메뉴 건너뛰기




Volumn 271, Issue , 2015, Pages 77-83

Serine phosphorylation and arginine methylation at the crossroads to neurodegeneration

Author keywords

Arginine methylation; Neurodegenerative diseases; Protein arginine methyltransferase (PRMT); Protein kinase B (Akt); Serine phosphorylation

Indexed keywords

ANDROGEN RECEPTOR; ARGININE; POLYGLUTAMINE; PROTEIN ARGININE METHYLTRANSFERASE; PROTEIN KINASE B; SERINE;

EID: 84929650719     PISSN: 00144886     EISSN: 10902430     Source Type: Journal    
DOI: 10.1016/j.expneurol.2015.05.003     Document Type: Review
Times cited : (25)

References (71)
  • 1
    • 84929619814 scopus 로고    scopus 로고
    • Neuroprotection signaling of nuclear akt in neuronal cells
    • Ahn J.Y. Neuroprotection signaling of nuclear akt in neuronal cells. Exp. Neurobiol. 2014, 23:200-206.
    • (2014) Exp. Neurobiol. , vol.23 , pp. 200-206
    • Ahn, J.Y.1
  • 5
    • 58149295717 scopus 로고    scopus 로고
    • Protein arginine methylation in mammals: who, what, and why
    • Bedford M.T., Clarke S.G. Protein arginine methylation in mammals: who, what, and why. Mol. Cell 2009, 33:1-13.
    • (2009) Mol. Cell , vol.33 , pp. 1-13
    • Bedford, M.T.1    Clarke, S.G.2
  • 6
    • 20444504698 scopus 로고    scopus 로고
    • The genetic epidemiology of neurodegenerative disease
    • Bertram L., Tanzi R.E. The genetic epidemiology of neurodegenerative disease. J. Clin. Invest. 2005, 115:1449-1457.
    • (2005) J. Clin. Invest. , vol.115 , pp. 1449-1457
    • Bertram, L.1    Tanzi, R.E.2
  • 8
    • 0035369623 scopus 로고    scopus 로고
    • Transcription-dependent and -independent control of neuronal survival by the PI3K-Akt signaling pathway
    • Brunet A., Datta S.R., Greenberg M.E. Transcription-dependent and -independent control of neuronal survival by the PI3K-Akt signaling pathway. Curr. Opin. Neurobiol. 2001, 11:297-305.
    • (2001) Curr. Opin. Neurobiol. , vol.11 , pp. 297-305
    • Brunet, A.1    Datta, S.R.2    Greenberg, M.E.3
  • 11
    • 33749042331 scopus 로고    scopus 로고
    • Transcriptional repression of PGC-1alpha by mutant huntingtin leads to mitochondrial dysfunction and neurodegeneration
    • Cui L., Jeong H., Borovecki F., Parkhurst C.N., Tanese N., Krainc D. Transcriptional repression of PGC-1alpha by mutant huntingtin leads to mitochondrial dysfunction and neurodegeneration. Cell 2006, 127:59-69.
    • (2006) Cell , vol.127 , pp. 59-69
    • Cui, L.1    Jeong, H.2    Borovecki, F.3    Parkhurst, C.N.4    Tanese, N.5    Krainc, D.6
  • 12
    • 84877923497 scopus 로고    scopus 로고
    • The VPS35 gene and Parkinson's disease
    • Deng H., Gao K., Jankovic J. The VPS35 gene and Parkinson's disease. Mov. Disord. 2013, 28:569-575.
    • (2013) Mov. Disord. , vol.28 , pp. 569-575
    • Deng, H.1    Gao, K.2    Jankovic, J.3
  • 13
    • 79151471350 scopus 로고    scopus 로고
    • TLS and PRMT1 synergistically coactivate transcription at the survivin promoter through TLS arginine methylation
    • Du K., Arai S., Kawamura T., Matsushita A., Kurokawa R. TLS and PRMT1 synergistically coactivate transcription at the survivin promoter through TLS arginine methylation. Biochem. Biophys. Res. Commun. 2011, 404:991-996.
    • (2011) Biochem. Biophys. Res. Commun. , vol.404 , pp. 991-996
    • Du, K.1    Arai, S.2    Kawamura, T.3    Matsushita, A.4    Kurokawa, R.5
  • 14
    • 77957007354 scopus 로고    scopus 로고
    • SCA1-like disease in mice expressing wild-type ataxin-1 with a serine to aspartic acid replacement at residue 776
    • Duvick L., Barnes J., Ebner B., Agrawal S., Andresen M., Lim J., Giesler G.J., Zoghbi H.Y., Orr H.T. SCA1-like disease in mice expressing wild-type ataxin-1 with a serine to aspartic acid replacement at residue 776. Neuron 2010, 67:929-935.
    • (2010) Neuron , vol.67 , pp. 929-935
    • Duvick, L.1    Barnes, J.2    Ebner, B.3    Agrawal, S.4    Andresen, M.5    Lim, J.6    Giesler, G.J.7    Zoghbi, H.Y.8    Orr, H.T.9
  • 15
    • 80053573543 scopus 로고    scopus 로고
    • Small changes, big impact: posttranslational modifications and function of huntingtin in Huntington disease
    • Ehrnhoefer D.E., Sutton L., Hayden M.R. Small changes, big impact: posttranslational modifications and function of huntingtin in Huntington disease. Neuroscientist 2011, 17:475-492.
    • (2011) Neuroscientist , vol.17 , pp. 475-492
    • Ehrnhoefer, D.E.1    Sutton, L.2    Hayden, M.R.3
  • 17
    • 8144228406 scopus 로고    scopus 로고
    • Trinucleotide repeats and neurodegenerative disease
    • Everett C.M., Wood N.W. Trinucleotide repeats and neurodegenerative disease. Brain 2004, 127:2385-2405.
    • (2004) Brain , vol.127 , pp. 2385-2405
    • Everett, C.M.1    Wood, N.W.2
  • 18
    • 27944460430 scopus 로고    scopus 로고
    • Protein arginine methyltransferases: guardians of the Arg?
    • Fackelmayer F.O. Protein arginine methyltransferases: guardians of the Arg?. Trends Biochem. Sci. 2005, 30:666-671.
    • (2005) Trends Biochem. Sci. , vol.30 , pp. 666-671
    • Fackelmayer, F.O.1
  • 20
    • 36448930958 scopus 로고    scopus 로고
    • Polyglutamine domain modulates the TBP-TFIIB interaction: implications for its normal function and neurodegeneration
    • Friedman M.J., Shah A.G., Fang Z.H., Ward E.G., Warren S.T., Li S., Li X.J. Polyglutamine domain modulates the TBP-TFIIB interaction: implications for its normal function and neurodegeneration. Nat. Neurosci. 2007, 10:1519-1528.
    • (2007) Nat. Neurosci. , vol.10 , pp. 1519-1528
    • Friedman, M.J.1    Shah, A.G.2    Fang, Z.H.3    Ward, E.G.4    Warren, S.T.5    Li, S.6    Li, X.J.7
  • 21
    • 0041355365 scopus 로고    scopus 로고
    • Two novel proteins that are linked to insulin-like growth factor (IGF-I) receptors by the Grb10 adapter and modulate IGF-I signaling
    • Giovannone B., Lee E., Laviola L., Giorgino F., Cleveland K.A., Smith R.J. Two novel proteins that are linked to insulin-like growth factor (IGF-I) receptors by the Grb10 adapter and modulate IGF-I signaling. J. Biol. Chem. 2003, 278:31564-31573.
    • (2003) J. Biol. Chem. , vol.278 , pp. 31564-31573
    • Giovannone, B.1    Lee, E.2    Laviola, L.3    Giorgino, F.4    Cleveland, K.A.5    Smith, R.J.6
  • 22
    • 69249208791 scopus 로고    scopus 로고
    • The Akt kinases: isoform specificity in metabolism and cancer
    • Gonzalez E., McGraw T.E. The Akt kinases: isoform specificity in metabolism and cancer. Cell Cycle 2009, 8:2502-2508.
    • (2009) Cell Cycle , vol.8 , pp. 2502-2508
    • Gonzalez, E.1    McGraw, T.E.2
  • 23
    • 27844433569 scopus 로고    scopus 로고
    • Dynamics of human protein arginine methyltransferase 1(PRMT1) in vivo
    • Herrmann F., Lee J., Bedford M.T., Fackelmayer F.O. Dynamics of human protein arginine methyltransferase 1(PRMT1) in vivo. J. Biol. Chem. 2005, 280:38005-38010.
    • (2005) J. Biol. Chem. , vol.280 , pp. 38005-38010
    • Herrmann, F.1    Lee, J.2    Bedford, M.T.3    Fackelmayer, F.O.4
  • 25
    • 63049100536 scopus 로고    scopus 로고
    • PRMT1 mediated methylation of TAF15 is required for its positive gene regulatory function
    • Jobert L., Argentini M., Tora L. PRMT1 mediated methylation of TAF15 is required for its positive gene regulatory function. Exp. Cell Res. 2009, 315:1273-1286.
    • (2009) Exp. Cell Res. , vol.315 , pp. 1273-1286
    • Jobert, L.1    Argentini, M.2    Tora, L.3
  • 27
    • 18644379256 scopus 로고    scopus 로고
    • Testosterone reduction prevents phenotypic expression in a transgenic mouse model of spinal and bulbar muscular atrophy
    • Katsuno M., Adachi H., Kume A., Li M., Nakagomi Y., Niwa H., Sang C., Kobayashi Y., Doyu M., Sobue G. Testosterone reduction prevents phenotypic expression in a transgenic mouse model of spinal and bulbar muscular atrophy. Neuron 2002, 35:843-854.
    • (2002) Neuron , vol.35 , pp. 843-854
    • Katsuno, M.1    Adachi, H.2    Kume, A.3    Li, M.4    Nakagomi, Y.5    Niwa, H.6    Sang, C.7    Kobayashi, Y.8    Doyu, M.9    Sobue, G.10
  • 29
    • 33751518400 scopus 로고    scopus 로고
    • Angiogenin-induced protein kinase B/Akt activation is necessary for angiogenesis but is independent of nuclear translocation of angiogenin in HUVE cells
    • Kim H.M., Kang D.K., Kim H.Y., Kang S.S., Chang S.I. Angiogenin-induced protein kinase B/Akt activation is necessary for angiogenesis but is independent of nuclear translocation of angiogenin in HUVE cells. Biochem. Biophys. Res. Commun. 2007, 352:509-513.
    • (2007) Biochem. Biophys. Res. Commun. , vol.352 , pp. 509-513
    • Kim, H.M.1    Kang, D.K.2    Kim, H.Y.3    Kang, S.S.4    Chang, S.I.5
  • 30
    • 53049097189 scopus 로고    scopus 로고
    • EWS is a substrate of type I protein arginine methyltransferase, PRMT8
    • Kim J.D., Kako K., Kakiuchi M., Park G.G., Fukamizu A. EWS is a substrate of type I protein arginine methyltransferase, PRMT8. Int. J. Mol. Med. 2008, 22:309-315.
    • (2008) Int. J. Mol. Med. , vol.22 , pp. 309-315
    • Kim, J.D.1    Kako, K.2    Kakiuchi, M.3    Park, G.G.4    Fukamizu, A.5
  • 32
    • 64749109224 scopus 로고    scopus 로고
    • Minireview: protein arginine methylation of nonhistone proteins in transcriptional regulation
    • Lee Y.H., Stallcup M.R. Minireview: protein arginine methylation of nonhistone proteins in transcriptional regulation. Mol. Endocrinol. 2009, 23:425-433.
    • (2009) Mol. Endocrinol. , vol.23 , pp. 425-433
    • Lee, Y.H.1    Stallcup, M.R.2
  • 34
    • 0035912833 scopus 로고    scopus 로고
    • Akt suppresses androgen-induced apoptosis by phosphorylating and inhibiting androgen receptor
    • Lin H.K., Yeh S., Kang H.Y., Chang C. Akt suppresses androgen-induced apoptosis by phosphorylating and inhibiting androgen receptor. Proc. Natl. Acad. Sci. U. S. A. 2001, 98:7200-7205.
    • (2001) Proc. Natl. Acad. Sci. U. S. A. , vol.98 , pp. 7200-7205
    • Lin, H.K.1    Yeh, S.2    Kang, H.Y.3    Chang, C.4
  • 35
    • 34250788809 scopus 로고    scopus 로고
    • AKT/PKB signaling: navigating downstream
    • Manning B.D., Cantley L.C. AKT/PKB signaling: navigating downstream. Cell 2007, 129:1261-1274.
    • (2007) Cell , vol.129 , pp. 1261-1274
    • Manning, B.D.1    Cantley, L.C.2
  • 36
    • 77957011660 scopus 로고    scopus 로고
    • Native functions of the androgen receptor are essential to pathogenesis in a Drosophila model of spinobulbar muscular atrophy
    • Nedelsky N.B., Pennuto M., Smith R.B., Palazzolo I., Moore J., Nie Z., Neale G., Taylor J.P. Native functions of the androgen receptor are essential to pathogenesis in a Drosophila model of spinobulbar muscular atrophy. Neuron 2010, 67:936-952.
    • (2010) Neuron , vol.67 , pp. 936-952
    • Nedelsky, N.B.1    Pennuto, M.2    Smith, R.B.3    Palazzolo, I.4    Moore, J.5    Nie, Z.6    Neale, G.7    Taylor, J.P.8
  • 37
  • 40
    • 32544432052 scopus 로고    scopus 로고
    • Inhibition of calcineurin by FK506 protects against polyglutamine-huntingtin toxicity through an increase of huntingtin phosphorylation at S421
    • Pardo R., Colin E., Regulier E., Aebischer P., Deglon N., Humbert S., Saudou F. Inhibition of calcineurin by FK506 protects against polyglutamine-huntingtin toxicity through an increase of huntingtin phosphorylation at S421. J. Neurosci. 2006, 26:1635-1645.
    • (2006) J. Neurosci. , vol.26 , pp. 1635-1645
    • Pardo, R.1    Colin, E.2    Regulier, E.3    Aebischer, P.4    Deglon, N.5    Humbert, S.6    Saudou, F.7
  • 42
    • 80053094971 scopus 로고    scopus 로고
    • Neurotoxic effects of androgens in spinal and bulbar muscular atrophy
    • Parodi S., Pennuto M. Neurotoxic effects of androgens in spinal and bulbar muscular atrophy. Front. Neuroendocrinol. 2011, 32:416-425.
    • (2011) Front. Neuroendocrinol. , vol.32 , pp. 416-425
    • Parodi, S.1    Pennuto, M.2
  • 43
    • 63149139630 scopus 로고    scopus 로고
    • Post-translational modifications of expanded polyglutamine proteins: impact on neurotoxicity
    • Pennuto M., Palazzolo I., Poletti A. Post-translational modifications of expanded polyglutamine proteins: impact on neurotoxicity. Hum. Mol. Genet. 2009, 18:R40-R47.
    • (2009) Hum. Mol. Genet. , vol.18 , pp. R40-R47
    • Pennuto, M.1    Palazzolo, I.2    Poletti, A.3
  • 44
    • 0842265636 scopus 로고    scopus 로고
    • The serum- and glucocorticoid-induced kinase SGK inhibits mutant huntingtin-induced toxicity by phosphorylating serine 421 of huntingtin
    • Rangone H., Poizat G., Troncoso J., Ross C.A., MacDonald M.E., Saudou F., Humbert S. The serum- and glucocorticoid-induced kinase SGK inhibits mutant huntingtin-induced toxicity by phosphorylating serine 421 of huntingtin. Eur. J. Neurosci. 2004, 19:273-279.
    • (2004) Eur. J. Neurosci. , vol.19 , pp. 273-279
    • Rangone, H.1    Poizat, G.2    Troncoso, J.3    Ross, C.A.4    MacDonald, M.E.5    Saudou, F.6    Humbert, S.7
  • 45
    • 0038000050 scopus 로고    scopus 로고
    • Detection of arginine dimethylated peptides by parallel precursor ion scanning mass spectrometry in positive ion mode
    • Rappsilber J., Friesen W.J., Paushkin S., Dreyfuss G., Mann M. Detection of arginine dimethylated peptides by parallel precursor ion scanning mass spectrometry in positive ion mode. Anal. Chem. 2003, 75:3107-3114.
    • (2003) Anal. Chem. , vol.75 , pp. 3107-3114
    • Rappsilber, J.1    Friesen, W.J.2    Paushkin, S.3    Dreyfuss, G.4    Mann, M.5
  • 46
    • 84929635972 scopus 로고    scopus 로고
    • PRMT5- mediated symmetric arginine dimethylation is attenuated by mutant huntingtin and is impaired in Huntington's Disease (HD)
    • Ratovitski T., Arbez N., Stewart J.C., Chighladze E., Ross C.A. PRMT5- mediated symmetric arginine dimethylation is attenuated by mutant huntingtin and is impaired in Huntington's Disease (HD). Cell Cycle 2015.
    • (2015) Cell Cycle
    • Ratovitski, T.1    Arbez, N.2    Stewart, J.C.3    Chighladze, E.4    Ross, C.A.5
  • 47
    • 84869127465 scopus 로고    scopus 로고
    • IGF-1 administration ameliorates disease manifestations in a mouse model of spinal and bulbar muscular atrophy
    • Rinaldi C., Bott L.C., Chen K.L., Harmison G.G., Katsuno M., Sobue G., Pennuto M., Fischbeck K.H. IGF-1 administration ameliorates disease manifestations in a mouse model of spinal and bulbar muscular atrophy. Mol. Med. 2012, 18:1261-1268.
    • (2012) Mol. Med. , vol.18 , pp. 1261-1268
    • Rinaldi, C.1    Bott, L.C.2    Chen, K.L.3    Harmison, G.G.4    Katsuno, M.5    Sobue, G.6    Pennuto, M.7    Fischbeck, K.H.8
  • 48
    • 79954992390 scopus 로고    scopus 로고
    • Arginine methylation of BCL-2 antagonist of cell death (BAD) counteracts its phosphorylation and inactivation by Akt
    • Sakamaki J., Daitoku H., Ueno K., Hagiwara A., Yamagata K., Fukamizu A. Arginine methylation of BCL-2 antagonist of cell death (BAD) counteracts its phosphorylation and inactivation by Akt. Proc. Natl. Acad. Sci. U. S. A. 2011, 108:6085-6090.
    • (2011) Proc. Natl. Acad. Sci. U. S. A. , vol.108 , pp. 6085-6090
    • Sakamaki, J.1    Daitoku, H.2    Ueno, K.3    Hagiwara, A.4    Yamagata, K.5    Fukamizu, A.6
  • 49
    • 41549135942 scopus 로고    scopus 로고
    • FoxO transcription factors in the maintenance of cellular homeostasis during aging
    • Salih D.A., Brunet A. FoxO transcription factors in the maintenance of cellular homeostasis during aging. Curr. Opin. Cell Biol. 2008, 20:126-136.
    • (2008) Curr. Opin. Cell Biol. , vol.20 , pp. 126-136
    • Salih, D.A.1    Brunet, A.2
  • 52
    • 17144395975 scopus 로고    scopus 로고
    • The activation of Akt/PKB signaling pathway and cell survival
    • Song G., Ouyang G., Bao S. The activation of Akt/PKB signaling pathway and cell survival. J. Cell. Mol. Med. 2005, 9:59-71.
    • (2005) J. Cell. Mol. Med. , vol.9 , pp. 59-71
    • Song, G.1    Ouyang, G.2    Bao, S.3
  • 55
    • 0037077040 scopus 로고    scopus 로고
    • Toxic proteins in neurodegenerative disease
    • Taylor J.P., Hardy J., Fischbeck K.H. Toxic proteins in neurodegenerative disease. Science 2002, 296:1991-1995.
    • (2002) Science , vol.296 , pp. 1991-1995
    • Taylor, J.P.1    Hardy, J.2    Fischbeck, K.H.3
  • 56
    • 22344440666 scopus 로고    scopus 로고
    • Activation of nuclear receptor coactivator PGC-1alpha by arginine methylation
    • Teyssier C., Ma H., Emter R., Kralli A., Stallcup M.R. Activation of nuclear receptor coactivator PGC-1alpha by arginine methylation. Genes Dev. 2005, 19:1466-1473.
    • (2005) Genes Dev. , vol.19 , pp. 1466-1473
    • Teyssier, C.1    Ma, H.2    Emter, R.3    Kralli, A.4    Stallcup, M.R.5
  • 58
    • 83455162720 scopus 로고    scopus 로고
    • Arginine methylation by PRMT1 regulates nuclear-cytoplasmic localization and toxicity of FUS/TLS harbouring ALS-linked mutations
    • Tradewell M.L., Yu Z., Tibshirani M., Boulanger M.C., Durham H.D., Richard S. Arginine methylation by PRMT1 regulates nuclear-cytoplasmic localization and toxicity of FUS/TLS harbouring ALS-linked mutations. Hum. Mol. Genet. 2012, 21:136-149.
    • (2012) Hum. Mol. Genet. , vol.21 , pp. 136-149
    • Tradewell, M.L.1    Yu, Z.2    Tibshirani, M.3    Boulanger, M.C.4    Durham, H.D.5    Richard, S.6
  • 60
    • 84918525811 scopus 로고    scopus 로고
    • Synthesis and evaluation of protein arginine N-methyltransferase inhibitors designed to simultaneously occupy both substrate binding sites
    • van Haren M., van Ufford L.Q., Moret E.E., Martin N.I. Synthesis and evaluation of protein arginine N-methyltransferase inhibitors designed to simultaneously occupy both substrate binding sites. Org. Biomol. Chem. 2015, 13:549-560.
    • (2015) Org. Biomol. Chem. , vol.13 , pp. 549-560
    • van Haren, M.1    van Ufford, L.Q.2    Moret, E.E.3    Martin, N.I.4
  • 62
    • 0037135695 scopus 로고    scopus 로고
    • Identification of methylated proteins by protein arginine N-methyltransferase 1, PRMT1, with a new expression cloning strategy
    • Wada K., Inoue K., Hagiwara M. Identification of methylated proteins by protein arginine N-methyltransferase 1, PRMT1, with a new expression cloning strategy. Biochim. Biophys. Acta 2002, 1591:1-10.
    • (2002) Biochim. Biophys. Acta , vol.1591 , pp. 1-10
    • Wada, K.1    Inoue, K.2    Hagiwara, M.3
  • 67
    • 67649968054 scopus 로고    scopus 로고
    • The protein arginine methyltransferase family: an update about function, new perspectives and the physiological role in humans
    • Wolf S.S. The protein arginine methyltransferase family: an update about function, new perspectives and the physiological role in humans. Cell. Mol. Life Sci. 2009, 66:2109-2121.
    • (2009) Cell. Mol. Life Sci. , vol.66 , pp. 2109-2121
    • Wolf, S.S.1
  • 69
    • 34249735817 scopus 로고    scopus 로고
    • Akt attenuation of the serine protease activity of HtrA2/Omi through phosphorylation of serine 212
    • Yang L., Sun M., Sun X.M., Cheng G.Z., Nicosia S.V., Cheng J.Q. Akt attenuation of the serine protease activity of HtrA2/Omi through phosphorylation of serine 212. J. Biol. Chem. 2007, 282:10981-10987.
    • (2007) J. Biol. Chem. , vol.282 , pp. 10981-10987
    • Yang, L.1    Sun, M.2    Sun, X.M.3    Cheng, G.Z.4    Nicosia, S.V.5    Cheng, J.Q.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.