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Volumn 7, Issue 4, 2011, Pages

PTG depletion removes lafora bodies and rescues the fatal epilepsy of lafora disease

Author keywords

[No Author keywords available]

Indexed keywords

CARBOHYDRATE DERIVATIVE; GLYCOGEN; GLYCOGEN SYNTHASE; GLYCOSYLTRANSFERASE INHIBITOR; PHOSPHOPROTEIN PHOSPHATASE 1; POLYGLUCOSAN; PROTEIN TARGETING TO GLYCOGEN; UNCLASSIFIED DRUG; GLUCAN; PPP1R3C PROTEIN, MOUSE; SIGNAL PEPTIDE;

EID: 79955634506     PISSN: 15537390     EISSN: 15537404     Source Type: Journal    
DOI: 10.1371/journal.pgen.1002037     Document Type: Article
Times cited : (105)

References (46)
  • 1
    • 0141618459 scopus 로고    scopus 로고
    • Mutations in NHLRC1 cause progressive myoclonus epilepsy
    • Chan EM, Young EJ, Ianzano L, Munteanu I, Zhao X, et al. (2003) Mutations in NHLRC1 cause progressive myoclonus epilepsy. Nat Genet 35: 125-127.
    • (2003) Nat Genet , vol.35 , pp. 125-127
    • Chan, E.M.1    Young, E.J.2    Ianzano, L.3    Munteanu, I.4    Zhao, X.5
  • 2
    • 17344362307 scopus 로고    scopus 로고
    • Mutations in a gene encoding a novel protein tyrosine phosphatase cause progressive myoclonus epilepsy
    • Minassian BA, Lee JR, Herbrick JA, Huizenga J, Soder S, et al. (1998) Mutations in a gene encoding a novel protein tyrosine phosphatase cause progressive myoclonus epilepsy. Nat Genet 20: 171-174.
    • (1998) Nat Genet , vol.20 , pp. 171-174
    • Minassian, B.A.1    Lee, J.R.2    Herbrick, J.A.3    Huizenga, J.4    Soder, S.5
  • 3
    • 0032937953 scopus 로고    scopus 로고
    • Corpora-amylacea and the family of polyglucosan diseases
    • Cavanagh JB, (1999) Corpora-amylacea and the family of polyglucosan diseases. Brain Res Brain Res Rev 29: 265-295.
    • (1999) Brain Res Brain Res Rev , vol.29 , pp. 265-295
    • Cavanagh, J.B.1
  • 5
    • 0034907260 scopus 로고    scopus 로고
    • Lafora's disease: towards a clinical, pathologic, and molecular synthesis
    • Minassian BA, (2001) Lafora's disease: towards a clinical, pathologic, and molecular synthesis. Pediatr Neurol 25: 21-29.
    • (2001) Pediatr Neurol , vol.25 , pp. 21-29
    • Minassian, B.A.1
  • 6
    • 0001617608 scopus 로고
    • Lafora disease, a form of progressive myoclonus epilepsy
    • In: Vinken PJBG, editors, Amsterdam, Elsevier
    • Van Heycop Ten Ham M, (1975) Lafora disease, a form of progressive myoclonus epilepsy. In: Vinken PJBG, editors. The epilepsies; Handbook of clinical neurology Amsterdam Elsevier pp. 382-422.
    • (1975) The Epilepsies; Handbook of Clinical Neurology , pp. 382-422
    • van Heycop Ten, H.M.1
  • 7
    • 77954326323 scopus 로고    scopus 로고
    • The regulation of muscle glycogen: the granule and its proteins
    • Graham TE, Yuan Z, Hill AK, Wilson RJ, (2010) The regulation of muscle glycogen: the granule and its proteins. Acta Physiol (Oxf) 199: 489-498.
    • (2010) Acta Physiol (Oxf) , vol.199 , pp. 489-498
    • Graham, T.E.1    Yuan, Z.2    Hill, A.K.3    Wilson, R.J.4
  • 8
    • 55249100297 scopus 로고    scopus 로고
    • Glucan, water dikinase phosphorylates crystalline maltodextrins and thereby initiates solubilization
    • Hejazi M, Fettke J, Haebel S, Edner C, Paris O, et al. (2008) Glucan, water dikinase phosphorylates crystalline maltodextrins and thereby initiates solubilization. Plant J 55: 323-334.
    • (2008) Plant J , vol.55 , pp. 323-334
    • Hejazi, M.1    Fettke, J.2    Haebel, S.3    Edner, C.4    Paris, O.5
  • 9
    • 0014739101 scopus 로고
    • Studies in myoclonus epilepsy (Lafora body form). II. Polyglucosans in the systemic deposits of myoclonus epilepsy and in corpora amylacea
    • Sakai M, Austin J, Witmer F, Trueb L, (1970) Studies in myoclonus epilepsy (Lafora body form). II. Polyglucosans in the systemic deposits of myoclonus epilepsy and in corpora amylacea. Neurology 20: 160-176.
    • (1970) Neurology , vol.20 , pp. 160-176
    • Sakai, M.1    Austin, J.2    Witmer, F.3    Trueb, L.4
  • 10
    • 0034634568 scopus 로고    scopus 로고
    • Identification of binding sites on protein targeting to glycogen for enzymes of glycogen metabolism
    • Fong NM, Jensen TC, Shah AS, Parekh NN, Saltiel AR, et al. (2000) Identification of binding sites on protein targeting to glycogen for enzymes of glycogen metabolism. J Biol Chem 275: 35034-35039.
    • (2000) J Biol Chem , vol.275 , pp. 35034-35039
    • Fong, N.M.1    Jensen, T.C.2    Shah, A.S.3    Parekh, N.N.4    Saltiel, A.R.5
  • 11
    • 0030614364 scopus 로고    scopus 로고
    • PTG, a protein phosphatase 1-binding protein with a role in glycogen metabolism
    • Printen JA, Brady MJ, Saltiel AR, (1997) PTG, a protein phosphatase 1-binding protein with a role in glycogen metabolism. Science 275: 1475-1478.
    • (1997) Science , vol.275 , pp. 1475-1478
    • Printen, J.A.1    Brady, M.J.2    Saltiel, A.R.3
  • 12
    • 17644444332 scopus 로고    scopus 로고
    • Laforin, the dual-phosphatase responsible for Lafora disease, interacts with R5 (PTG), a regulatory subunit of protein phosphatase-1 that enhances glycogen accumulation
    • Fernandez-Sanchez ME, Criado-Garcia O, Heath KE, Garcia-Fojeda B, Medrano-Fernandez I, et al. (2003) Laforin, the dual-phosphatase responsible for Lafora disease, interacts with R5 (PTG), a regulatory subunit of protein phosphatase-1 that enhances glycogen accumulation. Hum Mol Genet 12: 3161-3171.
    • (2003) Hum Mol Genet , vol.12 , pp. 3161-3171
    • Fernandez-Sanchez, M.E.1    Criado-Garcia, O.2    Heath, K.E.3    Garcia-Fojeda, B.4    Medrano-Fernandez, I.5
  • 13
    • 35548995067 scopus 로고    scopus 로고
    • Mechanism suppressing glycogen synthesis in neurons and its demise in progressive myoclonus epilepsy
    • Vilchez D, Ros S, Cifuentes D, Pujadas L, Valles J, et al. (2007) Mechanism suppressing glycogen synthesis in neurons and its demise in progressive myoclonus epilepsy. Nat Neurosci 10: 1407-1413.
    • (2007) Nat Neurosci , vol.10 , pp. 1407-1413
    • Vilchez, D.1    Ros, S.2    Cifuentes, D.3    Pujadas, L.4    Valles, J.5
  • 14
    • 42949086604 scopus 로고    scopus 로고
    • Malin decreases glycogen accumulation by promoting the degradation of protein targeting to glycogen (PTG)
    • Worby CA, Gentry MS, Dixon JE, (2008) Malin decreases glycogen accumulation by promoting the degradation of protein targeting to glycogen (PTG). J Biol Chem 283: 4069-4076.
    • (2008) J Biol Chem , vol.283 , pp. 4069-4076
    • Worby, C.A.1    Gentry, M.S.2    Dixon, J.E.3
  • 15
    • 77955486949 scopus 로고    scopus 로고
    • Genetic depletion of the malin E3 ubiquitin ligase in mice leads to lafora bodies and the accumulation of insoluble laforin
    • DePaoli-Roach AA, Tagliabracci VS, Segvich DM, Meyer CM, Irimia JM, et al. (2010) Genetic depletion of the malin E3 ubiquitin ligase in mice leads to lafora bodies and the accumulation of insoluble laforin. J Biol Chem 285: 25372-25381.
    • (2010) J Biol Chem , vol.285 , pp. 25372-25381
    • DePaoli-Roach, A.A.1    Tagliabracci, V.S.2    Segvich, D.M.3    Meyer, C.M.4    Irimia, J.M.5
  • 16
    • 57749088693 scopus 로고    scopus 로고
    • Abnormal metabolism of glycogen phosphate as a cause for Lafora disease
    • Tagliabracci VS, Girard JM, Segvich D, Meyer C, Turnbull J, et al. (2008) Abnormal metabolism of glycogen phosphate as a cause for Lafora disease. J Biol Chem 283: 33816-33825.
    • (2008) J Biol Chem , vol.283 , pp. 33816-33825
    • Tagliabracci, V.S.1    Girard, J.M.2    Segvich, D.3    Meyer, C.4    Turnbull, J.5
  • 18
    • 37649004558 scopus 로고    scopus 로고
    • Laforin is a glycogen phosphatase, deficiency of which leads to elevated phosphorylation of glycogen in vivo
    • Tagliabracci VS, Turnbull J, Wang W, Girard JM, Zhao X, et al. (2007) Laforin is a glycogen phosphatase, deficiency of which leads to elevated phosphorylation of glycogen in vivo. Proc Natl Acad Sci U S A 104: 19262-19266.
    • (2007) Proc Natl Acad Sci U S A , vol.104 , pp. 19262-19266
    • Tagliabracci, V.S.1    Turnbull, J.2    Wang, W.3    Girard, J.M.4    Zhao, X.5
  • 19
    • 33749620777 scopus 로고    scopus 로고
    • Laforin, a dual specificity phosphatase that dephosphorylates complex carbohydrates
    • Worby CA, Gentry MS, Dixon JE, (2006) Laforin, a dual specificity phosphatase that dephosphorylates complex carbohydrates. J Biol Chem 281: 30412-30418.
    • (2006) J Biol Chem , vol.281 , pp. 30412-30418
    • Worby, C.A.1    Gentry, M.S.2    Dixon, J.E.3
  • 20
    • 20444449699 scopus 로고    scopus 로고
    • Exercise capacity of mice genetically lacking muscle glycogen synthase: in mice, muscle glycogen is not essential for exercise
    • Pederson BA, Cope CR, Schroeder JM, Smith MW, Irimia JM, et al. (2005) Exercise capacity of mice genetically lacking muscle glycogen synthase: in mice, muscle glycogen is not essential for exercise. J Biol Chem 280: 17260-17265.
    • (2005) J Biol Chem , vol.280 , pp. 17260-17265
    • Pederson, B.A.1    Cope, C.R.2    Schroeder, J.M.3    Smith, M.W.4    Irimia, J.M.5
  • 22
    • 0038708307 scopus 로고    scopus 로고
    • PTG gene deletion causes impaired glycogen synthesis and developmental insulin resistance
    • Crosson SM, Khan A, Printen J, Pessin JE, Saltiel AR, (2003) PTG gene deletion causes impaired glycogen synthesis and developmental insulin resistance. J Clin Invest 111: 1423-1432.
    • (2003) J Clin Invest , vol.111 , pp. 1423-1432
    • Crosson, S.M.1    Khan, A.2    Printen, J.3    Pessin, J.E.4    Saltiel, A.R.5
  • 23
    • 79955613554 scopus 로고    scopus 로고
    • Enhanced Insulin Sensitivity and Energy Expenditure in PPP1R3C (PTG) Deleted Mice
    • Zhai L, Choi CS, Irimia-Dominguez J, Mcguire AC, Kim S, et al. (2007) Enhanced Insulin Sensitivity and Energy Expenditure in PPP1R3C (PTG) Deleted Mice. Diabetes 56: A62.
    • (2007) Diabetes , vol.56 , pp. 62
    • Zhai, L.1    Choi, C.S.2    Irimia-Dominguez, J.3    McGuire, A.C.4    Kim, S.5
  • 24
    • 18444405220 scopus 로고    scopus 로고
    • Targeted disruption of the Epm2a gene causes formation of Lafora inclusion bodies, neurodegeneration, ataxia, myoclonus epilepsy and impaired behavioral response in mice
    • Ganesh S, Delgado-Escueta AV, Sakamoto T, Avila MR, Machado-Salas J, et al. (2002) Targeted disruption of the Epm2a gene causes formation of Lafora inclusion bodies, neurodegeneration, ataxia, myoclonus epilepsy and impaired behavioral response in mice. Hum Mol Genet 11: 1251-1262.
    • (2002) Hum Mol Genet , vol.11 , pp. 1251-1262
    • Ganesh, S.1    Delgado-Escueta, A.V.2    Sakamoto, T.3    Avila, M.R.4    Machado-Salas, J.5
  • 25
    • 62149097997 scopus 로고    scopus 로고
    • The borderland of epilepsy: clinical and molecular features of phenomena that mimic epileptic seizures
    • Crompton DE, Berkovic SF, (2009) The borderland of epilepsy: clinical and molecular features of phenomena that mimic epileptic seizures. Lancet Neurol 8: 370-381.
    • (2009) Lancet Neurol , vol.8 , pp. 370-381
    • Crompton, D.E.1    Berkovic, S.F.2
  • 26
    • 33748935502 scopus 로고    scopus 로고
    • Myoclonus, motor deficits, alterations in emotional responses and monoamine metabolism in epsilon-sarcoglycan deficient mice
    • Yokoi F, Dang MT, Li J, Li Y, (2006) Myoclonus, motor deficits, alterations in emotional responses and monoamine metabolism in epsilon-sarcoglycan deficient mice. J Biochem 140: 141-146.
    • (2006) J Biochem , vol.140 , pp. 141-146
    • Yokoi, F.1    Dang, M.T.2    Li, J.3    Li, Y.4
  • 28
    • 0346728803 scopus 로고    scopus 로고
    • Functional diversity of protein phosphatase-1, a cellular economizer and reset button
    • Ceulemans H, Bollen M, (2004) Functional diversity of protein phosphatase-1, a cellular economizer and reset button. Physiol Rev 84: 1-39.
    • (2004) Physiol Rev , vol.84 , pp. 1-39
    • Ceulemans, H.1    Bollen, M.2
  • 29
    • 0014306984 scopus 로고
    • Studies in myoclonus epilepsy (Lafora body form). I. Isolation and preliminary characterization of Lafora bodies in two cases
    • Yokoi S, Austin J, Witmer F, Sakai M, (1968) Studies in myoclonus epilepsy (Lafora body form). I. Isolation and preliminary characterization of Lafora bodies in two cases. Arch Neurol 19: 15-33.
    • (1968) Arch Neurol , vol.19 , pp. 15-33
    • Yokoi, S.1    Austin, J.2    Witmer, F.3    Sakai, M.4
  • 30
    • 58949098465 scopus 로고    scopus 로고
    • The malin-laforin complex suppresses the cellular toxicity of misfolded proteins by promoting their degradation through the ubiquitin-proteasome system
    • Garyali P, Siwach P, Singh PK, Puri R, Mittal S, et al. (2009) The malin-laforin complex suppresses the cellular toxicity of misfolded proteins by promoting their degradation through the ubiquitin-proteasome system. Hum Mol Genet 18: 688-700.
    • (2009) Hum Mol Genet , vol.18 , pp. 688-700
    • Garyali, P.1    Siwach, P.2    Singh, P.K.3    Puri, R.4    Mittal, S.5
  • 31
    • 78149272475 scopus 로고    scopus 로고
    • Sequestration of chaperones and proteasome into Lafora bodies and proteasomal dysfunction induced by Lafora disease-associated mutations of malin
    • Rao SN, Maity R, Sharma J, Dey P, Shankar SK, et al. (2010) Sequestration of chaperones and proteasome into Lafora bodies and proteasomal dysfunction induced by Lafora disease-associated mutations of malin. Hum Mol Genet 19: 4726-4734.
    • (2010) Hum Mol Genet , vol.19 , pp. 4726-4734
    • Rao, S.N.1    Maity, R.2    Sharma, J.3    Dey, P.4    Shankar, S.K.5
  • 32
    • 67650110001 scopus 로고    scopus 로고
    • Increased endoplasmic reticulum stress and decreased proteasomal function in lafora disease models lacking the phosphatase laforin
    • doi:10.1371/journal.pone.0005907
    • Vernia S, Rubio T, Heredia M, Rodriguez de Cordoba S, Sanz P, (2009) Increased endoplasmic reticulum stress and decreased proteasomal function in lafora disease models lacking the phosphatase laforin. PLoS One 4: e5907 doi:10.1371/journal.pone.0005907.
    • (2009) PLoS One , vol.4 , pp. 5907
    • Vernia, S.1    Rubio, T.2    Heredia, M.3    Rodriguez de Cordoba, S.4    Sanz, P.5
  • 33
    • 77954486784 scopus 로고    scopus 로고
    • Laforin, the most common protein mutated in Lafora disease, regulates autophagy
    • Aguado C, Sarkar S, Korolchuk VI, Criado O, Vernia S, et al. (2010) Laforin, the most common protein mutated in Lafora disease, regulates autophagy. Hum Mol Genet 19: 2867-2876.
    • (2010) Hum Mol Genet , vol.19 , pp. 2867-2876
    • Aguado, C.1    Sarkar, S.2    Korolchuk, V.I.3    Criado, O.4    Vernia, S.5
  • 34
    • 0031770382 scopus 로고    scopus 로고
    • Adult polyglucosan body disease in Ashkenazi Jewish patients carrying the Tyr329Ser mutation in the glycogen-branching enzyme gene
    • Lossos A, Meiner Z, Barash V, Soffer D, Schlesinger I, et al. (1998) Adult polyglucosan body disease in Ashkenazi Jewish patients carrying the Tyr329Ser mutation in the glycogen-branching enzyme gene. Ann Neurol 44: 867-872.
    • (1998) Ann Neurol , vol.44 , pp. 867-872
    • Lossos, A.1    Meiner, Z.2    Barash, V.3    Soffer, D.4    Schlesinger, I.5
  • 35
    • 0018940303 scopus 로고
    • A distinct form of adult polyglucosan body disease with massive involvement of central and peripheral neuronal processes and astrocytes: a report of four cases and a review of the occurrence of polyglucosan bodies in other conditions such as Lafora's disease and normal ageing
    • Robitaille Y, Carpenter S, Karpati G, DiMauro SD, (1980) A distinct form of adult polyglucosan body disease with massive involvement of central and peripheral neuronal processes and astrocytes: a report of four cases and a review of the occurrence of polyglucosan bodies in other conditions such as Lafora's disease and normal ageing. Brain 103: 315-336.
    • (1980) Brain , vol.103 , pp. 315-336
    • Robitaille, Y.1    Carpenter, S.2    Karpati, G.3    DiMauro, S.D.4
  • 36
    • 57749209868 scopus 로고    scopus 로고
    • Crystal structures of protein phosphatase-1 bound to nodularin-R and tautomycin: a novel scaffold for structure-based drug design of serine/threonine phosphatase inhibitors
    • Kelker MS, Page R, Peti W, (2009) Crystal structures of protein phosphatase-1 bound to nodularin-R and tautomycin: a novel scaffold for structure-based drug design of serine/threonine phosphatase inhibitors. J Mol Biol 385: 11-21.
    • (2009) J Mol Biol , vol.385 , pp. 11-21
    • Kelker, M.S.1    Page, R.2    Peti, W.3
  • 38
    • 33646338642 scopus 로고    scopus 로고
    • Crystal structure of an archaeal glycogen synthase: insights into oligomerization and substrate binding of eukaryotic glycogen synthases
    • Horcajada C, Guinovart JJ, Fita I, Ferrer JC, (2006) Crystal structure of an archaeal glycogen synthase: insights into oligomerization and substrate binding of eukaryotic glycogen synthases. J Biol Chem 281: 2923-2931.
    • (2006) J Biol Chem , vol.281 , pp. 2923-2931
    • Horcajada, C.1    Guinovart, J.J.2    Fita, I.3    Ferrer, J.C.4
  • 39
    • 0024322304 scopus 로고
    • The allosteric transition of glycogen phosphorylase
    • Barford D, Johnson LN, (1989) The allosteric transition of glycogen phosphorylase. Nature 340: 609-616.
    • (1989) Nature , vol.340 , pp. 609-616
    • Barford, D.1    Johnson, L.N.2
  • 41
    • 0030812650 scopus 로고    scopus 로고
    • The crystal structure of a phosphorylase kinase peptide substrate complex: kinase substrate recognition
    • Lowe ED, Noble ME, Skamnaki VT, Oikonomakos NG, Owen DJ, et al. (1997) The crystal structure of a phosphorylase kinase peptide substrate complex: kinase substrate recognition. EMBO J 16: 6646-6658.
    • (1997) EMBO J , vol.16 , pp. 6646-6658
    • Lowe, E.D.1    Noble, M.E.2    Skamnaki, V.T.3    Oikonomakos, N.G.4    Owen, D.J.5
  • 42
    • 4644372268 scopus 로고    scopus 로고
    • Clinical and genetic heterogeneity of branching enzyme deficiency (glycogenosis type IV)
    • Bruno C, van Diggelen OP, Cassandrini D, Gimpelev M, Giuffre B, et al. (2004) Clinical and genetic heterogeneity of branching enzyme deficiency (glycogenosis type IV). Neurology 63: 1053-1058.
    • (2004) Neurology , vol.63 , pp. 1053-1058
    • Bruno, C.1    van Diggelen, O.P.2    Cassandrini, D.3    Gimpelev, M.4    Giuffre, B.5
  • 44
    • 77950342469 scopus 로고    scopus 로고
    • Restoration of muscle functionality by genetic suppression of glycogen synthesis in a murine model of Pompe disease
    • Douillard-Guilloux G, Raben N, Takikita S, Ferry A, Vignaud A, et al. (2010) Restoration of muscle functionality by genetic suppression of glycogen synthesis in a murine model of Pompe disease. Hum Mol Genet 19: 684-696.
    • (2010) Hum Mol Genet , vol.19 , pp. 684-696
    • Douillard-Guilloux, G.1    Raben, N.2    Takikita, S.3    Ferry, A.4    Vignaud, A.5
  • 45
    • 35248882500 scopus 로고    scopus 로고
    • Cardiomyopathy and exercise intolerance in muscle glycogen storage disease 0
    • Kollberg G, Tulinius M, Gilljam T, Ostman-Smith I, Forsander G, et al. (2007) Cardiomyopathy and exercise intolerance in muscle glycogen storage disease 0. N Engl J Med 357: 1507-1514.
    • (2007) N Engl J Med , vol.357 , pp. 1507-1514
    • Kollberg, G.1    Tulinius, M.2    Gilljam, T.3    Ostman-Smith, I.4    Forsander, G.5


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