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Volumn 289, Issue 30, 2014, Pages 20606-20614

Protein degradation and quality control in cells from laforin and malin knockout mice

Author keywords

[No Author keywords available]

Indexed keywords

DDIT3 PROTEIN, MOUSE; DUAL SPECIFICITY PHOSPHATASE; EPM2A PROTEIN, MOUSE; GROWTH ARREST AND DNA DAMAGE INDUCIBLE PROTEIN 153; LAMP1 PROTEIN, MOUSE; LYSOSOME ASSOCIATED MEMBRANE PROTEIN; NHLRC1 PROTEIN, MOUSE; PROTEASOME; UBIQUITIN PROTEIN LIGASE;

EID: 84905365244     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M114.580167     Document Type: Article
Times cited : (31)

References (46)
  • 1
    • 0004452545 scopus 로고
    • Progressive familial myoclonic epilepsy in three families: Its clinical features and pathological basis
    • Harriman, D. G., Millar, J. H., and Stevenson, A. C. (1955) Progressive familial myoclonic epilepsy in three families: its clinical features and pathological basis. Brain 78, 325-349
    • (1955) Brain , vol.78 , pp. 325-349
    • Harriman, D.G.1    Millar, J.H.2    Stevenson, A.C.3
  • 2
    • 0034907260 scopus 로고    scopus 로고
    • Lafora's disease: Towards a clinical, pathologic, and molecular synthesis
    • Minassian, B. A. (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
  • 3
    • 0023005321 scopus 로고
    • Progressive myoclonus epilepsies: Specific causes and diagnosis
    • Berkovic, S. F., Andermann, F., Carpenter, S., and Wolfe, L. S. (1986) Progressive myoclonus epilepsies: specific causes and diagnosis. N. Engl. J. Med. 315, 296-305
    • (1986) N. Engl. J. Med. , vol.315 , pp. 296-305
    • Berkovic, S.F.1    Andermann, F.2    Carpenter, S.3    Wolfe, L.S.4
  • 4
    • 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., and 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
  • 5
    • 51849175000 scopus 로고
    • Contribution on the histopathology of myoclonic epilepsies
    • Lafora, G. R., and Glueck, B. (1911) Contribution on the histopathology of myoclonic epilepsies. Z Gesamte Neurol. Psychiatr. 6, 1-14
    • (1911) Z Gesamte Neurol. Psychiatr. , vol.6 , pp. 1-14
    • Lafora, G.R.1    Glueck, B.2
  • 6
    • 0036079974 scopus 로고    scopus 로고
    • Glycogen and its metabolism
    • Roach, P. J. (2002) Glycogen and its metabolism. Curr. Mol. Med. 2, 101-120
    • (2002) Curr. Mol. Med. , vol.2 , pp. 101-120
    • Roach, P.J.1
  • 7
    • 84855929671 scopus 로고    scopus 로고
    • Glycogen and its metabolism: Some new developments and old themes
    • Roach, P. J., Depaoli-Roach, A. A., Hurley, T. D., and Tagliabracci, V. S. (2012) Glycogen and its metabolism: some new developments and old themes. Biochem. J. 441, 763-787
    • (2012) Biochem. J. , vol.441 , pp. 763-787
    • Roach, P.J.1    Depaoli-Roach, A.A.2    Hurley, T.D.3    Tagliabracci, V.S.4
  • 8
    • 0036214086 scopus 로고    scopus 로고
    • Glycogen storage disease
    • Kannourakis, G. (2002) Glycogen storage disease. Semin. Hematol. 39, 103-106
    • (2002) Semin. Hematol. , vol.39 , pp. 103-106
    • Kannourakis, G.1
  • 9
    • 33749250737 scopus 로고    scopus 로고
    • Glycogen storage disease: Clinical, biochemical, and molecular heterogeneity
    • Shin, Y. S. (2006) Glycogen storage disease: clinical, biochemical, and molecular heterogeneity. Semin. Pediatr. Neurol. 13, 115-120
    • (2006) Semin. Pediatr. Neurol. , vol.13 , pp. 115-120
    • Shin, Y.S.1
  • 13
    • 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., and Roach, P. J. (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    Roach, P.J.6
  • 16
    • 20844463813 scopus 로고    scopus 로고
    • Insights into Lafora disease: Malin is an E3 ubiquitin ligase that ubiquitinates and promotes the degradation of laforin
    • Gentry, M. S., Worby, C. A., and Dixon, J. E. (2005) Insights into Lafora disease: malin is an E3 ubiquitin ligase that ubiquitinates and promotes the degradation of laforin. Proc. Natl. Acad. Sci. U. S. A. 102, 8501-8506
    • (2005) Proc. Natl. Acad. Sci. U. S. A. , vol.102 , pp. 8501-8506
    • Gentry, M.S.1    Worby, C.A.2    Dixon, J.E.3
  • 18
    • 42949086604 scopus 로고    scopus 로고
    • Malin decreases glycogen accumulation by promoting the degradation of protein targeting to glycogen (PTG)
    • Worby, C. A., Gentry, M. S., and Dixon, J. E. (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
  • 19
    • 34948889895 scopus 로고    scopus 로고
    • A role for AGL ubiquitination in the glycogen storage disorders of Lafora and Cori's disease
    • Cheng, A., Zhang, M., Gentry, M. S., Worby, C. A., Dixon, J. E., and Saltiel, A. R. (2007) A role for AGL ubiquitination in the glycogen storage disorders of Lafora and Cori's disease. Genes Dev. 21, 2399-2409
    • (2007) Genes Dev. , vol.21 , pp. 2399-2409
    • Cheng, A.1    Zhang, M.2    Gentry, M.S.3    Worby, C.A.4    Dixon, J.E.5    Saltiel, A.R.6
  • 20
    • 84901318614 scopus 로고    scopus 로고
    • Glycogen accumulation underlies neurodegeneration and autophagy impairment in Lafora disease
    • Duran, J., Gruart, A., García-Rocha, M., Delgado-García, J. M., and Guinovart, J. J. (2014) Glycogen accumulation underlies neurodegeneration and autophagy impairment in Lafora disease. Hum. Mol. Genet. 23, 3147-3156
    • (2014) Hum. Mol. Genet. , vol.23 , pp. 3147-3156
    • Duran, J.1    Gruart, A.2    García-Rocha, M.3    Delgado-García, J.M.4    Guinovart, J.J.5
  • 22
    • 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, P. K., Puri, R., Mittal, S., Sengupta, S., Parihar, R., and Ganesh, S. (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    Sengupta, S.6    Parihar, R.7    Ganesh, S.8
  • 28
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford, M. M. (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72, 248-254
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 30
    • 0000440206 scopus 로고
    • D-glucose: UV methods with hexokinase and glucose-6-phosphate dehydrogenase
    • Bergmeyer, H. U., ed.., 3rd Ed., Verlag Chemie, Weinheim, Germany
    • Kunst, A., Draeger, B., and Ziegenhorn, J. (1984) in Methods of Enzymatic Analysis (Bergmeyer, H. U., ed.). D-glucose: UV methods with hexokinase and glucose-6-phosphate dehydrogenase. Vol. 6, 3rd Ed., pp. 163-172, Verlag Chemie, Weinheim, Germany
    • (1984) Methods of Enzymatic Analysis , vol.6 , pp. 163-172
    • Kunst, A.1    Draeger, B.2    Ziegenhorn, J.3
  • 31
    • 33746108329 scopus 로고    scopus 로고
    • Lysosomal turnover, but not a cellular level, of endogenous LC3 is a marker for autophagy
    • Tanida, I., Minematsu-Ikeguchi, N., Ueno, T., and Kominami, E. (2005) Lysosomal turnover, but not a cellular level, of endogenous LC3 is a marker for autophagy. Autophagy 1, 84-91
    • (2005) Autophagy , vol.1 , pp. 84-91
    • Tanida, I.1    Minematsu-Ikeguchi, N.2    Ueno, T.3    Kominami, E.4
  • 33
    • 0032512636 scopus 로고    scopus 로고
    • Tor, a phosphatidylinositol kinase homologue, controls autophagy in yeast
    • Noda, T., and Ohsumi, Y. (1998) Tor, a phosphatidylinositol kinase homologue, controls autophagy in yeast. J. Biol. Chem. 273, 3963-3966
    • (1998) J. Biol. Chem. , vol.273 , pp. 3963-3966
    • Noda, T.1    Ohsumi, Y.2
  • 34
    • 4344563878 scopus 로고    scopus 로고
    • Role and regulation of starvation-induced autophagy in the Drosophila fat body
    • Scott, R. C., Schuldiner, O., and Neufeld, T. P. (2004) Role and regulation of starvation-induced autophagy in the Drosophila fat body. Dev. Cell 7, 167-178
    • (2004) Dev. Cell , vol.7 , pp. 167-178
    • Scott, R.C.1    Schuldiner, O.2    Neufeld, T.P.3
  • 35
    • 80053338210 scopus 로고    scopus 로고
    • Starch-binding domaincontaining protein 1 (Stbd1) and glycogen metabolism: Identification of the Atg8 family interacting motif (AIM) in Stbd1 required for interaction with GABARAPL1
    • Jiang, S., Wells, C. D., and Roach, P. J. (2011) Starch-binding domaincontaining protein 1 (Stbd1) and glycogen metabolism: identification of the Atg8 family interacting motif (AIM) in Stbd1 required for interaction with GABARAPL1. Biochem. Biophys. Res. Commun. 413, 420-425
    • (2011) Biochem. Biophys. Res. Commun. , vol.413 , pp. 420-425
    • Jiang, S.1    Wells, C.D.2    Roach, P.J.3
  • 37
    • 27144529182 scopus 로고    scopus 로고
    • Ubiquitylation and cell signaling
    • Haglund, K., and Dikic, I. (2005) Ubiquitylation and cell signaling. EMBO J. 24, 3353-3359
    • (2005) EMBO J. , vol.24 , pp. 3353-3359
    • Haglund, K.1    Dikic, I.2
  • 38
    • 67650110001 scopus 로고    scopus 로고
    • Increased endoplasmic reticulum stress and decreased proteasomal function in lafora disease models lacking the phosphatase laforin
    • Vernia, S., Rubio, T., Heredia, M., Rodríguez de Córdoba, S., and Sanz, P. (2009) Increased endoplasmic reticulum stress and decreased proteasomal function in lafora disease models lacking the phosphatase laforin. PLoS ONE 4, e5907
    • (2009) PLoS ONE , vol.4
    • Vernia, S.1    Rubio, T.2    Heredia, M.3    Rodríguez De Córdoba, S.4    Sanz, P.5
  • 39
    • 0032054744 scopus 로고    scopus 로고
    • CHOP is implicated in programmed cell death in response to impaired function of the endoplasmic reticulum
    • Zinszner, H., Kuroda, M., Wang, X., Batchvarova, N., Lightfoot, R. T., Remotti, H., Stevens, J. L., and Ron, D. (1998) CHOP is implicated in programmed cell death in response to impaired function of the endoplasmic reticulum. Genes Dev. 12, 982-995
    • (1998) Genes Dev. , vol.12 , pp. 982-995
    • Zinszner, H.1    Kuroda, M.2    Wang, X.3    Batchvarova, N.4    Lightfoot, R.T.5    Remotti, H.6    Stevens, J.L.7    Ron, D.8
  • 40
    • 67649760225 scopus 로고    scopus 로고
    • AMP-activated protein kinase phosphorylates R5/PTG, the glycogen targeting subunit of the R5/PTG-protein phosphatase 1 holoenzyme, and accelerates its down-regulation by the laforin-malin complex
    • Vernia, S., Solaz-Fuster, M. C., Gimeno-Alcañiz, J. V., Rubio, T., García-Haro, L., Foretz, M., de Córdoba, S. R., and Sanz, P. (2009) AMP-activated protein kinase phosphorylates R5/PTG, the glycogen targeting subunit of the R5/PTG-protein phosphatase 1 holoenzyme, and accelerates its down-regulation by the laforin-malin complex. J. Biol. Chem. 284, 8247-8255
    • (2009) J. Biol. Chem. , vol.284 , pp. 8247-8255
    • Vernia, S.1    Solaz-Fuster, M.C.2    Gimeno-Alcañiz, J.V.3    Rubio, T.4    García-Haro, L.5    Foretz, M.6    De Córdoba, S.R.7    Sanz, P.8
  • 41
    • 79961127916 scopus 로고    scopus 로고
    • Lafora disease ubiquitin ligase malin promotes proteasomal degradation of neuronatin and regulates glycogen synthesis
    • Sharma, J., Rao, S. N., Shankar, S. K., Satishchandra, P., and Jana, N. R. (2011) Lafora disease ubiquitin ligase malin promotes proteasomal degradation of neuronatin and regulates glycogen synthesis. Neurobiol. Dis. 44, 133-141
    • (2011) Neurobiol. Dis. , vol.44 , pp. 133-141
    • Sharma, J.1    Rao, S.N.2    Shankar, S.K.3    Satishchandra, P.4    Jana, N.R.5
  • 43
    • 83455206095 scopus 로고    scopus 로고
    • Dysfunctions in endosomal-lysosomal and autophagy pathways underlie neuropathology in a mouse model for Lafora disease
    • Puri, R., Suzuki, T., Yamakawa, K., and Ganesh, S. (2012) Dysfunctions in endosomal-lysosomal and autophagy pathways underlie neuropathology in a mouse model for Lafora disease. Hum. Mol. Genet. 21, 175-184
    • (2012) Hum. Mol. Genet. , vol.21 , pp. 175-184
    • Puri, R.1    Suzuki, T.2    Yamakawa, K.3    Ganesh, S.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.