
    • BCL2 protein is topographically restricted in tissues characterized by apoptotic cell death
    • Hockenbery, D. M., Zutter, M., Hickey, W., Nahm, M., and Korsmeyer, S. J. (1991) BCL2 protein is topographically restricted in tissues characterized by apoptotic cell death. Proc. Natl. Acad. Sci. U.S.A. 88, 6961-6965
    • (1991) Proc. Natl. Acad. Sci. U.S.A. , vol.88 , pp. 6961-6965
    • Hockenbery, D.M.1    Zutter, M.2    Hickey, W.3    Nahm, M.4    Korsmeyer, S.J.5
  • 26
  • 27
    • 0026508561 scopus 로고
    • Exposure of phosphatidylserine on the surface of apoptotic lymphocytes triggers specific recognition and removal by macrophages
    • Fadok, V. A., Voelker, D. R., Campbell, P. A., Cohen, J. J., Bratton, D. L., and Henson, P. M. (1992) Exposure of phosphatidylserine on the surface of apoptotic lymphocytes triggers specific recognition and removal by macrophages. J. Immunol. 148, 2207-2216
    • (1992) J. Immunol. , vol.148 , pp. 2207-2216
    • Fadok, V.A.1    Voelker, D.R.2    Campbell, P.A.3    Cohen, J.J.4    Bratton, D.L.5    Henson, P.M.6
  • 28
    • 0034725570 scopus 로고    scopus 로고
    • Regulation of phospholipid scramblase activity during apoptosis and cell activation by protein kinase Cδ
    • Frasch, S. C., Henson, P. M., Kailey, J. M., Richter, D. A., Janes, M. S., Fadok, V. A., and Bratton, D. L. (2000) Regulation of phospholipid scramblase activity during apoptosis and cell activation by protein kinase Cδ. J. Biol. Chem. 275, 23065-23073
    • (2000) J. Biol. Chem. , vol.275 , pp. 23065-23073
    • Frasch, S.C.1    Henson, P.M.2    Kailey, J.M.3    Richter, D.A.4    Janes, M.S.5    Fadok, V.A.6    Bratton, D.L.7
  • 30
    • 58149175555 scopus 로고    scopus 로고
    • The life of a cell: Apoptosis regulation by the PI3K/PKB pathway
    • Duronio, V. (2008) The life of a cell: apoptosis regulation by the PI3K/PKB pathway. Biochem. J. 415, 333-344
    • (2008) Biochem. J. , vol.415 , pp. 333-344
    • Duronio, V.1
  • 31
    • 52449095361 scopus 로고    scopus 로고
    • The RSK family of kinases: Emerging roles in cellular signalling
    • Anjum, R., and Blenis, J. (2008) The RSK family of kinases: emerging roles in cellular signalling. Nat. Rev. Mol. Cell Biol. 9, 747-758
    • (2008) Nat. Rev. Mol. Cell Biol. , vol.9 , pp. 747-758
    • Anjum, R.1    Blenis, J.2
  • 32
    • 77956095537 scopus 로고    scopus 로고
    • Mitochondria and cell death: Outer membrane permeabilization and beyond
    • Tait, S. W., and Green, D. R. (2010) Mitochondria and cell death: outer membrane permeabilization and beyond. Nat. Rev. Mol. Cell Biol. 11, 621-632
    • (2010) Nat. Rev. Mol. Cell Biol. , vol.11 , pp. 621-632
    • Tait, S.W.1    Green, D.R.2
  • 33
    • 0033769127 scopus 로고    scopus 로고
    • Interferon-γ sensitizes colonic epithelial cell lines to physiological and therapeutic inducers of colonocyte apoptosis
    • O'Connell, J., Bennett, M. W., Nally, K., O'Sullivan, G. C., Collins, J. K., and Shanahan, F. (2000) Interferon-γ sensitizes colonic epithelial cell lines to physiological and therapeutic inducers of colonocyte apoptosis. J. Cell. Physiol. 185, 331-338
    • (2000) J. Cell. Physiol. , vol.185 , pp. 331-338
    • O'connell, J.1    Bennett, M.W.2    Nally, K.3    O'sullivan, G.C.4    Collins, J.K.5    Shanahan, F.6
  • 34
    • 0037008761 scopus 로고    scopus 로고
    • Activation of BAD by therapeutic inhibition of epidermal growth factor receptor and transactivation by insulin-like growth factor receptor
    • Gilmore, A. P., Valentijn, A. J., Wang, P., Ranger, A. M., Bundred, N., O'Hare, M. J., Wakeling, A., Korsmeyer, S. J., and Streuli, C. H. (2002) Activation of BAD by therapeutic inhibition of epidermal growth factor receptor and transactivation by insulin-like growth factor receptor. J. Biol. Chem. 277, 27643-27650
    • (2002) J. Biol. Chem. , vol.277 , pp. 27643-27650
    • Gilmore, A.P.1    Valentijn, A.J.2    Wang, P.3    Ranger, A.M.4    Bundred, N.5    O'hare, M.J.6    Wakeling, A.7    Korsmeyer, S.J.8    Streuli, C.H.9
  • 35
    • 76249122645 scopus 로고    scopus 로고
    • GLP-1 mediates antiapoptotic effect by phosphorylating Bad through a β-arrestin 1-mediated ERK1/2 activation in pancreatic β-cells
    • Quoyer, J., Longuet, C., Broca, C., Linck, N., Costes, S., Varin, E., Bockaert, J., Bertrand, G., and Dalle, S. (2010) GLP-1 mediates antiapoptotic effect by phosphorylating Bad through a β-arrestin 1-mediated ERK1/2 activation in pancreatic β-cells. J. Biol. Chem. 285, 1989-2002
    • (2010) J. Biol. Chem. , vol.285 , pp. 1989-2002
    • Quoyer, J.1    Longuet, C.2    Broca, C.3    Linck, N.4    Costes, S.5    Varin, E.6    Bockaert, J.7    Bertrand, G.8    Dalle, S.9
  • 36
    • 79956113945 scopus 로고    scopus 로고
    • Epidermal growth factor regulates Mcl-1 expression through the MAPK-Elk-1 signalling pathway contributing to cell survival in breast cancer
    • Booy, E. P., Henson, E. S., and Gibson, S. B. (2011) Epidermal growth factor regulates Mcl-1 expression through the MAPK-Elk-1 signalling pathway contributing to cell survival in breast cancer. Oncogene 30, 2367-2378
    • (2011) Oncogene , vol.30 , pp. 2367-2378
    • Booy, E.P.1    Henson, E.S.2    Gibson, S.B.3
  • 37
    • 20444452357 scopus 로고    scopus 로고
    • Interleukin-6 contributes to Mcl-1 up-regulation and TRAIL resistance via an Akt-signaling pathway in cholangiocarcinoma cells
    • Kobayashi, S., Werneburg, N. W., Bronk, S. F., Kaufmann, S. H., and Gores, G. J. (2005) Interleukin-6 contributes to Mcl-1 up-regulation and TRAIL resistance via an Akt-signaling pathway in cholangiocarcinoma cells. Gastroenterology 128, 2054-2065
    • (2005) Gastroenterology , vol.128 , pp. 2054-2065
    • Kobayashi, S.1    Werneburg, N.W.2    Bronk, S.F.3    Kaufmann, S.H.4    Gores, G.J.5
  • 38
    • 0024386731 scopus 로고
    • Selective cellular expression of tissue factor in human tissues. Implications for disorders of hemostasis and thrombosis
    • Drake, T. A., Morrissey, J. H., and Edgington, T. S. (1989) Selective cellular expression of tissue factor in human tissues. Implications for disorders of hemostasis and thrombosis. Am. J. Pathol. 134, 1087-1097
    • (1989) Am. J. Pathol. , vol.134 , pp. 1087-1097
    • Drake, T.A.1    Morrissey, J.H.2    Edgington, T.S.3
  • 39
    • 0034624973 scopus 로고    scopus 로고
    • Tissue factor- and factor X-dependent activation of protease-activated receptor 2 by factor VIIa
    • Camerer, E., Huang, W., and Coughlin, S. R. (2000) Tissue factor- and factor X-dependent activation of protease-activated receptor 2 by factor VIIa. Proc. Natl. Acad. Sci. U.S.A. 97, 5255-5260
    • (2000) Proc. Natl. Acad. Sci. U.S.A. , vol.97 , pp. 5255-5260
    • Camerer, E.1    Huang, W.2    Coughlin, S.R.3
  • 41
    • 0842308313 scopus 로고    scopus 로고
    • Coagulation factors VIIa and Xa inhibit apoptosis and anoikis
    • Versteeg, H. H., Spek, C. A., Richel, D. J., and Peppelenbosch, M. P. (2004) Coagulation factors VIIa and Xa inhibit apoptosis and anoikis. Oncogene 23, 410-417
    • (2004) Oncogene , vol.23 , pp. 410-417
    • Versteeg, H.H.1    Spek, C.A.2    Richel, D.J.3    Peppelenbosch, M.P.4
  • 42
    • 0035831473 scopus 로고    scopus 로고
    • Executioner caspase-3, -6, and -7 perform distinct, non-redundant roles during the demolition phase of apoptosis
    • Slee, E. A., Adrain, C., and Martin, S. J. (2001) Executioner caspase-3, -6, and -7 perform distinct, non-redundant roles during the demolition phase of apoptosis. J. Biol. Chem. 276, 7320-7326
    • (2001) J. Biol. Chem. , vol.276 , pp. 7320-7326
    • Slee, E.A.1    Adrain, C.2    Martin, S.J.3
  • 43
    • 77950541887 scopus 로고    scopus 로고
    • Mast cell-derived tryptase inhibits apoptosis of human rheumatoid synovial fibroblasts via ρ-mediated signaling
    • Sawamukai, N., Yukawa, S., Saito, K., Nakayamada, S., Kambayashi, T., and Tanaka, Y. (2010) Mast cell-derived tryptase inhibits apoptosis of human rheumatoid synovial fibroblasts via ρ-mediated signaling. Arthritis Rheum. 62, 952-959
    • (2010) Arthritis Rheum. , vol.62 , pp. 952-959
    • Sawamukai, N.1    Yukawa, S.2    Saito, K.3    Nakayamada, S.4    Kambayashi, T.5    Tanaka, Y.6
  • 45
  • 46
    • 0034714379 scopus 로고    scopus 로고
    • Cellular localization of membrane-type serine protease 1 and identification of protease-activated receptor-2 and single-chain urokinase-type plasminogen activator as substrates
    • Takeuchi, T., Harris, J. L., Huang, W., Yan, K. W., Coughlin, S. R., and Craik, C. S. (2000) Cellular localization of membrane-type serine protease 1 and identification of protease-activated receptor-2 and single-chain urokinase-type plasminogen activator as substrates. J. Biol. Chem. 275, 26333-26342
    • (2000) J. Biol. Chem. , vol.275 , pp. 26333-26342
    • Takeuchi, T.1    Harris, J.L.2    Huang, W.3    Yan, K.W.4    Coughlin, S.R.5    Craik, C.S.6
  • 48
    • 84883056969 scopus 로고    scopus 로고
    • MicroRNA-34a mediates the autocrine signaling of PAR2-activating proteinase and its role in colonic cancer cell proliferation
    • Ma, Y., Bao-Han, W., Lv, X., Su, Y., Zhao, X., Yin, Y., and Zhang, X. (2013) MicroRNA-34a mediates the autocrine signaling of PAR2-activating proteinase and its role in colonic cancer cell proliferation. PLoS One 8, e72383
    • (2013) PLoS One , vol.8 , pp. e72383
    • Ma, Y.1    Bao-Han, W.2    Lv, X.3    Su, Y.4    Zhao, X.5    Yin, Y.6    Zhang, X.7
  • 49
    • 1842791710 scopus 로고    scopus 로고
    • Trypsin IV, a novel agonist of protease-activated receptors 2 and 4
    • Cottrell, G. S., Amadesi, S., Grady, E. F., and Bunnett, N. W. (2004) Trypsin IV, a novel agonist of protease-activated receptors 2 and 4. J. Biol. Chem. 279, 13532-13539
    • (2004) J. Biol. Chem. , vol.279 , pp. 13532-13539
    • Cottrell, G.S.1    Amadesi, S.2    Grady, E.F.3    Bunnett, N.W.4
  • 50
    • 0030702123 scopus 로고    scopus 로고
    • Akt phosphorylation of BAD couples survival signals to the cell-intrinsic death machinery
    • Datta, S. R., Dudek, H., Tao, X., Masters, S., Fu, H., Gotoh, Y., and Greenberg, M. E. (1997) Akt phosphorylation of BAD couples survival signals to the cell-intrinsic death machinery. Cell 91, 231-241
    • (1997) Cell , vol.91 , pp. 231-241
    • Datta, S.R.1    Dudek, H.2    Tao, X.3    Masters, S.4    Fu, H.5    Gotoh, Y.6    Greenberg, M.E.7
  • 51
    • 0032747134 scopus 로고    scopus 로고
    • Regulation of bad phosphorylation and association with Bcl-x(L) by the MAPK/Erk kinase
    • Scheid, M. P., Schubert, K. M., and Duronio, V. (1999) Regulation of bad phosphorylation and association with Bcl-x(L) by the MAPK/Erk kinase. J. Biol. Chem. 274, 31108-31113
    • (1999) J. Biol. Chem. , vol.274 , pp. 31108-31113
    • Scheid, M.P.1    Schubert, K.M.2    Duronio, V.3
  • 52
    • 0034682812 scopus 로고    scopus 로고
    • BAD Ser-155 phosphorylation regulates BAD/Bcl-XL interaction and cell survival
    • Tan, Y., Demeter, M. R., Ruan, H., and Comb, M. J. (2000) BAD Ser-155 phosphorylation regulates BAD/Bcl-XL interaction and cell survival. J. Biol. Chem. 275, 25865-25869
    • (2000) J. Biol. Chem. , vol.275 , pp. 25865-25869
    • Tan, Y.1    Demeter, M.R.2    Ruan, H.3    Comb, M.J.4
  • 54
    • 0033581927 scopus 로고    scopus 로고
    • Regulation of BAD phosphorylation at serine 112 by the Ras-mitogen- activated protein kinase pathway
    • Fang, X., Yu, S., Eder, A., Mao, M., Bast, R. C., Jr., Boyd, D., and Mills, G. B. (1999) Regulation of BAD phosphorylation at serine 112 by the Ras-mitogen- activated protein kinase pathway. Oncogene 18, 6635-6640
    • (1999) Oncogene , vol.18 , pp. 6635-6640
    • Fang, X.1    Yu, S.2    Eder, A.3    Mao, M.4    Bast, R.C.5    Boyd, D.6    Mills, G.B.7
  • 55
    • 0030584088 scopus 로고    scopus 로고
    • Serine phosphorylation of death agonist BAD in response to survival factor results in binding to 14-3-3 not BCL-X (L)
    • Zha, J., Harada, H., Yang, E., Jockel, J., and Korsmeyer, S. J. (1996) Serine phosphorylation of death agonist BAD in response to survival factor results in binding to 14-3-3 not BCL-X (L). Cell 87, 619-628
    • (1996) Cell , vol.87 , pp. 619-628
    • Zha, J.1    Harada, H.2    Yang, E.3    Jockel, J.4    Korsmeyer, S.J.5
  • 56
    • 0032772367 scopus 로고    scopus 로고
    • The antiapoptotic gene mcl-1 is up-regulated by the phosphatidylinositol 3-kinase/Akt signaling pathway through a transcription factor complex containing CREB
    • Wang, J. M., Chao, J. R., Chen, W., Kuo, M. L., Yen, J. J., and Yang-Yen, H. F. (1999) The antiapoptotic gene mcl-1 is up-regulated by the phosphatidylinositol 3-kinase/Akt signaling pathway through a transcription factor complex containing CREB. Mol. Cell. Biol. 19, 6195-6206
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 6195-6206
    • Wang, J.M.1    Chao, J.R.2    Chen, W.3    Kuo, M.L.4    Yen, J.J.5    Yang-Yen, H.F.6
  • 57
    • 0033556387 scopus 로고    scopus 로고
    • Regulation of MCL1 through a serum response factor/Elk-1-mediated mechanism links expression of a viability-promoting member of the BCL2 family to the induction of hematopoietic cell differentiation
    • Townsend, K. J., Zhou, P., Qian, L., Bieszczad, C. K., Lowrey, C. H., Yen, A., and Craig, R. W. (1999) Regulation of MCL1 through a serum response factor/Elk-1-mediated mechanism links expression of a viability-promoting member of the BCL2 family to the induction of hematopoietic cell differentiation. J. Biol. Chem. 274, 1801-1813
    • (1999) J. Biol. Chem. , vol.274 , pp. 1801-1813
    • Townsend, K.J.1    Zhou, P.2    Qian, L.3    Bieszczad, C.K.4    Lowrey, C.H.5    Yen, A.6    Craig, R.W.7
  • 58
    • 3142683869 scopus 로고    scopus 로고
    • MCL1 is phosphorylated in the PEST region and stabilized upon ERK activation in viable cells, and at additional sites with cytotoxic okadaic acid or taxol
    • Domina, A. M., Vrana, J. A., Gregory, M. A., Hann, S. R., and Craig, R. W. (2004) MCL1 is phosphorylated in the PEST region and stabilized upon ERK activation in viable cells, and at additional sites with cytotoxic okadaic acid or taxol. Oncogene 23, 5301-5315
    • (2004) Oncogene , vol.23 , pp. 5301-5315
    • Domina, A.M.1    Vrana, J.A.2    Gregory, M.A.3    Hann, S.R.4    Craig, R.W.5
  • 60
    • 0037134431 scopus 로고    scopus 로고
    • The phosphatidylinositol 3-kinase (PI3K)-Akt pathway suppresses Bax translocation to mitochondria
    • Tsuruta, F., Masuyama, N., and Gotoh, Y. (2002) The phosphatidylinositol 3-kinase (PI3K)-Akt pathway suppresses Bax translocation to mitochondria. J. Biol. Chem. 277, 14040-14047
    • (2002) J. Biol. Chem. , vol.277 , pp. 14040-14047
    • Tsuruta, F.1    Masuyama, N.2    Gotoh, Y.3
  • 62
    • 0038482050 scopus 로고    scopus 로고
    • Activation of the ERK1/2 signaling pathway promotes phosphorylation and proteasome-dependent degradation of the BH3-only protein, Bim
    • Ley, R., Balmanno, K., Hadfield, K., Weston, C., and Cook, S. J. (2003) Activation of the ERK1/2 signaling pathway promotes phosphorylation and proteasome-dependent degradation of the BH3-only protein, Bim. J. Biol. Chem. 278, 18811-18816
    • (2003) J. Biol. Chem. , vol.278 , pp. 18811-18816
    • Ley, R.1    Balmanno, K.2    Hadfield, K.3    Weston, C.4    Cook, S.J.5
  • 63
    • 0242521470 scopus 로고    scopus 로고
    • Phosphorylation of Bim-EL by Erk1/2 on serine 69 promotes its degradation via the proteasome pathway and regulates its proapoptotic function
    • Luciano, F., Jacquel, A., Colosetti, P., Herrant, M., Cagnol, S., Pages, G., and Auberger, P. (2003) Phosphorylation of Bim-EL by Erk1/2 on serine 69 promotes its degradation via the proteasome pathway and regulates its proapoptotic function. Oncogene 22, 6785-6793
    • (2003) Oncogene , vol.22 , pp. 6785-6793
    • Luciano, F.1    Jacquel, A.2    Colosetti, P.3    Herrant, M.4    Cagnol, S.5    Pages, G.6    Auberger, P.7


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