메뉴 건너뛰기




Volumn 18, Issue 8, 2009, Pages 1415-1423

MeCP2 involvement in the regulation of neuronal α-tubulin production

Author keywords

[No Author keywords available]

Indexed keywords

ALPHA TUBULIN; CYTOSKELETON PROTEIN; METHYL CPG BINDING PROTEIN 2;

EID: 64549113411     PISSN: 09646906     EISSN: 14602083     Source Type: Journal    
DOI: 10.1093/hmg/ddp048     Document Type: Article
Times cited : (21)

References (45)
  • 1
    • 0037280319 scopus 로고    scopus 로고
    • Elevated methyl-CpG-binding protein 2 expression is acquired during postnatal human brain development and is correlated with alternative polyadenylation
    • Balmer, D., Goldstine, J., Rao, Y.M. and LaSalle, J.M. (2003) Elevated methyl-CpG-binding protein 2 expression is acquired during postnatal human brain development and is correlated with alternative polyadenylation. J. Mol. Med., 81, 61-68.
    • (2003) J. Mol. Med , vol.81 , pp. 61-68
    • Balmer, D.1    Goldstine, J.2    Rao, Y.M.3    LaSalle, J.M.4
  • 2
    • 0037081840 scopus 로고    scopus 로고
    • Insight into Rett syndrome: MeCP2 levels display tissue- and cell- specific differences and correlate with neuronal maturation
    • Shahbazian, M.D., Antalffy, B., Armstrong, D.L. and Zoghbi, H.Y. (2002) Insight into Rett syndrome: MeCP2 levels display tissue- and cell- specific differences and correlate with neuronal maturation. Hum. Mol. Genet., 11, 115-124.
    • (2002) Hum. Mol. Genet , vol.11 , pp. 115-124
    • Shahbazian, M.D.1    Antalffy, B.2    Armstrong, D.L.3    Zoghbi, H.Y.4
  • 5
    • 0032574977 scopus 로고    scopus 로고
    • Transcriptional repression by the methyl-CpG-binding protein MeCP2 involves a histone deacetylase complex
    • Nan, X., Ng, H.-H., Johnson, C.A., Laherty, C.D., Turner, B.M., Eisenman, R.N. and Bird, A. (1998) Transcriptional repression by the methyl-CpG-binding protein MeCP2 involves a histone deacetylase complex. Nature, 393, 386-389.
    • (1998) Nature , vol.393 , pp. 386-389
    • Nan, X.1    Ng, H.-H.2    Johnson, C.A.3    Laherty, C.D.4    Turner, B.M.5    Eisenman, R.N.6    Bird, A.7
  • 7
    • 0342437491 scopus 로고    scopus 로고
    • MeCP2 is a transcriptional repressor with abundant binding sites in genomic chromatin
    • Nan, X., Campoy, F.J. and Bird, A. (1997) MeCP2 is a transcriptional repressor with abundant binding sites in genomic chromatin. Cell, 88, 471-481.
    • (1997) Cell , vol.88 , pp. 471-481
    • Nan, X.1    Campoy, F.J.2    Bird, A.3
  • 8
    • 0031792779 scopus 로고    scopus 로고
    • Identification and characterization of a family of mammalian methyl-CpG binding proteins
    • Hendrich, B. and Bird, A. (1998) Identification and characterization of a family of mammalian methyl-CpG binding proteins. Mol. Cell. Biol. 18, 6538-6547.
    • (1998) Mol. Cell. Biol , vol.18 , pp. 6538-6547
    • Hendrich, B.1    Bird, A.2
  • 9
    • 0032168678 scopus 로고    scopus 로고
    • CpG methylation, chromatin structure and gene silencing - a three-way connection
    • Razin, A. (1998) CpG methylation, chromatin structure and gene silencing - a three-way connection. EMBO J., 17, 4905-4908.
    • (1998) EMBO J , vol.17 , pp. 4905-4908
    • Razin, A.1
  • 10
    • 39749193120 scopus 로고    scopus 로고
    • MeCP2 deficiency in the brain decreases BDNF levels by REST/ CoREST-mediated repression and increases TRKB production
    • Abuhatzira, L., Makedonski, K., Kaufman, Y., Razin, A. and Shemer, R. (2007) MeCP2 deficiency in the brain decreases BDNF levels by REST/ CoREST-mediated repression and increases TRKB production. Epigenetics 2, 214-222.
    • (2007) Epigenetics , vol.2 , pp. 214-222
    • Abuhatzira, L.1    Makedonski, K.2    Kaufman, Y.3    Razin, A.4    Shemer, R.5
  • 12
    • 45849105557 scopus 로고    scopus 로고
    • MeCP2, a key contributor to neurological disease, activates and represses transcription
    • Chahrour, M., Jung, S.Y., Shaw, C., Zhou, X., Wong, S.T., Qin, J. and Zoghbi, H.Y. (2008) MeCP2, a key contributor to neurological disease, activates and represses transcription. Science, 320, 1224-1229.
    • (2008) Science , vol.320 , pp. 1224-1229
    • Chahrour, M.1    Jung, S.Y.2    Shaw, C.3    Zhou, X.4    Wong, S.T.5    Qin, J.6    Zoghbi, H.Y.7
  • 13
    • 0032830639 scopus 로고    scopus 로고
    • Rett syndrome is caused by mutations in X-linked MECP2, encoding methyl-CpG-binding protein 2
    • Amir, R.E., Van den Veyver, I.B., Wan, M., Tran, C.Q., Francke, U. and Zoghbi, H.Y. (1999) Rett syndrome is caused by mutations in X-linked MECP2, encoding methyl-CpG-binding protein 2. Nat. Genet., 23 185-188.
    • (1999) Nat. Genet , vol.23 , pp. 185-188
    • Amir, R.E.1    Van den Veyver, I.B.2    Wan, M.3    Tran, C.Q.4    Francke, U.5    Zoghbi, H.Y.6
  • 14
    • 0032231652 scopus 로고    scopus 로고
    • Rett syndrome: Confirmation of X-linked dominant inheritance, and localization of the gene to Xq28
    • Sirianni, N., Naidu, S., Pereira, J., Pillotto, R.F. and Hoffman, E.P. (1998) Rett syndrome: Confirmation of X-linked dominant inheritance, and localization of the gene to Xq28. Am. J. Hum. Genet., 63, 1552-1558.
    • (1998) Am. J. Hum. Genet , vol.63 , pp. 1552-1558
    • Sirianni, N.1    Naidu, S.2    Pereira, J.3    Pillotto, R.F.4    Hoffman, E.P.5
  • 15
    • 0032848963 scopus 로고    scopus 로고
    • Rett syndrome: Clinical update and review of recent genetic advances
    • Ellaway, C. and Christodoulou, J. (1999) Rett syndrome: Clinical update and review of recent genetic advances. J. Paediatr. Child Health, 35, 419-426.
    • (1999) J. Paediatr. Child Health , vol.35 , pp. 419-426
    • Ellaway, C.1    Christodoulou, J.2
  • 16
    • 0034123060 scopus 로고    scopus 로고
    • Methyl-CpG-binding protein 2 mutations in Rett syndrome
    • Van den Veyver, I.B. and Zoghbi, H.Y. (2000) Methyl-CpG-binding protein 2 mutations in Rett syndrome. Curr. Opin. Genet. Dev., 10, 275-279.
    • (2000) Curr. Opin. Genet. Dev , vol.10 , pp. 275-279
    • Van den Veyver, I.B.1    Zoghbi, H.Y.2
  • 17
    • 0031455739 scopus 로고    scopus 로고
    • Abnormalities in neuronal maturation in Rett syndrome neocortex: Preliminary molecular correlates
    • Kaufmann, W.E., Taylor, C.V., Hohmann, C.F., Sanwal, I.B. and Naidu, S. (1997) Abnormalities in neuronal maturation in Rett syndrome neocortex: preliminary molecular correlates. Eur. Child. Adolesc. Psychiatry, 6(Suppl. 1), 75-77.
    • (1997) Eur. Child. Adolesc. Psychiatry , vol.6 , Issue.SUPPL. 1 , pp. 75-77
    • Kaufmann, W.E.1    Taylor, C.V.2    Hohmann, C.F.3    Sanwal, I.B.4    Naidu, S.5
  • 18
    • 0031761177 scopus 로고    scopus 로고
    • Decreased dendritic branching in frontal, motor and limbic cortex in Rett syndrome compared with trisomy 21
    • Armstrong, D.D., Dunn, K. and Antalffy, B. (1998) Decreased dendritic branching in frontal, motor and limbic cortex in Rett syndrome compared with trisomy 21. J. Neuropathol. Exp. Neurol., 57, 1013-1017.
    • (1998) J. Neuropathol. Exp. Neurol , vol.57 , pp. 1013-1017
    • Armstrong, D.D.1    Dunn, K.2    Antalffy, B.3
  • 19
    • 0028969321 scopus 로고
    • Dendrites shed their dull image
    • Barinaga, M. (1995) Dendrites shed their dull image. Science, 268, 200-201.
    • (1995) Science , vol.268 , pp. 200-201
    • Barinaga, M.1
  • 20
    • 0030462207 scopus 로고    scopus 로고
    • Cytoskeletal plasticity in cells expressing neuronal microtubule-associated proteins
    • Kaech, S., Ludin, B. and Matus, A. (1996) Cytoskeletal plasticity in cells expressing neuronal microtubule-associated proteins. Neuron, 17, 1189-1199.
    • (1996) Neuron , vol.17 , pp. 1189-1199
    • Kaech, S.1    Ludin, B.2    Matus, A.3
  • 21
    • 0035200432 scopus 로고    scopus 로고
    • Neuronal instability: Implications for Rett's syndrome
    • Azmitia, E.C. (2001) Neuronal instability: Implications for Rett's syndrome. Brain Dev., 23 (Suppl. 1), S1-S10.
    • (2001) Brain Dev , vol.23 , Issue.SUPPL. 1
    • Azmitia, E.C.1
  • 22
    • 0027329103 scopus 로고
    • Pathobiochemical aspects of cytoskeleton components
    • Kunze, D. and Rustow, B. (1993) Pathobiochemical aspects of cytoskeleton components. Eur. J. Clin. Chem. Clin. Biochem., 31, 477-489.
    • (1993) Eur. J. Clin. Chem. Clin. Biochem , vol.31 , pp. 477-489
    • Kunze, D.1    Rustow, B.2
  • 23
    • 0037328861 scopus 로고    scopus 로고
    • Angelman syndrome: A review of the clinical and genetic aspects
    • Clayton-Smith, J. and Laan, L. (2003) Angelman syndrome: A review of the clinical and genetic aspects. J. Med. Genet., 40, 87-95.
    • (2003) J. Med. Genet , vol.40 , pp. 87-95
    • Clayton-Smith, J.1    Laan, L.2
  • 24
    • 0035054930 scopus 로고    scopus 로고
    • Angelman syndrome phenotype associated with mutations in MECP2, a gene encoding a methyl CpG binding protein
    • Watson, P., Black, G., Ramsden, S., Barrow, M., Super, M., Kerr, B. and Clayton-Smith, J. (2001) Angelman syndrome phenotype associated with mutations in MECP2, a gene encoding a methyl CpG binding protein. J. Med. Genet., 38, 224-228.
    • (2001) J. Med. Genet , vol.38 , pp. 224-228
    • Watson, P.1    Black, G.2    Ramsden, S.3    Barrow, M.4    Super, M.5    Kerr, B.6    Clayton-Smith, J.7
  • 27
    • 12744269033 scopus 로고    scopus 로고
    • Neurological aspects of the Angelman syndrome
    • Williams, C.A. (2005) Neurological aspects of the Angelman syndrome. Brain Dev., 27, 88-94.
    • (2005) Brain Dev , vol.27 , pp. 88-94
    • Williams, C.A.1
  • 28
    • 34247095504 scopus 로고    scopus 로고
    • Reduced MeCP2 expression is frequent in autism frontal cortex and correlates with aberrant MECP2 promoter methylation
    • Nagarajan, R.P., Hogart, A.R., Gwye, Y., Martin, M.R. and LaSalle, J.M. (2006) Reduced MeCP2 expression is frequent in autism frontal cortex and correlates with aberrant MECP2 promoter methylation. Epigenetics, 1, e1-e11.
    • (2006) Epigenetics , vol.1
    • Nagarajan, R.P.1    Hogart, A.R.2    Gwye, Y.3    Martin, M.R.4    LaSalle, J.M.5
  • 29
    • 17744380972 scopus 로고    scopus 로고
    • MeCP2 deficiency in Rett syndrome causes epigenetic aberrations at the PWS/AS imprinting center that affect UBE3A expression
    • Makedonski, K., Abuhatzira, L., Razin, A. and Shemer, R. (2005) MeCP2 deficiency in Rett syndrome causes epigenetic aberrations at the PWS/AS imprinting center that affect UBE3A expression. Hum. Mol. Genet., 14, 1049-1058.
    • (2005) Hum. Mol. Genet , vol.14 , pp. 1049-1058
    • Makedonski, K.1    Abuhatzira, L.2    Razin, A.3    Shemer, R.4
  • 30
    • 14044252235 scopus 로고    scopus 로고
    • Epigenetic overlap in autism-spectrum neurodevelopmental disorders: MECP2 deficiency causes reduced expression of UBE3A and GABRB3
    • Samaco, R.C., Hogart, A. and LaSalle, J.M. (2005) Epigenetic overlap in autism-spectrum neurodevelopmental disorders: MECP2 deficiency causes reduced expression of UBE3A and GABRB3. Hum. Mol. Genet., 14 483-492.
    • (2005) Hum. Mol. Genet , vol.14 , pp. 483-492
    • Samaco, R.C.1    Hogart, A.2    LaSalle, J.M.3
  • 31
    • 37549057995 scopus 로고    scopus 로고
    • The Angelman syndrome ubiquitin ligase localizes to the synapse and nucleus, and maternal deficiency results in abnormal dendritic spine morphology
    • Dindot, S.V., Antalffy, B.A., Bhattacharjee, M.B. and Beaudet, A.L. (2008) The Angelman syndrome ubiquitin ligase localizes to the synapse and nucleus, and maternal deficiency results in abnormal dendritic spine morphology. Hum. Mol. Genet., 17, 111-118.
    • (2008) Hum. Mol. Genet , vol.17 , pp. 111-118
    • Dindot, S.V.1    Antalffy, B.A.2    Bhattacharjee, M.B.3    Beaudet, A.L.4
  • 32
    • 0345169048 scopus 로고    scopus 로고
    • Post-translational modifications regulate microtubule function
    • Westermann, S. and Weber, K. (2003) Post-translational modifications regulate microtubule function. Nat. Rev. Mol. Cell. Biol., 4 938-947.
    • (2003) Nat. Rev. Mol. Cell. Biol , vol.4 , pp. 938-947
    • Westermann, S.1    Weber, K.2
  • 33
    • 0024020919 scopus 로고
    • Posttranslational tyrosination/detyrosination of tubulin
    • Barra, H.S., Arce, C.A. and Argarana, C.E. (1988) Posttranslational tyrosination/detyrosination of tubulin. Mol. Neurobiol., 2, 133-153.
    • (1988) Mol. Neurobiol , vol.2 , pp. 133-153
    • Barra, H.S.1    Arce, C.A.2    Argarana, C.E.3
  • 35
    • 0025294639 scopus 로고
    • Detyrosination of alpha tubulin does not stabilize microtubules in vivo
    • Webster, D.R., Wehland, J., Weber, K. and Borisy, G.G. (1990) Detyrosination of alpha tubulin does not stabilize microtubules in vivo. J. Cell. Biol., 111, 113-122.
    • (1990) J. Cell. Biol , vol.111 , pp. 113-122
    • Webster, D.R.1    Wehland, J.2    Weber, K.3    Borisy, G.G.4
  • 36
    • 0025313509 scopus 로고
    • Individual microtubules in the axon consist of domains that differ in both composition and stability
    • Baas, P.W. and Black, M.M. (1990) Individual microtubules in the axon consist of domains that differ in both composition and stability. J. Cell. Biol., 111, 495-509.
    • (1990) J. Cell. Biol , vol.111 , pp. 495-509
    • Baas, P.W.1    Black, M.M.2
  • 38
    • 0028283568 scopus 로고
    • Accumulation of delta 2-tubulin, a major tubulin variant that cannot be tyrosinated, in neuronal tissues and in stable microtubule assemblies
    • Paturle-Lafanechere, L., Manier, M., Trigault, N., Pirollet, F., Mazarguil, H. and Job, D. (1994) Accumulation of delta 2-tubulin, a major tubulin variant that cannot be tyrosinated, in neuronal tissues and in stable microtubule assemblies. J. Cell. Sci., 107, 1529-1543.
    • (1994) J. Cell. Sci , vol.107 , pp. 1529-1543
    • Paturle-Lafanechere, L.1    Manier, M.2    Trigault, N.3    Pirollet, F.4    Mazarguil, H.5    Job, D.6
  • 39
    • 3142764484 scopus 로고    scopus 로고
    • Genome-wide analysis of repressor element 1 silencing transcription factor/neuron-restrictive silencing factor (REST/NRSF) target genes
    • Bruce, A.W., Donaldson, I.J., Wood, I.C., Yerbury, S.A., Sadowski, M.I., Chapman, M., Gottgens, B. and Buckley, N.J. (2004) Genome-wide analysis of repressor element 1 silencing transcription factor/neuron-restrictive silencing factor (REST/NRSF) target genes. Proc. Natl Acad. Sci. USA 101, 10458-10463.
    • (2004) Proc. Natl Acad. Sci. USA , vol.101 , pp. 10458-10463
    • Bruce, A.W.1    Donaldson, I.J.2    Wood, I.C.3    Yerbury, S.A.4    Sadowski, M.I.5    Chapman, M.6    Gottgens, B.7    Buckley, N.J.8
  • 40
    • 0018526835 scopus 로고
    • The phylogenetic distribution of tubulin:tYrosine ligase
    • Preston, S.F., Deanin, G.G., Hanson, R.K. and Gordon, M.W. (1979) The phylogenetic distribution of tubulin:tYrosine ligase. J.Mol. Evol. 13, 233-244.
    • (1979) J.Mol. Evol , vol.13 , pp. 233-244
    • Preston, S.F.1    Deanin, G.G.2    Hanson, R.K.3    Gordon, M.W.4
  • 41
    • 0032540307 scopus 로고    scopus 로고
    • Kinesin is a candidate for cross-bridging microtubules and intermediate filaments. Selective binding of kinesin to detyrosinated tubulin and vimentin
    • Liao, G. and Gundersen, G.G. (1998) Kinesin is a candidate for cross-bridging microtubules and intermediate filaments. Selective binding of kinesin to detyrosinated tubulin and vimentin. J. Biol. Chem., 273, 9797-9803.
    • (1998) J. Biol. Chem , vol.273 , pp. 9797-9803
    • Liao, G.1    Gundersen, G.G.2
  • 42
    • 0032941748 scopus 로고    scopus 로고
    • Detyrosination of tubulin regulates the interaction of intermediate filaments with microtubules in vivo via a kinesin-dependent mechanism
    • Kreitzer, G., Liao, G. and Gundersen, G.G. (1999) Detyrosination of tubulin regulates the interaction of intermediate filaments with microtubules in vivo via a kinesin-dependent mechanism. Mol. Biol. Cell., 10, 1105-1118.
    • (1999) Mol. Biol. Cell , vol.10 , pp. 1105-1118
    • Kreitzer, G.1    Liao, G.2    Gundersen, G.G.3
  • 43
    • 0036156394 scopus 로고    scopus 로고
    • Export from pericentriolar endocytic recycling compartment to cell surface depends on stable, detyrosinated (glu) microtubules and kinesin
    • Lin, S.X., Gundersen, G.G. and Maxfield, F.R. (2002) Export from pericentriolar endocytic recycling compartment to cell surface depends on stable, detyrosinated (glu) microtubules and kinesin. Mol. Biol. Cell., 13, 96-109.
    • (2002) Mol. Biol. Cell , vol.13 , pp. 96-109
    • Lin, S.X.1    Gundersen, G.G.2    Maxfield, F.R.3
  • 44
    • 33847266846 scopus 로고    scopus 로고
    • Reversal of neurological defects in a mouse model of Rett syndrome
    • Guy, J., Gan, J., Selfridge, J., Cobb, S. and Bird, A. (2007) Reversal of neurological defects in a mouse model of Rett syndrome. Science 315, 1143-1147.
    • (2007) Science , vol.315 , pp. 1143-1147
    • Guy, J.1    Gan, J.2    Selfridge, J.3    Cobb, S.4    Bird, A.5
  • 45
    • 0030883534 scopus 로고    scopus 로고
    • Regional differences in synaptogenesis in human cerebral cortex
    • Huttenlocher, P.R. and Dabholkar, A.S. (1997) Regional differences in synaptogenesis in human cerebral cortex. J. Comp. Neurol., 387 167-178.
    • (1997) J. Comp. Neurol , vol.387 , pp. 167-178
    • Huttenlocher, P.R.1    Dabholkar, A.S.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.