메뉴 건너뛰기




Volumn 12, Issue 5, 2013, Pages 1377-1394

Integrated proteomics identified novel activation of dynein IC2-GR-COX-1 signaling in neurofibromatosis type I (NF1) disease model cells

Author keywords

[No Author keywords available]

Indexed keywords

CYCLOOXYGENASE 1; DYNEIN ADENOSINE TRIPHOSPHATASE; DYNEIN INTERMEDIATE CHAIN 2; GLUCOCORTICOID RECEPTOR; SMALL INTERFERING RNA; UNCLASSIFIED DRUG;

EID: 84877617181     PISSN: 15359476     EISSN: 15359484     Source Type: Journal    
DOI: 10.1074/mcp.M112.024802     Document Type: Article
Times cited : (19)

References (48)
  • 3
    • 0037203821 scopus 로고    scopus 로고
    • Mechanism for the learning deficits in a mouse model of neurofibromatosis type 1
    • DOI 10.1038/nature711
    • Costa, R. M., Federov, N. B., Kogan, J. H., Murphy, G. G., Stern, J., Ohno, M., Kucherlapati, R., Jacks, T., and Silva, A. J. (2002) Mechanism for the learning deficits in a mouse model of neurofibromatosis type 1. Nature 415, 526-530 (Pubitemid 34130607)
    • (2002) Nature , vol.415 , Issue.6871 , pp. 526-530
    • Costa, R.M.1    Federov, N.B.2    Kogan, J.H.3    Murphy, G.G.4    Stern, J.5    Ohno, M.6    Kucherlapati, R.7    Jacks, T.8    Silva, A.J.9
  • 4
    • 0034708076 scopus 로고    scopus 로고
    • A neurofibromatosis-1-regulated pathway is required for learning in Drosophila
    • DOI 10.1038/35002593
    • Guo, H. F., Tong, J., Hannan, F., Luo, L., and Zhong, Y. (2000) A neurofi-bromatosis- 1-regulated pathway is required for learning in Drosophila. Nature 403, 895-898 (Pubitemid 30130991)
    • (2000) Nature , vol.403 , Issue.6772 , pp. 895-898
    • Guo, H.-F.1    Tong, J.2    Hannan, F.3    Luo, L.4    Zhong, Y.5
  • 6
    • 0038711739 scopus 로고    scopus 로고
    • Neurofibromatosis type I tumor suppressor neurofibromin regulates neuronal differentiation via its GTPase-activating protein function toward Ras
    • DOI 10.1074/jbc.M209413200
    • Yunoue, S., Tokuo, H., Fukunaga, K., Feng, L., Ozawa, T., Nishi, T., Kikuchi, A., Hattori, S., Kuratsu, J., Saya, H., and Araki, N. (2003) Neurofibromatosis type I tumor suppressor neurofibromin regulates neuronal differentiation via its GTPase-activating protein function toward Ras. J. Biol. Chem. 278, 26958-26969 (Pubitemid 36876849)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.29 , pp. 26958-26969
    • Yunoue, S.1    Tokuo, H.2    Fukunaga, K.3    Feng, L.4    Ozawa, T.5    Nishi, T.6    Kikuchi, A.7    Hattori, S.8    Kuratsu, J.9    Saya, H.10    Araki, N.11
  • 8
    • 71049171988 scopus 로고    scopus 로고
    • An integrated approach of differential mass spectrometry and gene ontology analysis identified novel proteins regulating neuronal differentiation and survival
    • Kobayashi, D., Kumagai, J., Morikawa, T., Wilson-Morifuji, M., Wilson, A., Irie, A., and Araki, N. (2009) An integrated approach of differential mass spectrometry and gene ontology analysis identified novel proteins regulating neuronal differentiation and survival. Mol. Cell. Proteomics 8, 2350-2367
    • (2009) Mol. Cell. Proteomics , vol.8 , pp. 2350-2367
    • Kobayashi, D.1    Kumagai, J.2    Morikawa, T.3    Wilson-Morifuji, M.4    Wilson, A.5    Irie, A.6    Araki, N.7
  • 9
    • 34848889259 scopus 로고    scopus 로고
    • The paragon algorithm, a next generation search engine that uses sequence temperature values sequence temperature values and feature probabilities to identify peptides from tandem mass spectra
    • DOI 10.1074/mcp.T600050-MCP200
    • Shilov, I. V., Seymour, S. L., Patel, A. A., Loboda, A., Tang, W. H., Keating, S. P., Hunter, C. L., Nuwaysir, L. M., and Schaeffer, D. A. (2007) The Paragon Algorithm, a next generation search engine that uses sequence temperature values and feature probabilities to identify peptides from tandem mass spectra. Mol. Cell. Proteomics 6, 1638-1655 (Pubitemid 47506173)
    • (2007) Molecular and Cellular Proteomics , vol.6 , Issue.9 , pp. 1638-1655
    • Shilov, I.V.1    Seymourt, S.L.2    Patel, A.A.3    Loboda, A.4    Tang, W.H.5    Keating, S.P.6    Hunter, C.L.7    Nuwaysir, L.M.8    Schaeffer, D.A.9
  • 10
    • 28244469687 scopus 로고    scopus 로고
    • The neurofibromatosis type 1 gene product neurofibromin enhances cell motility by regulating actin filament dynamics via the Rho-ROCK-LIMK2-cofilin pathway
    • DOI 10.1074/jbc.M503707200
    • Ozawa, T., Araki, N., Yunoue, S., Tokuo, H., Feng, L., Patrakitkomjorn, S., Hara, T., Ichikawa, Y., Matsumoto, K., Fujii, K., and Saya, H. (2005) The neurofibromatosis type 1 gene product neurofibromin enhances cell motility by regulating actin filament dynamics via the Rho-ROCK-LIMK2-cofilin pathway. J. Biol. Chem. 280, 39524-39533 (Pubitemid 41713911)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.47 , pp. 39524-39533
    • Ozawa, T.1    Araki, N.2    Yunoue, S.3    Tokuo, H.4    Feng, L.5    Patrakitkomjorn, S.6    Hara, T.7    Ichikawa, Y.8    Matsumoto, K.9    Fuji, K.10    Saya, H.11
  • 11
    • 45349098064 scopus 로고    scopus 로고
    • A neuron-specific cytoplasmic dynein isoform preferentially transports TrkB signaling endosomes
    • DOI 10.1083/jcb.200803150
    • Ha, J., Lo, K. W., Myers, K. R., Carr, T. M., Humsi, M. K., Rasoul, B. A., Segal, R. A., and Pfister, K. K. (2008) A neuron-specific cytoplasmic dynein isoform preferentially transports TrkB signaling endosomes. J. Cell Biol. 181, 1027-1039 (Pubitemid 351846834)
    • (2008) Journal of Cell Biology , vol.181 , Issue.6 , pp. 1027-1039
    • Ha, J.1    Lo, K.W.-H.2    Myers, K.R.3    Carr, T.M.4    Humsi, M.K.5    Rasoul, B.A.6    Segal, R.A.7    Pfister, K.K.8
  • 12
    • 0030066783 scopus 로고    scopus 로고
    • Differential expression and phosphorylation of the 74-kDa intermediate chains of cytoplasmic dynein in cultured neurons and glia
    • DOI 10.1074/jbc.271.3.1687
    • Pfister, K. K., Salata, M. W., Dillman, J. F., 3rd, Vaughan, K. T., Vallee, R. B., Torre, E., and Lye, R. J. (1996) Differential expression and phosphorylation of the 74-kDa intermediate chains of cytoplasmic dynein in cultured neurons and glia. J. Biol. Chem. 271, 1687-1694 (Pubitemid 26028660)
    • (1996) Journal of Biological Chemistry , vol.271 , Issue.3 , pp. 1687-1694
    • Pfister, K.K.1    Salata, M.W.2    Dillman III, J.F.3    Vaughan, K.T.4    Vallee, R.B.5    Torre, E.6    Lye, R.J.7
  • 13
    • 0023441954 scopus 로고
    • Two signals mediate hormone-dependent nuclear localization of the glucocorticoid receptor
    • Picard, D., and Yamamoto, K. R. (1987) Two signals mediate hormone-dependent nuclear localization of the glucocorticoid receptor. EMBO J. 6, 3333-3340
    • (1987) EMBO J. , vol.6 , pp. 3333-3340
    • Picard, D.1    Yamamoto, K.R.2
  • 15
    • 0035805599 scopus 로고    scopus 로고
    • Evidence that the peptidylprolyl isomerase domain of the hsp90-binding immunophilin FKBP52 is involved in both dynein interaction and glucocorticoid receptor movement to the nucleus
    • Galigniana, M. D., Radanyi, C., Renoir, J. M., Housley, P. R., and Pratt, W. B. (2001) Evidence that the peptidylprolyl isomerase domain of the hsp90-binding immunophilin FKBP52 is involved in both dynein interaction and glucocorticoid receptor movement to the nucleus. J. Biol. Chem. 276, 14884-14889
    • (2001) J. Biol. Chem. , vol.276 , pp. 14884-14889
    • Galigniana, M.D.1    Radanyi, C.2    Renoir, J.M.3    Housley, P.R.4    Pratt, W.B.5
  • 17
    • 14244262261 scopus 로고    scopus 로고
    • FK506-binding proteins 51 and 52 differentially regulate dynein interaction and nuclear translocation of the glucocorticoid receptor in mammalian cells
    • DOI 10.1074/jbc.M407498200
    • Wochnik, G. M., Ruegg, J., Abel, G. A., Schmidt, U., Holsboer, F., and Rein, T. (2005) FK506-binding proteins 51 and 52 differentially regulate dynein interaction and nuclear translocation of the glucocorticoid receptor in mammalian cells. J. Biol. Chem. 280, 4609-4616 (Pubitemid 40288629)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.6 , pp. 4609-4616
    • Wochnik, G.M.1    Ruegg, J.2    Abel, G.A.3    Schmidt, U.4    Holsboer, F.5    Rein, T.6
  • 18
    • 0035854775 scopus 로고    scopus 로고
    • Cytoplasmic dynein intermediate chain phosphorylation regulates binding to dynactin
    • Vaughan, P. S., Leszyk, J. D., and Vaughan, K. T. (2001) Cytoplasmic dynein intermediate chain phosphorylation regulates binding to dynactin. J. Biol. Chem. 276, 26171-26179
    • (2001) J. Biol. Chem. , vol.276 , pp. 26171-26179
    • Vaughan, P.S.1    Leszyk, J.D.2    Vaughan, K.T.3
  • 19
    • 84877589635 scopus 로고    scopus 로고
    • A Mango Smoothies
    • BioBit, ASBMB Today August 2009
    • BioBit, ASBMB Journal Science (2009) A Mango Smoothies. ASBMB Today August 2009, 31
    • (2009) ASBMB Journal Science , pp. 31
  • 21
    • 0024604298 scopus 로고
    • Cytoplasmic dynein is a minus end-directed motor for membranous organelles
    • DOI 10.1016/0092-8674(89)90627-2
    • Schroer, T. A., Steuer, E. R., and Sheetz, M. P. (1989) Cytoplasmic dynein is a minus end-directed motor for membranous organelles. Cell 56, 937-946 (Pubitemid 19091006)
    • (1989) Cell , vol.56 , Issue.6 , pp. 937-946
    • Schroer, T.A.1    Steuer, E.R.2    Sheetz, M.P.3
  • 22
    • 78449269612 scopus 로고    scopus 로고
    • Molecular motors in neurons: transport mechanisms and roles in brain function, development, and disease
    • Hirokawa, N., Niwa, S., and Tanaka, Y. (2010) Molecular motors in neurons: transport mechanisms and roles in brain function, development, and disease. Neuron 68, 610-638
    • (2010) Neuron , vol.68 , pp. 610-638
    • Hirokawa, N.1    Niwa, S.2    Tanaka, Y.3
  • 24
    • 0035449118 scopus 로고    scopus 로고
    • Growth factor regulation of cytoplasmic dynein intermediate chain subunit expression preceding neurite extension
    • DOI 10.1002/jnr.1168
    • Salata, M. W., Dillman, J. F., 3rd, Lye, R. J., and Pfister, K. K. (2001) Growth factor regulation of cytoplasmic dynein intermediate chain subunit expression preceding neurite extension. J. Neurosci. Res. 65, 408-416 (Pubitemid 32831393)
    • (2001) Journal of Neuroscience Research , vol.65 , Issue.5 , pp. 408-416
    • Salata, M.W.1    Dillman III, J.F.2    John, L.R.3    Pfister, K.K.4
  • 26
    • 0031047830 scopus 로고    scopus 로고
    • Casein kinase II binds to and phosphorylates cytoplasmic dynein
    • DOI 10.1074/jbc.272.9.5887
    • Karki, S., Tokito, M. K., and Holzbaur, E. L. (1997) Casein kinase II binds to and phosphorylates cytoplasmic dynein. J. Biol. Chem. 272, 5887-5891 (Pubitemid 27102423)
    • (1997) Journal of Biological Chemistry , vol.272 , Issue.9 , pp. 5887-5891
    • Karki, S.1    Tokito, M.K.2    Holzbaur, E.L.F.3
  • 29
    • 22144489915 scopus 로고    scopus 로고
    • Role of 14-3-3 eta as a positive regulator of the glucocorticoid receptor transcriptional activation
    • DOI 10.1210/en.2004-1455
    • Kim, Y. S., Jang, S. W., Sung, H. J., Lee, H. J., Kim, I. S., Na, D. S., and Ko, J. (2005) Role of 14-3-3 eta as a positive regulator of the glucocorticoid receptor transcriptional activation. Endocrinology 146, 3133-3140 (Pubitemid 41002823)
    • (2005) Endocrinology , vol.146 , Issue.7 , pp. 3133-3140
    • Kim, Y.S.1    Jang, S.-W.2    Sung, H.J.3    Lee, H.J.4    Kim, I.S.5    Na, D.S.6    Ko, J.7
  • 30
    • 0033551847 scopus 로고    scopus 로고
    • Arachidonic acid oxygenation by COX-1 and COX-2. Mechanisms of catalysis and inhibition
    • Marnett, L. J., Rowlinson, S. W., Goodwin, D. C., Kalgutkar, A. S., and Lanzo, C. A. (1999) Arachidonic acid oxygenation by COX-1 and COX-2. Mechanisms of catalysis and inhibition. J. Biol. Chem. 274, 22903-22906
    • (1999) J. Biol. Chem. , vol.274 , pp. 22903-22906
    • Marnett, L.J.1    Rowlinson, S.W.2    Goodwin, D.C.3    Kalgutkar, A.S.4    Lanzo, C.A.5
  • 31
    • 0030479496 scopus 로고    scopus 로고
    • Prostaglandin endoperoxide H synthases (cyclooxygenases)-1 and -2
    • DOI 10.1074/jbc.271.52.33157
    • Smith, W. L., Garavito, R. M., and DeWitt, D. L. (1996) Prostaglandin endoperoxide H synthases (cyclooxygenases)-1 and -2. J. Biol. Chem. 271, 33157-33160 (Pubitemid 27010118)
    • (1996) Journal of Biological Chemistry , vol.271 , Issue.52 , pp. 33157-33160
    • Smith, W.L.1    Garavito, R.M.2    DeWitt, D.L.3
  • 32
    • 50649103235 scopus 로고    scopus 로고
    • Corticosteroids induce cyclooxygenase 1 expression in cardiomyocytes: Role of glucocorticoid receptor and Sp3 transcription factor
    • Sun, H., Sheveleva, E., and Chen, Q. M. (2008) Corticosteroids induce cyclooxygenase 1 expression in cardiomyocytes: role of glucocorticoid receptor and Sp3 transcription factor. Mol. Endocrinol. 22, 2076-2084
    • (2008) Mol. Endocrinol. , vol.22 , pp. 2076-2084
    • Sun, H.1    Sheveleva, E.2    Chen, Q.M.3
  • 33
    • 0033791318 scopus 로고    scopus 로고
    • Cyclooxygenases: Structural, cellular, and molecular biology
    • Smith, W. L., DeWitt, D. L., and Garavito, R. M. (2000) Cyclooxygenases: structural, cellular, and molecular biology. Annu. Rev. Biochem. 69, 145-182
    • (2000) Annu. Rev. Biochem. , vol.69 , pp. 145-182
    • Smith, W.L.1    DeWitt, D.L.2    Garavito, R.M.3
  • 34
    • 80755175881 scopus 로고    scopus 로고
    • Aberrant cAMP metabolism in NF1 malignant peripheral nerve sheath tumor cells
    • Dang, I., and De Vries, G. H. (2011) Aberrant cAMP metabolism in NF1 malignant peripheral nerve sheath tumor cells. Neurochem. Res. 36, 1697-1705
    • (2011) Neurochem. Res. , vol.36 , pp. 1697-1705
    • Dang, I.1    De Vries, G.H.2
  • 35
    • 78751481808 scopus 로고    scopus 로고
    • The effects of the stromal cell-derived cyclooxygenase-2 metabolite prostaglandin E2 on the proliferation of colon cancer cells
    • Park, S. W., Kim, H. S., Choi, M. S., Jeong, W. J., Heo, D. S., Kim, K. H., and Sung, M. W. (2011) The effects of the stromal cell-derived cyclooxygenase-2 metabolite prostaglandin E2 on the proliferation of colon cancer cells. J. Pharmacol. Exp. Ther. 336, 516-523
    • (2011) J. Pharmacol. Exp. Ther. , vol.336 , pp. 516-523
    • Park, S.W.1    Kim, H.S.2    Choi, M.S.3    Jeong, W.J.4    Heo, D.S.5    Kim, K.H.6    Sung, M.W.7
  • 36
    • 36849036243 scopus 로고    scopus 로고
    • The effect of cyclooxygenase-2 overexpression on skin carcinogenesis is context dependent
    • DOI 10.1002/mc.20340
    • Rundhaug, J. E., Pavone, A., Kim, E., and Fischer, S. M. (2007) The effect of cyclooxygenase-2 overexpression on skin carcinogenesis is context dependent. Mol. Carcinog. 46, 981-992 (Pubitemid 350234255)
    • (2007) Molecular Carcinogenesis , vol.46 , Issue.12 , pp. 981-992
    • Rundhaug, J.E.1    Pavone, A.2    Kim, E.3    Fischer, S.M.4
  • 39
    • 0034747981 scopus 로고    scopus 로고
    • Role of cyclooxygenase isoforms in gastric mucosal defence
    • Peskar, B. M. (2001) Role of cyclooxygenase isoforms in gastric mucosal defence. J. Physiol. Paris 95, 3-9
    • (2001) J. Physiol. Paris , vol.95 , pp. 3-9
    • Peskar, B.M.1
  • 40
    • 80054694701 scopus 로고    scopus 로고
    • Purinergic signaling induces cyclooxygenase-1-dependent prostanoid synthesis in microglia: Roles in the outcome of excitotoxic brain injury
    • Anrather, J., Gallo, E. F., Kawano, T., Orio, M., Abe, T., Gooden, C., Zhou, P., and Iadecola, C. (2011) Purinergic signaling induces cyclooxygenase-1-dependent prostanoid synthesis in microglia: roles in the outcome of excitotoxic brain injury. PLoS One 6, e25916
    • (2011) PLoS One , vol.6
    • Anrather, J.1    Gallo, E.F.2    Kawano, T.3    Orio, M.4    Abe, T.5    Gooden, C.6    Zhou, P.7    Iadecola, C.8
  • 41
    • 62949176283 scopus 로고    scopus 로고
    • The distinct roles of cyclooxygenase-1 and -2 in neuroinflammation: Implications for translational research
    • Choi, S. H., Aid, S., and Bosetti, F. (2009) The distinct roles of cyclooxygenase-1 and -2 in neuroinflammation: implications for translational research. Trends Pharmacol. Sci. 30, 174-181
    • (2009) Trends Pharmacol. Sci. , vol.30 , pp. 174-181
    • Choi, S.H.1    Aid, S.2    Bosetti, F.3
  • 42
    • 0030744590 scopus 로고    scopus 로고
    • Cyclooxygenase-1 behaves as a delayed response gene in PC12 cells differentiated by nerve growth factor
    • DOI 10.1074/jbc.272.30.18534
    • Kaplan, M. D., Olschowka, J. A., and O'Banion, M. K. (1997) Cyclooxygenase-1 behaves as a delayed response gene in PC12 cells differentiated by nerve growth factor. J. Biol. Chem. 272, 18534-18537 (Pubitemid 27318189)
    • (1997) Journal of Biological Chemistry , vol.272 , Issue.30 , pp. 18534-18537
    • Kaplan, M.D.1    Olschowka, J.A.2    O'Banion, M.K.3
  • 43
    • 67649421604 scopus 로고    scopus 로고
    • Gi-coupled prostanoid receptors are the likely targets for COX-1-generated prostanoids in rat pheochromocytoma (PC12) cells
    • Yung, H. S., Chow, K. B., Lai, K. H., and Wise, H. (2009) Gi-coupled prostanoid receptors are the likely targets for COX-1-generated prostanoids in rat pheochromocytoma (PC12) cells. Prostaglandins Leukot. Essent. Fatty Acids 81, 65-71
    • (2009) Prostaglandins Leukot. Essent. Fatty Acids , vol.81 , pp. 65-71
    • Yung, H.S.1    Chow, K.B.2    Lai, K.H.3    Wise, H.4
  • 44
    • 34249729416 scopus 로고    scopus 로고
    • Prostaglandin E receptors
    • DOI 10.1074/jbc.R600038200
    • Sugimoto, Y., and Narumiya, S. (2007) Prostaglandin E receptors. J. Biol. Chem. 282, 11613-11617 (Pubitemid 47100657)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.16 , pp. 11613-11617
    • Sugimoto, Y.1    Narumiya, S.2
  • 45
    • 77955282361 scopus 로고    scopus 로고
    • Prostaglandin E(2) and misoprostol induce neurite retraction in Neuro-2a cells
    • Tamiji, J., and Crawford, D. A. (2010) Prostaglandin E(2) and misoprostol induce neurite retraction in Neuro-2a cells. Biochem. Biophys. Res. Commun. 398, 450-456
    • (2010) Biochem. Biophys. Res. Commun. , vol.398 , pp. 450-456
    • Tamiji, J.1    Crawford, D.A.2
  • 46
    • 0029860810 scopus 로고    scopus 로고
    • Prostaglandin E receptor EP3 subtype induces neurite retraction via small GTPase rho
    • DOI 10.1074/jbc.271.47.29780
    • Katoh, H., Negishi, M., and Ichikawa, A. (1996) Prostaglandin E receptor EP3 subtype induces neurite retraction via small GTPase Rho. J. Biol. Chem. 271, 29780-29784 (Pubitemid 26389607)
    • (1996) Journal of Biological Chemistry , vol.271 , Issue.47 , pp. 29780-29784
    • Katoh, H.1    Negishi, M.2    Ichikawa, A.3
  • 47
    • 0031018226 scopus 로고    scopus 로고
    • A mouse model for the learning and memory deficits associated with neurofibromatosis type I
    • DOI 10.1038/ng0397-281
    • Silva, A. J., Frankland, P. W., Marowitz, Z., Friedman, E., Laszlo, G. S., Cioffi, D., Jacks, T., and Bourtchuladze, R. (1997) A mouse model for the learning and memory deficits associated with neurofibromatosis type I. Nat. Genet. 15, 281-284 (Pubitemid 27098723)
    • (1997) Nature Genetics , vol.15 , Issue.3 , pp. 281-284
    • Silva, A.J.1    Frankland, P.W.2    Marowitz, Z.3    Friedman, E.4    Lazlo, G.5    Cioffi, D.6    Jacks, T.7    Bourtchuladze, R.8
  • 48
    • 77951610854 scopus 로고    scopus 로고
    • Defective cAMP generation underlies the sensitivity of CNS neurons to neurofibromatosis-1 heterozygosity
    • Brown, J. A., Gianino, S. M., and Gutmann, D. H. (2010) Defective cAMP generation underlies the sensitivity of CNS neurons to neurofibromatosis-1 heterozygosity. J. Neurosci. 30, 5579-5589
    • (2010) J. Neurosci. , vol.30 , pp. 5579-5589
    • Brown, J.A.1    Gianino, S.M.2    Gutmann, D.H.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.