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Volumn 57, Issue 2, 2015, Pages 261-272

Structural mechanism of laforin function in glycogen dephosphorylation and lafora disease

Author keywords

[No Author keywords available]

Indexed keywords

GLUCAN; GLYCOGEN; LAFORIN; UNCLASSIFIED DRUG; EPM2A PROTEIN, HUMAN; MALTOHEXAOSE; NON RECEPTOR PROTEIN TYROSINE PHOSPHATASE; OLIGOSACCHARIDE; PHOSPHATE; PROTEIN BINDING;

EID: 84921567531     PISSN: 10972765     EISSN: 10974164     Source Type: Journal    
DOI: 10.1016/j.molcel.2014.11.020     Document Type: Article
Times cited : (47)

References (53)
  • 1
    • 0142027784 scopus 로고    scopus 로고
    • Membrane association of myotubularin-related protein 2 is mediated by a pleckstrin homology-GRAM domain and a coiled-coil dimerization module
    • Berger P., Schaffitzel C., Berger I., Ban N., Suter U. Membrane association of myotubularin-related protein 2 is mediated by a pleckstrin homology-GRAM domain and a coiled-coil dimerization module. Proc. Natl. Acad. Sci. USA 2003, 100:12177-12182.
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 12177-12182
    • Berger, P.1    Schaffitzel, C.2    Berger, I.3    Ban, N.4    Suter, U.5
  • 2
    • 0025896221 scopus 로고
    • Progressive myoclonus epilepsies: clinical and neurophysiological diagnosis
    • Berkovic S.F., So N.K., Andermann F. Progressive myoclonus epilepsies: clinical and neurophysiological diagnosis. J.Clin. Neurophysiol. 1991, 8:261-274.
    • (1991) J.Clin. Neurophysiol. , vol.8 , pp. 261-274
    • Berkovic, S.F.1    So, N.K.2    Andermann, F.3
  • 3
    • 77950519125 scopus 로고    scopus 로고
    • Helix-breaking news: fighting crystalline starch energy deposits in the cell
    • Blennow A., Engelsen S.B. Helix-breaking news: fighting crystalline starch energy deposits in the cell. Trends Plant Sci. 2010, 15:236-240.
    • (2010) Trends Plant Sci. , vol.15 , pp. 236-240
    • Blennow, A.1    Engelsen, S.B.2
  • 4
    • 0032937953 scopus 로고    scopus 로고
    • Corpora-amylacea and the family of polyglucosan diseases
    • Cavanagh J.B. Corpora-amylacea and the family of polyglucosan diseases. Brain Res. Brain Res. Rev. 1999, 29:265-295.
    • (1999) Brain Res. Brain Res. Rev. , vol.29 , pp. 265-295
    • Cavanagh, J.B.1
  • 5
    • 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 A.A., Tagliabracci V.S., Segvich D.M., Meyer C.M., Irimia J.M., Roach P.J. Genetic depletion of the malin E3 ubiquitin ligase in mice leads to lafora bodies and the accumulation of insoluble laforin. J.Biol. Chem. 2010, 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    Roach, P.J.6
  • 6
    • 84958058043 scopus 로고    scopus 로고
    • Does abnormal glycogen structure contribute to increased susceptibility to seizures in epilepsy?
    • Published online March 19, 2014
    • Dinuzzo M., Mangia S., Maraviglia B., Giove F. Does abnormal glycogen structure contribute to increased susceptibility to seizures in epilepsy?. Metab. Brain Dis. 2014, Published online March 19, 2014. 10.1007/s11011-014-9524-5.
    • (2014) Metab. Brain Dis.
    • Dinuzzo, M.1    Mangia, S.2    Maraviglia, B.3    Giove, F.4
  • 7
    • 80052048669 scopus 로고    scopus 로고
    • Laforin, a dual specificity phosphatase involved in Lafora disease, is present mainly as monomeric form with full phosphatase activity
    • Dukhande V.V., Rogers D.M., Romá-Mateo C., Donderis J., Marina A., Taylor A.O., Sanz P., Gentry M.S. Laforin, a dual specificity phosphatase involved in Lafora disease, is present mainly as monomeric form with full phosphatase activity. PLoS ONE 2011, 6:e24040.
    • (2011) PLoS ONE , vol.6 , pp. e24040
    • Dukhande, V.V.1    Rogers, D.M.2    Romá-Mateo, C.3    Donderis, J.4    Marina, A.5    Taylor, A.O.6    Sanz, P.7    Gentry, M.S.8
  • 9
    • 84895091082 scopus 로고    scopus 로고
    • Pluralistic roles for glycogen in the central and peripheral nervous systems
    • Published online March 8, 2014
    • Fryer K.L., Brown A.M. Pluralistic roles for glycogen in the central and peripheral nervous systems. Metab. Brain Dis. 2014, Published online March 8, 2014. 10.1007/s11011-014-9516-5.
    • (2014) Metab. Brain Dis.
    • Fryer, K.L.1    Brown, A.M.2
  • 10
    • 0031100018 scopus 로고    scopus 로고
    • Microscopy of starch: evidence of a new level of granule organization
    • Gallant D.J., Bouchet B., Baldwin P.M. Microscopy of starch: evidence of a new level of granule organization. Carbohydr. Polym. 1997, 32:177-191.
    • (1997) Carbohydr. Polym. , vol.32 , pp. 177-191
    • Gallant, D.J.1    Bouchet, B.2    Baldwin, P.M.3
  • 11
    • 67651244247 scopus 로고    scopus 로고
    • Conservation of the glucan phosphatase laforin is linked to rates of molecular evolution and the glucan metabolism of the organism
    • Gentry M.S., Pace R.M. Conservation of the glucan phosphatase laforin is linked to rates of molecular evolution and the glucan metabolism of the organism. BMC Evol. Biol. 2009, 9:138.
    • (2009) BMC Evol. Biol. , vol.9 , pp. 138
    • Gentry, M.S.1    Pace, R.M.2
  • 12
    • 34547559799 scopus 로고    scopus 로고
    • The phosphatase laforin crosses evolutionary boundaries and links carbohydrate metabolism to neuronal disease
    • Gentry M.S., Dowen R.H., Worby C.A., Mattoo S., Ecker J.R., Dixon J.E. The phosphatase laforin crosses evolutionary boundaries and links carbohydrate metabolism to neuronal disease. J.Cell Biol. 2007, 178:477-488.
    • (2007) J.Cell Biol. , vol.178 , pp. 477-488
    • Gentry, M.S.1    Dowen, R.H.2    Worby, C.A.3    Mattoo, S.4    Ecker, J.R.5    Dixon, J.E.6
  • 13
    • 70449955237 scopus 로고    scopus 로고
    • Lafora disease: insights into neurodegeneration from plant metabolism
    • Gentry M.S., Dixon J.E., Worby C.A. Lafora disease: insights into neurodegeneration from plant metabolism. Trends Biochem. Sci. 2009, 34:628-639.
    • (2009) Trends Biochem. Sci. , vol.34 , pp. 628-639
    • Gentry, M.S.1    Dixon, J.E.2    Worby, C.A.3
  • 14
    • 70350068694 scopus 로고    scopus 로고
    • Structural insights into glucan phosphatase dynamics using amide hydrogen-deuterium exchange mass spectrometry
    • Hsu S., Kim Y., Li S., Durrant E.S., Pace R.M., Woods V.L., Gentry M.S. Structural insights into glucan phosphatase dynamics using amide hydrogen-deuterium exchange mass spectrometry. Biochemistry 2009, 48:9891-9902.
    • (2009) Biochemistry , vol.48 , pp. 9891-9902
    • Hsu, S.1    Kim, Y.2    Li, S.3    Durrant, E.S.4    Pace, R.M.5    Woods, V.L.6    Gentry, M.S.7
  • 15
    • 79954592899 scopus 로고    scopus 로고
    • Dimerization of Vaccinia virus VH1 is essential for dephosphorylation of STAT1 at tyrosine 701
    • Koksal A.C., Cingolani G. Dimerization of Vaccinia virus VH1 is essential for dephosphorylation of STAT1 at tyrosine 701. J.Biol. Chem. 2011, 286:14373-14382.
    • (2011) J.Biol. Chem. , vol.286 , pp. 14373-14382
    • Koksal, A.C.1    Cingolani, G.2
  • 17
    • 33645970231 scopus 로고    scopus 로고
    • Familial Wolff-Parkinson-White Syndrome: a disease of glycogen storage or ion channel dysfunction?
    • Light P.E. Familial Wolff-Parkinson-White Syndrome: a disease of glycogen storage or ion channel dysfunction?. J.Cardiovasc. Electrophysiol. 2006, 17(1):S158-S161.
    • (2006) J.Cardiovasc. Electrophysiol. , vol.17 , Issue.1 , pp. S158-S161
    • Light, P.E.1
  • 18
    • 33846025444 scopus 로고    scopus 로고
    • Dimerization of Laforin is required for its optimal phosphatase activity, regulation of GSK3beta phosphorylation, and Wnt signaling
    • Liu Y., Wang Y., Wu C., Liu Y., Zheng P. Dimerization of Laforin is required for its optimal phosphatase activity, regulation of GSK3beta phosphorylation, and Wnt signaling. J.Biol. Chem. 2006, 281:34768-34774.
    • (2006) J.Biol. Chem. , vol.281 , pp. 34768-34774
    • Liu, Y.1    Wang, Y.2    Wu, C.3    Liu, Y.4    Zheng, P.5
  • 19
    • 67649859658 scopus 로고    scopus 로고
    • Deletions and missense mutations of EPM2A exacerbate unfolded protein response and apoptosis of neuronal cells induced by endoplasm reticulum stress
    • Liu Y., Wang Y., Wu C., Liu Y., Zheng P. Deletions and missense mutations of EPM2A exacerbate unfolded protein response and apoptosis of neuronal cells induced by endoplasm reticulum stress. Hum. Mol. Genet. 2009, 18:2622-2631.
    • (2009) Hum. Mol. Genet. , vol.18 , pp. 2622-2631
    • Liu, Y.1    Wang, Y.2    Wu, C.3    Liu, Y.4    Zheng, P.5
  • 25
    • 58249089943 scopus 로고    scopus 로고
    • Evolution of protein phosphatases in plants and animals
    • Moorhead G.B., De Wever V., Templeton G., Kerk D. Evolution of protein phosphatases in plants and animals. Biochem. J. 2009, 417:401-409.
    • (2009) Biochem. J. , vol.417 , pp. 401-409
    • Moorhead, G.B.1    De Wever, V.2    Templeton, G.3    Kerk, D.4
  • 28
    • 0037380981 scopus 로고    scopus 로고
    • Immunocytochemical localization of glycogen phosphorylase isozymes in rat nervous tissues by using isozyme-specific antibodies
    • Pfeiffer-Guglielmi B., Fleckenstein B., Jung G., Hamprecht B. Immunocytochemical localization of glycogen phosphorylase isozymes in rat nervous tissues by using isozyme-specific antibodies. J.Neurochem. 2003, 85:73-81.
    • (2003) J.Neurochem. , vol.85 , pp. 73-81
    • Pfeiffer-Guglielmi, B.1    Fleckenstein, B.2    Jung, G.3    Hamprecht, B.4
  • 29
    • 34249024007 scopus 로고    scopus 로고
    • Structure-assisted discovery of Variola major H1 phosphatase inhibitors
    • Phan J., Tropea J.E., Waugh D.S. Structure-assisted discovery of Variola major H1 phosphatase inhibitors. Acta Crystallogr. D Biol. Crystallogr. 2007, 63:698-704.
    • (2007) Acta Crystallogr. D Biol. Crystallogr. , vol.63 , pp. 698-704
    • Phan, J.1    Tropea, J.E.2    Waugh, D.S.3
  • 30
    • 0036079974 scopus 로고    scopus 로고
    • Glycogen and its metabolism
    • Roach P.J. Glycogen and its metabolism. Curr. Mol. Med. 2002, 2:101-120.
    • (2002) Curr. Mol. Med. , vol.2 , pp. 101-120
    • Roach, P.J.1
  • 32
    • 84870519496 scopus 로고    scopus 로고
    • Linking glycogen and senescence in cancer cells
    • Ros S., Schulze A. Linking glycogen and senescence in cancer cells. Cell Metab. 2012, 16:687-688.
    • (2012) Cell Metab. , vol.16 , pp. 687-688
    • Ros, S.1    Schulze, A.2
  • 37
    • 84873334806 scopus 로고    scopus 로고
    • A malachite green-based assay to assess glucan phosphatase activity
    • Sherwood A.R., Paasch B.C., Worby C.A., Gentry M.S. A malachite green-based assay to assess glucan phosphatase activity. Anal. Biochem. 2013, 435:54-56.
    • (2013) Anal. Biochem. , vol.435 , pp. 54-56
    • Sherwood, A.R.1    Paasch, B.C.2    Worby, C.A.3    Gentry, M.S.4
  • 38
    • 84903618324 scopus 로고    scopus 로고
    • Phosphoglucan phosphatase function sheds light on starch degradation
    • Silver D.M., Kötting O., Moorhead G.B. Phosphoglucan phosphatase function sheds light on starch degradation. Trends Plant Sci. 2014, 19:471-478.
    • (2014) Trends Plant Sci. , vol.19 , pp. 471-478
    • Silver, D.M.1    Kötting, O.2    Moorhead, G.B.3
  • 40
  • 41
    • 0027058922 scopus 로고
    • Physiologic coupling of glial glycogen metabolism to neuronal activity in brain
    • Swanson R.A. Physiologic coupling of glial glycogen metabolism to neuronal activity in brain. Can. J. Physiol. Pharmacol. 1992, 70:S138-S144.
    • (1992) Can. J. Physiol. Pharmacol. , vol.70 , pp. S138-S144
    • Swanson, R.A.1
  • 45
    • 33750299450 scopus 로고    scopus 로고
    • Protein tyrosine phosphatases: from genes, to function, to disease
    • Tonks N.K. Protein tyrosine phosphatases: from genes, to function, to disease. Nat. Rev. Mol. Cell Biol. 2006, 7:833-846.
    • (2006) Nat. Rev. Mol. Cell Biol. , vol.7 , pp. 833-846
    • Tonks, N.K.1
  • 46
    • 84872759784 scopus 로고    scopus 로고
    • Protein tyrosine phosphatases-from housekeeping enzymes to master regulators of signal transduction
    • Tonks N.K. Protein tyrosine phosphatases-from housekeeping enzymes to master regulators of signal transduction. FEBS J. 2013, 280:346-378.
    • (2013) FEBS J. , vol.280 , pp. 346-378
    • Tonks, N.K.1
  • 51
    • 0037169553 scopus 로고    scopus 로고
    • A unique carbohydrate binding domain targets the lafora disease phosphatase to glycogen
    • Wang J., Stuckey J.A., Wishart M.J., Dixon J.E. A unique carbohydrate binding domain targets the lafora disease phosphatase to glycogen. J.Biol. Chem. 2002, 277:2377-2380.
    • (2002) J.Biol. Chem. , vol.277 , pp. 2377-2380
    • Wang, J.1    Stuckey, J.A.2    Wishart, M.J.3    Dixon, J.E.4
  • 52
    • 33749620777 scopus 로고    scopus 로고
    • Laforin, a dual specificity phosphatase that dephosphorylates complex carbohydrates
    • Worby C.A., Gentry M.S., Dixon J.E. Laforin, a dual specificity phosphatase that dephosphorylates complex carbohydrates. J.Biol. Chem. 2006, 281:30412-30418.
    • (2006) J.Biol. Chem. , vol.281 , pp. 30412-30418
    • Worby, C.A.1    Gentry, M.S.2    Dixon, J.E.3
  • 53
    • 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. Studies in myoclonus epilepsy (Lafora body form). I. Isolation and preliminary characterization of Lafora bodies in two cases. Arch. Neurol. 1968, 19:15-33.
    • (1968) Arch. Neurol. , vol.19 , pp. 15-33
    • Yokoi, S.1    Austin, J.2    Witmer, F.3    Sakai, M.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.