메뉴 건너뛰기




Volumn 289, Issue 17, 2014, Pages 11715-11724

Dopamine d2 receptor relies upon ppm/pp2c protein phosphatases to dephosphorylate huntingtin protein

Author keywords

[No Author keywords available]

Indexed keywords

NEUROPHYSIOLOGY; PHOSPHATASES; PROTEINS;

EID: 84899439613     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M113.544312     Document Type: Article
Times cited : (17)

References (41)
  • 1
    • 0030752709 scopus 로고    scopus 로고
    • Aggregation of huntingtin in neuronal intranuclear inclusions and dystrophic neurites in brain
    • DiFiglia, M., Sapp, E., Chase, K. O., Davies, S. W., Bates, G. P., Vonsattel, J. P., and Aronin, N. (1997) Aggregation of huntingtin in neuronal intranuclear inclusions and dystrophic neurites in brain. Science 277, 1990-1993
    • (1997) Science , vol.277 , pp. 1990-1993
    • Difiglia, M.1    Sapp, E.2    Chase, K.O.3    Davies, S.W.4    Bates, G.P.5    Vonsattel, J.P.6    Aronin, N.7
  • 2
    • 33845612662 scopus 로고    scopus 로고
    • Dopamine enhances motor and neuropathological consequences of polyglutamine expanded huntingtin
    • Cyr, M., Sotnikova, T. D., Gainetdinov, R. R., and Caron M. G. (2006) Dopamine enhances motor and neuropathological consequences of polyglutamine expanded huntingtin. FASEB J. 20, 2541-2543
    • (2006) FASEB J. , vol.20 , pp. 2541-2543
    • Cyr, M.1    Sotnikova, T.D.2    Gainetdinov, R.R.3    Caron, M.G.4
  • 4
    • 24744434920 scopus 로고    scopus 로고
    • Unraveling a role for dopamine in Huntington's disease: The dual role of reactive oxygen species and D2 receptor stimulation
    • Charvin, D., Vanhoutte, P., Pagès, C., Borrelli, E., and Caboche, J. (2005) Unraveling a role for dopamine in Huntington's disease: the dual role of reactive oxygen species and D2 receptor stimulation. Proc. Natl. Acad. Sci. U.S.A. 102, 12218-12223
    • (2005) Proc. Natl. Acad. Sci. U.S.A. , vol.102 , pp. 12218-12223
    • Charvin, D.1    Vanhoutte, P.2    Pagès, C.3    Borrelli, E.4    Caboche, J.5
  • 6
    • 0031029072 scopus 로고    scopus 로고
    • Long-term effects of tetrabenazine in hyperkinetic movement disorders
    • Jankovic, J., and Beach, J. (1997) Long-term effects of tetrabenazine in hyperkinetic movement disorders. Neurology 48, 358-362
    • (1997) Neurology , vol.48 , pp. 358-362
    • Jankovic, J.1    Beach, J.2
  • 7
    • 33751242500 scopus 로고    scopus 로고
    • Vesicular monoamine transporter 2: Role as a novel target for drug development
    • Zheng, G., Dwoskin, L. P., and Crooks, P. A. (2006) Vesicular monoamine transporter 2: role as a novel target for drug development. AAPS J. 8, E682-E692
    • (2006) AAPS J. , vol.8
    • Zheng, G.1    Dwoskin, L.P.2    Crooks, P.A.3
  • 8
    • 33645798913 scopus 로고    scopus 로고
    • Tetrabenazine as antichorea therapy in Huntington disease: A randomized controlled trial
    • Huntington Study Group
    • Huntington Study Group (2006) Tetrabenazine as antichorea therapy in Huntington disease: a randomized controlled trial. Neurology 66, 366-372
    • (2006) Neurology , vol.66 , pp. 366-372
  • 9
    • 22344439156 scopus 로고    scopus 로고
    • Cdk5 phosphorylation of huntingtin reduces its cleavage by caspases: Implications for mutant huntingtin toxicity
    • Luo, S., Vacher, C., Davies, J. E., and Rubinsztein, D. C. (2005) Cdk5 phosphorylation of huntingtin reduces its cleavage by caspases: implications for mutant huntingtin toxicity. J. Cell Biol. 169, 647-656
    • (2005) J. Cell Biol. , vol.169 , pp. 647-656
    • Luo, S.1    Vacher, C.2    Davies, J.E.3    Rubinsztein, D.C.4
  • 11
  • 13
    • 79952615363 scopus 로고    scopus 로고
    • Preferential accumulation of N-terminal mutant huntingtin in the nuclei of striatal neurons is regulated by phosphorylation
    • Havel, L. S., Wang, C.-E., Wade, B., Huang, B., Li, S., and Li, X.-J. (2011) Preferential accumulation of N-terminal mutant huntingtin in the nuclei of striatal neurons is regulated by phosphorylation. Hum. Mol. Genet. 20, 1424-1437
    • (2011) Hum. Mol. Genet. , vol.20 , pp. 1424-1437
    • Havel, L.S.1    Wang, C.-E.2    Wade, B.3    Huang, B.4    Li, S.5    Li, X.-J.6
  • 14
    • 84864583212 scopus 로고    scopus 로고
    • The human phosphatase interactome: An intricate family portrait
    • Sacco, F., Perfetto, L., Castagnoli, L., and Cesareni G (2012) The human phosphatase interactome: An intricate family portrait. FEBS Lett. 586, 2732-2739
    • (2012) FEBS Lett. , vol.586 , pp. 2732-2739
    • Sacco, F.1    Perfetto, L.2    Castagnoli, L.3    Cesareni, G.4
  • 15
    • 49149112606 scopus 로고    scopus 로고
    • Huntingtin phosphorylation acts as a molecular switch for anterograde/retrograde transport in neurons
    • Colin, E., Zala, D., Liot, G., Rangone, H., Borrell-Pagès, M., Li, X. J., Saudou, F., and Humbert, S. (2008) Huntingtin phosphorylation acts as a molecular switch for anterograde/retrograde transport in neurons.EMBO J. 27, 2124-2134
    • (2008) EMBO J. , vol.27 , pp. 2124-2134
    • Colin, E.1    Zala, D.2    Liot, G.3    Rangone, H.4    Borrell-Pagès, M.5    Li, X.J.6    Saudou, F.7    Humbert, S.8
  • 17
    • 20444448900 scopus 로고    scopus 로고
    • Huntingtin phosphorylation on serine 421 is significantly reduced in the striatum and by polyglutamine expansion in vivo
    • Warby, S. C., Chan, E. Y., Metzler, M., Gan, L., Singaraja, R. R., Crocker, S. F., Robertson, H. A., and Hayden, M. R. (2005) Huntingtin phosphorylation on serine 421 is significantly reduced in the striatum and by polyglutamine expansion in vivo. Hum. Mol. Genet. 14, 1569-1577
    • (2005) Hum. Mol. Genet. , vol.14 , pp. 1569-1577
    • Warby, S.C.1    Chan, E.Y.2    Metzler, M.3    Gan, L.4    Singaraja, R.R.5    Crocker, S.F.6    Robertson, H.A.7    Hayden, M.R.8
  • 18
    • 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., Régulier, E., Aebischer, P., Déglon, N., Humbert, S., and Saudou, F. (2006) Inhibition of calcineurin by FK506 protects against polyglutamine-huntingtin toxicity through an increase of huntingtin phosphorylation at S421. J. Neurosci. 26, 1635-1645
    • (2006) J. Neurosci. , vol.26 , pp. 1635-1645
    • Pardo, R.1    Colin, E.2    Régulier, E.3    Aebischer, P.4    Déglon, N.5    Humbert, S.6    Saudou, F.7
  • 19
    • 22744449073 scopus 로고    scopus 로고
    • An Akt/α-arrestin 2/PP2A signaling complex mediates dopaminergic neurotransmission and behavior
    • Beaulieu, J. M., Sotnikova, T. D., Marion, S., Lefkowitz, R. J., Gainetdinov, R. R., and Caron, M. G. (2005) An Akt/α-arrestin 2/PP2A signaling complex mediates dopaminergic neurotransmission and behavior. Cell 122, 261-273
    • (2005) Cell , vol.122 , pp. 261-273
    • Beaulieu, J.M.1    Sotnikova, T.D.2    Marion, S.3    Lefkowitz, R.J.4    Gainetdinov, R.R.5    Caron, M.G.6
  • 21
    • 78049342155 scopus 로고    scopus 로고
    • Phosphorylation of huntingtin at s421 in yac128 neurons is associated with protection of yac128 neurons from nmda-mediated excitotoxicity and is modulated by pp1 and pp2a
    • Metzler, M., Gan, L., Mazarei, G., Graham, R. K., Liu, L., Bissada, N., Lu, G., Leavitt, B. R., and Hayden, M. R. (2010) Phosphorylation of Huntingtin at S421 in YAC128 Neurons Is Associated with Protection of YAC128 Neurons from NMDA-Mediated Excitotoxicity and Is Modulated by PP1 and PP2A. J. Neurosci. 30, 14318-14329
    • (2010) J. Neurosci. , vol.30 , pp. 14318-14329
    • Metzler, M.1    Gan, L.2    Mazarei, G.3    Graham, R.K.4    Liu, L.5    Bissada, N.6    Lu, G.7    Leavitt, B.R.8    Hayden, M.R.9
  • 22
    • 0023691731 scopus 로고
    • Inhibitory effect of a marine-sponge toxin, okadaic acid, on protein phosphatases
    • Bialojan, C., and Takai, A. (1988) Inhibitory effect of a marine-sponge toxin, okadaic acid, on protein phosphatases. Biochem. J. 256, 283-290
    • (1988) Biochem. J. , vol.256 , pp. 283-290
    • Bialojan, C.1    Takai, A.2
  • 23
    • 0027522757 scopus 로고
    • PPX, a novel protein serine/threonine phosphatase localized to centrosomes
    • Brewis, N. D., Street, A. J., Prescott, A. R., and Cohen P. T. (1993) PPX, a novel protein serine/threonine phosphatase localized to centrosomes. EMBO J. 12, 987-996
    • (1993) EMBO J. , vol.12 , pp. 987-996
    • Brewis, N.D.1    Street, A.J.2    Prescott, A.R.3    Cohen, P.T.4
  • 24
    • 0028133445 scopus 로고
    • Anovel human protein serine/threonine phosphatase, which possesses four tetratricopeptide repeat motifs and localizes to the nucleus
    • Chen, M. X., McPartlin, A. E., Brown, L., Chen, Y. H., Barker, H. M., and Cohen, P. T. (1994)Anovel human protein serine/threonine phosphatase, which possesses four tetratricopeptide repeat motifs and localizes to the nucleus. EMBO J. 13, 4278-4290
    • (1994) EMBO J. , vol.13 , pp. 4278-4290
    • Chen, M.X.1    McPartlin, A.E.2    Brown, L.3    Chen, Y.H.4    Barker, H.M.5    Cohen, P.T.6
  • 25
    • 40649115739 scopus 로고    scopus 로고
    • Use of protein phosphatase inhibitors
    • Chapter 13, Unit 13.10, John Wiley & Sons, Inc., Hoboken, NJ
    • Weiser, D. C., and Shenolikar, S. (2003) Use of protein phosphatase inhibitors. in Current Protocols in Protein Science, Chapter 13, Unit 13.10, John Wiley & Sons, Inc., Hoboken, NJ
    • (2003) Current Protocols in Protein Science
    • Weiser, D.C.1    Shenolikar, S.2
  • 26
    • 0024792262 scopus 로고
    • Protein phosphatases come of age
    • Cohen, P., and Cohen, P. T. (1989) Protein phosphatases come of age. J. Biol. Chem. 264, 21435-21438
    • (1989) J. Biol. Chem. , vol.264 , pp. 21435-21438
    • Cohen, P.1    Cohen, P.T.2
  • 27
    • 0031915128 scopus 로고    scopus 로고
    • Molecular cloning, expression, and characterization of a novel human serine/threonine protein phosphatase, PP7, that is homologous to Drosophila retinal degeneration C gene product (rdgC)
    • Huang, X., and Honkanen, R. E. (1998) Molecular cloning, expression, and characterization of a novel human serine/threonine protein phosphatase, PP7, that is homologous to Drosophila retinal degeneration C gene product (rdgC). J. Biol. Chem. 273, 1462-1468
    • (1998) J. Biol. Chem. , vol.273 , pp. 1462-1468
    • Huang, X.1    Honkanen, R.E.2
  • 28
    • 33846851965 scopus 로고    scopus 로고
    • The toxofilin-actin-PP2C complex of Toxoplasma: Identification of interacting domains
    • Jan, G., Delorme, V., David, V., Revenu, C., Rebollo, A., Cayla, X., and Tardieux, I. (2007) The toxofilin-actin-PP2C complex of Toxoplasma: identification of interacting domains. Biochem. J. 401, 711-719
    • (2007) Biochem. J. , vol.401 , pp. 711-719
    • Jan, G.1    Delorme, V.2    David, V.3    Revenu, C.4    Rebollo, A.5    Cayla, X.6    Tardieux, I.7
  • 29
    • 8544252382 scopus 로고    scopus 로고
    • A novel human serine-threonine phosphatase related to the Drosophila retinal degeneration C (rdgC) gene is selectively expressed in sensory neurons of neural crest origin
    • Montini, E., Rugarli, E. I., Van de Vosse, E., Andolfi, G., Mariani, M., Puca, A. A., Consalez, G. G., den Dunnen, J. T., Ballabio, A., and Franco, B. (1997) A novel human serine-threonine phosphatase related to the Drosophila retinal degeneration C (rdgC) gene is selectively expressed in sensory neurons of neural crest origin. Hum. Mol. Genet. 6, 1137-1145
    • (1997) Hum. Mol. Genet. , vol.6 , pp. 1137-1145
    • Montini, E.1    Rugarli, E.I.2    Van De Vosse, E.3    Andolfi, G.4    Mariani, M.5    Puca, A.A.6    Consalez, G.G.7    Den Dunnen, J.T.8    Ballabio, A.9    Franco, B.10
  • 31
    • 0033578730 scopus 로고    scopus 로고
    • Protein phosphatase 2C inactivates F-actin binding of human platelet moesin
    • Hishiya, A., Ohnishi, M., Tamura, S., and Nakamura, F. (1999) Protein phosphatase 2C inactivates F-actin binding of human platelet moesin. J. Biol. Chem. 274, 26705-26712
    • (1999) J. Biol. Chem. , vol.274 , pp. 26705-26712
    • Hishiya, A.1    Ohnishi, M.2    Tamura, S.3    Nakamura, F.4
  • 33
    • 58849164925 scopus 로고    scopus 로고
    • A dopamine D2 receptor mutant capable of G protein-mediated signaling but deficient in arrestin binding
    • Lan, H., Liu, Y., Bell, M. I., Gurevich, V. V., and Neve, K. A. (2009) A dopamine D2 receptor mutant capable of G protein-mediated signaling but deficient in arrestin binding. Mol. Pharmacol. 75, 113-123
    • (2009) Mol. Pharmacol. , vol.75 , pp. 113-123
    • Lan, H.1    Liu, Y.2    Bell, M.I.3    Gurevich, V.V.4    Neve, K.A.5
  • 34
    • 70350340056 scopus 로고    scopus 로고
    • Serine/threonine phosphatases: Mechanism through structure
    • Shi, Y. (2009) Serine/threonine phosphatases: mechanism through structure. Cell 139, 468-484
    • (2009) Cell , vol.139 , pp. 468-484
    • Shi, Y.1
  • 39
    • 72949098095 scopus 로고    scopus 로고
    • Genetic and pharmacological inhibition of calcineurin corrects the BDNF transport defect in Huntington's disease
    • Pineda, J. R., Pardo, R., Zala, D., Yu, H., Humbert, S., and Saudou, F. (2009) Genetic and pharmacological inhibition of calcineurin corrects the BDNF transport defect in Huntington's disease. Mol. Brain 2, 33
    • (2009) Mol. Brain , vol.2 , pp. 33
    • Pineda, J.R.1    Pardo, R.2    Zala, D.3    Yu, H.4    Humbert, S.5    Saudou, F.6
  • 41
    • 33750090125 scopus 로고    scopus 로고
    • Characterization of the desensitization properties of five dopamine receptor subtypes and alternatively spliced variants of dopamine D2 and D4 receptors
    • Cho, D. I., Beom, S., Van Tol, H. H., Caron, M. G., and Kim, K. M. (2006) Characterization of the desensitization properties of five dopamine receptor subtypes and alternatively spliced variants of dopamine D2 and D4 receptors. Biochem. Biophys. Res. Commun. 350, 634-640
    • (2006) Biochem. Biophys. Res. Commun. , vol.350 , pp. 634-640
    • Cho, D.I.1    Beom, S.2    Van Tol, H.H.3    Caron, M.G.4    Kim, K.M.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.