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Volumn 82, Issue , 2015, Pages 281-288

Differential recruitment of UBQLN2 to nuclear inclusions in the polyglutamine diseases HD and SCA3

Author keywords

Huntington's disease; Polyglutamine; SCA3; UBA; UBL; UBQLN2

Indexed keywords

ADAPTOR PROTEIN; ATAXIN 3; HUNTINGTIN; PROTEIN P62; UBIQUILIN 1; UBIQUILIN 2; UBIQUITIN; UNCLASSIFIED DRUG; ATXN3 PROTEIN, HUMAN; CELL CYCLE PROTEIN; HTT PROTEIN, HUMAN; NERVE PROTEIN; REPRESSOR PROTEIN; UBQLN2 PROTEIN, HUMAN; UBQLN2 PROTEIN, MOUSE; VESICULAR TRANSPORT ADAPTOR PROTEIN;

EID: 84936857047     PISSN: 09699961     EISSN: 1095953X     Source Type: Journal    
DOI: 10.1016/j.nbd.2015.06.017     Document Type: Article
Times cited : (23)

References (39)
  • 1
    • 84862756869 scopus 로고    scopus 로고
    • Pattern of ubiquilin pathology in ALS and FTLD indicates presence of C9ORF72 hexanucleotide expansion
    • Brettschneider J., et al. Pattern of ubiquilin pathology in ALS and FTLD indicates presence of C9ORF72 hexanucleotide expansion. Acta Neuropathol. 2012, 123:825-839.
    • (2012) Acta Neuropathol. , vol.123 , pp. 825-839
    • Brettschneider, J.1
  • 2
    • 0036566229 scopus 로고    scopus 로고
    • YAC transgenic mice carrying pathological alleles of the MJD1 locus exhibit a mild and slowly progressive cerebellar deficit
    • Cemal C.K., et al. YAC transgenic mice carrying pathological alleles of the MJD1 locus exhibit a mild and slowly progressive cerebellar deficit. Hum. Mol. Genet. 2002, 11:1075-1094.
    • (2002) Hum. Mol. Genet. , vol.11 , pp. 1075-1094
    • Cemal, C.K.1
  • 3
    • 0037047123 scopus 로고    scopus 로고
    • Live-cell imaging reveals divergent intracellular dynamics of polyglutamine disease proteins and supports a sequestration model of pathogenesis
    • Chai Y., et al. Live-cell imaging reveals divergent intracellular dynamics of polyglutamine disease proteins and supports a sequestration model of pathogenesis. Proc. Natl. Acad. Sci. U. S. A. 2002, 99:9310-9315.
    • (2002) Proc. Natl. Acad. Sci. U. S. A. , vol.99 , pp. 9310-9315
    • Chai, Y.1
  • 4
    • 84885023000 scopus 로고    scopus 로고
    • Toward RNAi therapy for the polyglutamine disease Machado-Joseph disease
    • Costa Mdo C., et al. Toward RNAi therapy for the polyglutamine disease Machado-Joseph disease. Mol. Ther. 2013, 21:1898-1908.
    • (2013) Mol. Ther. , vol.21 , pp. 1898-1908
    • Costa, M.C.1
  • 5
    • 80052580969 scopus 로고    scopus 로고
    • Mutations in UBQLN2 cause dominant X-linked juvenile and adult-onset ALS and ALS/dementia
    • Deng H.X., et al. Mutations in UBQLN2 cause dominant X-linked juvenile and adult-onset ALS and ALS/dementia. Nature 2011, 477:211-215.
    • (2011) Nature , vol.477 , pp. 211-215
    • Deng, H.X.1
  • 6
    • 3342879140 scopus 로고    scopus 로고
    • Identification of ubiquitin-interacting proteins in purified polyglutamine aggregates
    • Doi H., et al. Identification of ubiquitin-interacting proteins in purified polyglutamine aggregates. FEBS Lett. 2004, 571:171-176.
    • (2004) FEBS Lett. , vol.571 , pp. 171-176
    • Doi, H.1
  • 7
    • 84936858964 scopus 로고    scopus 로고
    • ALS-linked mutations in ubiquilin-2 or hnRNPA1 reduce interaction between ubiquilin-2 and hnRNPA1
    • Gilpin K.M., et al. ALS-linked mutations in ubiquilin-2 or hnRNPA1 reduce interaction between ubiquilin-2 and hnRNPA1. Hum. Mol. Genet. 2015, 24:2565-2577.
    • (2015) Hum. Mol. Genet. , vol.24 , pp. 2565-2577
    • Gilpin, K.M.1
  • 8
    • 33751514845 scopus 로고    scopus 로고
    • The UBL domain of PLIC-1 regulates aggresome formation
    • Heir R., et al. The UBL domain of PLIC-1 regulates aggresome formation. EMBO Rep. 2006, 7:1252-1258.
    • (2006) EMBO Rep. , vol.7 , pp. 1252-1258
    • Heir, R.1
  • 9
    • 77956514970 scopus 로고    scopus 로고
    • Early autophagic response in a novel knock-in model of Huntington disease
    • Heng M.Y., et al. Early autophagic response in a novel knock-in model of Huntington disease. Hum. Mol. Genet. 2010, 19:3702-3720.
    • (2010) Hum. Mol. Genet. , vol.19 , pp. 3702-3720
    • Heng, M.Y.1
  • 10
    • 0033636785 scopus 로고    scopus 로고
    • The hPLIC proteins may provide a link between the ubiquitination machinery and the proteasome
    • Kleijnen M.F., et al. The hPLIC proteins may provide a link between the ubiquitination machinery and the proteasome. Mol. Cell 2000, 6:409-419.
    • (2000) Mol. Cell , vol.6 , pp. 409-419
    • Kleijnen, M.F.1
  • 11
    • 2442520399 scopus 로고    scopus 로고
    • Ubiquilin interacts with ubiquitylated proteins and proteasome through its ubiquitin-associated and ubiquitin-like domains
    • Ko H.S., et al. Ubiquilin interacts with ubiquitylated proteins and proteasome through its ubiquitin-associated and ubiquitin-like domains. FEBS Lett. 2004, 566:110-114.
    • (2004) FEBS Lett. , vol.566 , pp. 110-114
    • Ko, H.S.1
  • 12
    • 84861356966 scopus 로고    scopus 로고
    • Ubiquilins in the crosstalk among proteolytic pathways
    • Lee D.Y., Brown E.J. Ubiquilins in the crosstalk among proteolytic pathways. Biol. Chem. 2012, 393:441-447.
    • (2012) Biol. Chem. , vol.393 , pp. 441-447
    • Lee, D.Y.1    Brown, E.J.2
  • 13
    • 70449723717 scopus 로고    scopus 로고
    • Ubiquilin and p97/VCP bind erasin, forming a complex involved in ERAD
    • Lim P.J., et al. Ubiquilin and p97/VCP bind erasin, forming a complex involved in ERAD. J. Cell Biol. 2009, 187:201-217.
    • (2009) J. Cell Biol. , vol.187 , pp. 201-217
    • Lim, P.J.1
  • 14
    • 0035862896 scopus 로고    scopus 로고
    • Neurological abnormalities in a knock-in mouse model of Huntington's disease
    • Lin C.H., et al. Neurological abnormalities in a knock-in mouse model of Huntington's disease. Hum. Mol. Genet. 2001, 10:137-144.
    • (2001) Hum. Mol. Genet. , vol.10 , pp. 137-144
    • Lin, C.H.1
  • 15
    • 0034645063 scopus 로고    scopus 로고
    • Identification of ubiquilin, a novel presenilin interactor that increases presenilin protein accumulation
    • Mah A.L., et al. Identification of ubiquilin, a novel presenilin interactor that increases presenilin protein accumulation. J. Cell Biol. 2000, 151:847-862.
    • (2000) J. Cell Biol. , vol.151 , pp. 847-862
    • Mah, A.L.1
  • 16
    • 84862765926 scopus 로고    scopus 로고
    • Ubiquilin immunoreactivity in cytoplasmic and nuclear inclusions in synucleinopathies, polyglutamine diseases and intranuclear inclusion body disease
    • Mori F., et al. Ubiquilin immunoreactivity in cytoplasmic and nuclear inclusions in synucleinopathies, polyglutamine diseases and intranuclear inclusion body disease. Acta Neuropathol. 2012, 124:149-151.
    • (2012) Acta Neuropathol. , vol.124 , pp. 149-151
    • Mori, F.1
  • 17
    • 79957947433 scopus 로고    scopus 로고
    • Removing protein aggregates: the role of proteolysis in neurodegeneration
    • Nijholt D.A., et al. Removing protein aggregates: the role of proteolysis in neurodegeneration. Curr. Med. Chem. 2011, 18:2459-2476.
    • (2011) Curr. Med. Chem. , vol.18 , pp. 2459-2476
    • Nijholt, D.A.1
  • 18
    • 84884634935 scopus 로고    scopus 로고
    • Ubiquilin 2 is not associated with tau pathology
    • e76598
    • Nolle A., et al. Ubiquilin 2 is not associated with tau pathology. PLoS One 2013, 8:e76598.
    • (2013) PLoS One , vol.8
    • Nolle, A.1
  • 19
    • 0034737293 scopus 로고    scopus 로고
    • Reversing neurodegeneration: a promise unfolds
    • Orr H.T., Zoghbi H.Y. Reversing neurodegeneration: a promise unfolds. Cell 2000, 101:1-4.
    • (2000) Cell , vol.101 , pp. 1-4
    • Orr, H.T.1    Zoghbi, H.Y.2
  • 20
    • 84935851738 scopus 로고    scopus 로고
    • Evidence of a link between ubiquilin 2 and optineurin in amyotrophic lateral sclerosis
    • Osaka M., et al. Evidence of a link between ubiquilin 2 and optineurin in amyotrophic lateral sclerosis. Hum. Mol. Genet. 2014, 1617-1629.
    • (2014) Hum. Mol. Genet. , pp. 1617-1629
    • Osaka, M.1
  • 21
    • 0030850412 scopus 로고    scopus 로고
    • Intranuclear inclusions of expanded polyglutamine protein in spinocerebellar ataxia type 3
    • Paulson H.L., et al. Intranuclear inclusions of expanded polyglutamine protein in spinocerebellar ataxia type 3. Neuron 1997, 19:333-344.
    • (1997) Neuron , vol.19 , pp. 333-344
    • Paulson, H.L.1
  • 22
    • 84924488574 scopus 로고    scopus 로고
    • A knock-in mouse model of spinocerebellar ataxia type 3 exhibits prominent aggregate pathology and aberrant splicing of the disease gene transcript
    • Ramani B., et al. A knock-in mouse model of spinocerebellar ataxia type 3 exhibits prominent aggregate pathology and aberrant splicing of the disease gene transcript. Hum. Mol. Genet. 2014, 1211-1224.
    • (2014) Hum. Mol. Genet. , pp. 1211-1224
    • Ramani, B.1
  • 23
    • 77955023765 scopus 로고    scopus 로고
    • Ubiquilin functions in autophagy and is degraded by chaperone-mediated autophagy
    • Rothenberg C., et al. Ubiquilin functions in autophagy and is degraded by chaperone-mediated autophagy. Hum. Mol. Genet. 2010, 19:3219-3232.
    • (2010) Hum. Mol. Genet. , vol.19 , pp. 3219-3232
    • Rothenberg, C.1
  • 24
    • 33750363298 scopus 로고    scopus 로고
    • The roles of intracellular protein-degradation pathways in neurodegeneration
    • Rubinsztein D.C. The roles of intracellular protein-degradation pathways in neurodegeneration. Nature 2006, 443:780-786.
    • (2006) Nature , vol.443 , pp. 780-786
    • Rubinsztein, D.C.1
  • 25
    • 84880325702 scopus 로고    scopus 로고
    • Unbiased screen reveals ubiquilin-1 and -2 highly associated with huntingtin inclusions
    • Rutherford N.J., et al. Unbiased screen reveals ubiquilin-1 and -2 highly associated with huntingtin inclusions. Brain Res. 2013, 1524:62-73.
    • (2013) Brain Res. , vol.1524 , pp. 62-73
    • Rutherford, N.J.1
  • 26
    • 84898728074 scopus 로고    scopus 로고
    • Ubiquilin-1 overexpression increases the lifespan and delays accumulation of Huntingtin aggregates in the R6/2 mouse model of Huntington's disease
    • e87513
    • Safren N., et al. Ubiquilin-1 overexpression increases the lifespan and delays accumulation of Huntingtin aggregates in the R6/2 mouse model of Huntington's disease. PLoS One 2014, 9:e87513.
    • (2014) PLoS One , vol.9
    • Safren, N.1
  • 27
    • 84923233814 scopus 로고    scopus 로고
    • Signature changes in ubiquilin expression in the R6/2 mouse model of Huntington's disease
    • Safren N., et al. Signature changes in ubiquilin expression in the R6/2 mouse model of Huntington's disease. Brain Res. 2015, 1597:37-46.
    • (2015) Brain Res. , vol.1597 , pp. 37-46
    • Safren, N.1
  • 28
    • 84884660504 scopus 로고    scopus 로고
    • Ubiquilin-1 immunoreactivity is concentrated on Hirano bodies and dystrophic neurites in Alzheimer's disease brains
    • Satoh J., et al. Ubiquilin-1 immunoreactivity is concentrated on Hirano bodies and dystrophic neurites in Alzheimer's disease brains. Neuropathol. Appl. Neurobiol. 2013, 39:817-830.
    • (2013) Neuropathol. Appl. Neurobiol. , vol.39 , pp. 817-830
    • Satoh, J.1
  • 29
    • 80053927521 scopus 로고    scopus 로고
    • Ubiquilin-1 is a molecular chaperone for the amyloid precursor protein
    • Stieren E.S., et al. Ubiquilin-1 is a molecular chaperone for the amyloid precursor protein. J. Biol. Chem. 2011, 286:35689-35698.
    • (2011) J. Biol. Chem. , vol.286 , pp. 35689-35698
    • Stieren, E.S.1
  • 30
    • 79751480230 scopus 로고    scopus 로고
    • Alzheimer's disease-associated ubiquilin-1 regulates presenilin-1 accumulation and aggresome formation
    • Viswanathan J., et al. Alzheimer's disease-associated ubiquilin-1 regulates presenilin-1 accumulation and aggresome formation. Traffic 2011, 12:330-348.
    • (2011) Traffic , vol.12 , pp. 330-348
    • Viswanathan, J.1
  • 31
    • 0037065732 scopus 로고    scopus 로고
    • Structural studies of the interaction between ubiquitin family proteins and proteasome subunit S5a
    • Walters K.J., et al. Structural studies of the interaction between ubiquitin family proteins and proteasome subunit S5a. Biochemistry 2002, 41:1767-1777.
    • (2002) Biochemistry , vol.41 , pp. 1767-1777
    • Walters, K.J.1
  • 32
    • 34447095637 scopus 로고    scopus 로고
    • Ubiquilin interacts and enhances the degradation of expanded-polyglutamine proteins
    • Wang H., Monteiro M.J. Ubiquilin interacts and enhances the degradation of expanded-polyglutamine proteins. Biochem. Biophys. Res. Commun. 2007, 360:423-427.
    • (2007) Biochem. Biophys. Res. Commun. , vol.360 , pp. 423-427
    • Wang, H.1    Monteiro, M.J.2
  • 33
    • 33644771265 scopus 로고    scopus 로고
    • Suppression of polyglutamine-induced toxicity in cell and animal models of Huntington's disease by ubiquilin
    • Wang H., et al. Suppression of polyglutamine-induced toxicity in cell and animal models of Huntington's disease by ubiquilin. Hum. Mol. Genet. 2006, 15:1025-1041.
    • (2006) Hum. Mol. Genet. , vol.15 , pp. 1025-1041
    • Wang, H.1
  • 34
    • 0033213325 scopus 로고    scopus 로고
    • Ubiquitin-related proteins regulate interaction of vimentin intermediate filaments with the plasma membrane
    • Wu A.L., et al. Ubiquitin-related proteins regulate interaction of vimentin intermediate filaments with the plasma membrane. Mol. Cell 1999, 4:619-625.
    • (1999) Mol. Cell , vol.4 , pp. 619-625
    • Wu, A.L.1
  • 35
    • 33846696670 scopus 로고    scopus 로고
    • Ubiquitin ligase Hrd1 enhances the degradation and suppresses the toxicity of polyglutamine-expanded huntingtin
    • Yang H., et al. Ubiquitin ligase Hrd1 enhances the degradation and suppresses the toxicity of polyglutamine-expanded huntingtin. Exp. Cell Res. 2007, 313:538-550.
    • (2007) Exp. Cell Res. , vol.313 , pp. 538-550
    • Yang, H.1
  • 36
    • 84863454044 scopus 로고    scopus 로고
    • Laforin is required for the functional activation of malin in endoplasmic reticulum stress resistance in neuronal cells
    • Zeng L., et al. Laforin is required for the functional activation of malin in endoplasmic reticulum stress resistance in neuronal cells. FEBS J. 2012, 279:2467-2478.
    • (2012) FEBS J. , vol.279 , pp. 2467-2478
    • Zeng, L.1
  • 37
    • 84908024986 scopus 로고    scopus 로고
    • The de-ubiquitinating enzyme ataxin-3 does not modulate disease progression in a knock-in mouse model of Huntington disease
    • Zeng L., et al. The de-ubiquitinating enzyme ataxin-3 does not modulate disease progression in a knock-in mouse model of Huntington disease. J. Huntingt. Dis. 2013, 2:201-215.
    • (2013) J. Huntingt. Dis. , vol.2 , pp. 201-215
    • Zeng, L.1
  • 38
    • 77951183159 scopus 로고    scopus 로고
    • An emerging role for ubiquilin 1 in regulating protein quality control system and in disease pathogenesis
    • Zhang C., Saunders A.J. An emerging role for ubiquilin 1 in regulating protein quality control system and in disease pathogenesis. Discov. Med. 2009, 8:18-22.
    • (2009) Discov. Med. , vol.8 , pp. 18-22
    • Zhang, C.1    Saunders, A.J.2
  • 39
    • 84897863195 scopus 로고    scopus 로고
    • Ubiquilin 2: a component of the ubiquitin-proteasome system with an emerging role in neurodegeneration
    • Zhang K.Y., et al. Ubiquilin 2: a component of the ubiquitin-proteasome system with an emerging role in neurodegeneration. Int. J. Biochem. Cell Biol. 2014, 50:123-126.
    • (2014) Int. J. Biochem. Cell Biol. , vol.50 , pp. 123-126
    • Zhang, K.Y.1


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