메뉴 건너뛰기




Volumn 56, Issue 8, 2010, Pages 911-918

Skeletal muscles of Uchl3 knockout mice show polyubiquitinated protein accumulation and stress responses

Author keywords

Accumulation of polyubiquitinated proteins; De ubiquitinating enzyme; Proteotoxic stress; Ubiquitin C terminal hydroalse L3; Ubiquitin proteasome system

Indexed keywords

ACTIVATING TRANSCRIPTION FACTOR 6; GLUCOSE REGULATED PROTEIN 78; HEAT SHOCK PROTEIN 110; HEAT SHOCK PROTEIN 27; HEAT SHOCK PROTEIN 70; HEAT SHOCK PROTEIN 90; UBIQUITIN; UBIQUITIN THIOLESTERASE;

EID: 77952878619     PISSN: 01970186     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.neuint.2010.03.021     Document Type: Article
Times cited : (18)

References (57)
  • 1
    • 56749104288 scopus 로고    scopus 로고
    • Inclusion-body myositis: muscle-fiber molecular pathology and possible pathogenic significance of its similarity to Alzheimer's and Parkinson's disease brains
    • Askanas V., Engel W.K. Inclusion-body myositis: muscle-fiber molecular pathology and possible pathogenic significance of its similarity to Alzheimer's and Parkinson's disease brains. Acta Neuropathol. 2008, 116:583-595.
    • (2008) Acta Neuropathol. , vol.116 , pp. 583-595
    • Askanas, V.1    Engel, W.K.2
  • 2
    • 66949145779 scopus 로고    scopus 로고
    • Inclusion body myositis: a degenerative muscle disease associated with intra-muscle fiber multi-protein aggregates, proteasome inhibition, endoplasmic reticulum stress and decreased lysosomal degradation
    • Askanas V., Engel W.K., Nogalska A. Inclusion body myositis: a degenerative muscle disease associated with intra-muscle fiber multi-protein aggregates, proteasome inhibition, endoplasmic reticulum stress and decreased lysosomal degradation. Brain Pathol. 2009, 19:493-506.
    • (2009) Brain Pathol. , vol.19 , pp. 493-506
    • Askanas, V.1    Engel, W.K.2    Nogalska, A.3
  • 3
    • 0035947372 scopus 로고    scopus 로고
    • Impairment of the ubiquitin-proteasome system by protein aggregation
    • Bence N.F., Sampat R.M., Kopito R.R. Impairment of the ubiquitin-proteasome system by protein aggregation. Science 2001, 292:1552-1555.
    • (2001) Science , vol.292 , pp. 1552-1555
    • Bence, N.F.1    Sampat, R.M.2    Kopito, R.R.3
  • 4
    • 0030898710 scopus 로고    scopus 로고
    • Proteasome inhibition leads to a heat-shock response, induction of endoplasmic reticulum chaperones, and thermotolerance
    • Bush K.T., Goldberg A.L., Nigam S.K. Proteasome inhibition leads to a heat-shock response, induction of endoplasmic reticulum chaperones, and thermotolerance. J. Biol. Chem. 1997, 272:9086-9092.
    • (1997) J. Biol. Chem. , vol.272 , pp. 9086-9092
    • Bush, K.T.1    Goldberg, A.L.2    Nigam, S.K.3
  • 5
    • 38049177658 scopus 로고    scopus 로고
    • The Deubiquitinating Enzyme UCH-L3 Regulates the Apical Membrane Recycling of the Epithelial Sodium Channel
    • Butterworth M.B., Edinger R.S., Ovaa H., Burg D., Johnson J.P., Frizzell R.A. The Deubiquitinating Enzyme UCH-L3 Regulates the Apical Membrane Recycling of the Epithelial Sodium Channel. J. Biol. Chem. 2007, 282:37885-37893.
    • (2007) J. Biol. Chem. , vol.282 , pp. 37885-37893
    • Butterworth, M.B.1    Edinger, R.S.2    Ovaa, H.3    Burg, D.4    Johnson, J.P.5    Frizzell, R.A.6
  • 6
    • 0030841343 scopus 로고    scopus 로고
    • Conformational disease
    • Carrell R.W., Lomas D.A. Conformational disease. Lancet 1997, 350:134-138.
    • (1997) Lancet , vol.350 , pp. 134-138
    • Carrell, R.W.1    Lomas, D.A.2
  • 7
    • 0033391428 scopus 로고    scopus 로고
    • Mutation of the E6-AP ubiquitin ligase reduces nuclear inclusion frequency while accelerating polyglutamine-induced pathology in SCA1 mice
    • Cummings C.J., Reinstein E., Sun Y., Antalffy B., Jiang Y., Ciechanover A., Orr H.T., Beaudet A.L., Zoghbi H.Y. Mutation of the E6-AP ubiquitin ligase reduces nuclear inclusion frequency while accelerating polyglutamine-induced pathology in SCA1 mice. Neuron 1999, 24:879-892.
    • (1999) Neuron , vol.24 , pp. 879-892
    • Cummings, C.J.1    Reinstein, E.2    Sun, Y.3    Antalffy, B.4    Jiang, Y.5    Ciechanover, A.6    Orr, H.T.7    Beaudet, A.L.8    Zoghbi, H.Y.9
  • 11
    • 33745365931 scopus 로고    scopus 로고
    • Proteolytic and lipolytic responses to starvation
    • Finn P.F., Dice J.F. Proteolytic and lipolytic responses to starvation. Nutrition 2006, 22:830-844.
    • (2006) Nutrition , vol.22 , pp. 830-844
    • Finn, P.F.1    Dice, J.F.2
  • 12
    • 0041424822 scopus 로고    scopus 로고
    • Molecular mechanisms modulating muscle mass
    • Glass D.J. Molecular mechanisms modulating muscle mass. Trends Mol. Med. 2003, 9:344-350.
    • (2003) Trends Mol. Med. , vol.9 , pp. 344-350
    • Glass, D.J.1
  • 13
    • 0036083396 scopus 로고    scopus 로고
    • The ubiquitin-proteasome proteolytic pathway: destruction for the sake of construction
    • Glickman M.H., Ciechanover A. The ubiquitin-proteasome proteolytic pathway: destruction for the sake of construction. Physiol. Rev. 2002, 82:373-428.
    • (2002) Physiol. Rev. , vol.82 , pp. 373-428
    • Glickman, M.H.1    Ciechanover, A.2
  • 14
    • 0346727127 scopus 로고    scopus 로고
    • Protein degradation and protection against misfolded or damaged proteins
    • Goldberg A.L. Protein degradation and protection against misfolded or damaged proteins. Nature 2003, 426:895-899.
    • (2003) Nature , vol.426 , pp. 895-899
    • Goldberg, A.L.1
  • 15
    • 34447098604 scopus 로고    scopus 로고
    • Valosin-containing protein and the pathogenesis of frontotemporal dementia associated with inclusion body myopathy
    • Guinto J.B., Ritson G.P., Taylor J.P., Forman M.S. Valosin-containing protein and the pathogenesis of frontotemporal dementia associated with inclusion body myopathy. Acta Neuropathol. 2007, 114:55-61.
    • (2007) Acta Neuropathol. , vol.114 , pp. 55-61
    • Guinto, J.B.1    Ritson, G.P.2    Taylor, J.P.3    Forman, M.S.4
  • 16
    • 33745224935 scopus 로고    scopus 로고
    • P97: the cell's molecular purgatory?
    • Halawani D., Latterich M. p97: the cell's molecular purgatory?. Mol. Cell 2006, 22:713-717.
    • (2006) Mol. Cell , vol.22 , pp. 713-717
    • Halawani, D.1    Latterich, M.2
  • 17
    • 33749348820 scopus 로고    scopus 로고
    • A novel proteasome interacting protein recruits the deubiquitinating enzyme UCH37 to 26S proteasomes
    • Hamazaki J., Iemura S., Natsume T., Yashiroda H., Tanaka K., Murata S. A novel proteasome interacting protein recruits the deubiquitinating enzyme UCH37 to 26S proteasomes. EMBO J. 2006, 25:4524-4536.
    • (2006) EMBO J. , vol.25 , pp. 4524-4536
    • Hamazaki, J.1    Iemura, S.2    Natsume, T.3    Yashiroda, H.4    Tanaka, K.5    Murata, S.6
  • 21
    • 0035293622 scopus 로고    scopus 로고
    • Protein regulation by monoubiquitin
    • Hicke L. Protein regulation by monoubiquitin. Nat. Rev. Mol. Cell Biol. 2001, 2:195-201.
    • (2001) Nat. Rev. Mol. Cell Biol. , vol.2 , pp. 195-201
    • Hicke, L.1
  • 22
    • 0031011721 scopus 로고    scopus 로고
    • Crystal structure of a deubiquitinating enzyme (human UCH-L3) at 1.8A resolution
    • Johnston S.C., Larsen C.N., Cook W.J., Wilkinson K.D., Hill C.P. Crystal structure of a deubiquitinating enzyme (human UCH-L3) at 1.8A resolution. EMBO J. 1997, 16:3787-3796.
    • (1997) EMBO J. , vol.16 , pp. 3787-3796
    • Johnston, S.C.1    Larsen, C.N.2    Cook, W.J.3    Wilkinson, K.D.4    Hill, C.P.5
  • 23
    • 68049084674 scopus 로고    scopus 로고
    • Breaking the chains: structure and function of the deubiquitinases
    • Komander D., Clague M.J., Urbe S. Breaking the chains: structure and function of the deubiquitinases. Nat. Rev. Mol. Cell Biol. 2009, 10:550-563.
    • (2009) Nat. Rev. Mol. Cell Biol. , vol.10 , pp. 550-563
    • Komander, D.1    Clague, M.J.2    Urbe, S.3
  • 24
    • 0034117284 scopus 로고    scopus 로고
    • Expression and functional analysis of Uch-L3 during mouse development
    • Kurihara L.J., Semenova E., Levorse J.M., Tilghman S.M. Expression and functional analysis of Uch-L3 during mouse development. Mol. Cell. Biol. 2000, 20:2498-2504.
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 2498-2504
    • Kurihara, L.J.1    Semenova, E.2    Levorse, J.M.3    Tilghman, S.M.4
  • 26
    • 4644263753 scopus 로고    scopus 로고
    • Two closely related ubiquitin C-terminal hydrolase isozymes function as reciprocal modulators of germ cell apoptosis in cryptorchid testis
    • Kwon J., Wang Y.L., Setsuie R., Sekiguchi S., Sato Y., Sakurai M., Noda M., Aoki S., Yoshikawa Y., Wada K. Two closely related ubiquitin C-terminal hydrolase isozymes function as reciprocal modulators of germ cell apoptosis in cryptorchid testis. Am. J. Pathol. 2004, 165:1367-1374.
    • (2004) Am. J. Pathol. , vol.165 , pp. 1367-1374
    • Kwon, J.1    Wang, Y.L.2    Setsuie, R.3    Sekiguchi, S.4    Sato, Y.5    Sakurai, M.6    Noda, M.7    Aoki, S.8    Yoshikawa, Y.9    Wada, K.10
  • 27
    • 0032502276 scopus 로고    scopus 로고
    • Substrate specificity of deubiquitinating enzymes: ubiquitin C-terminal hydrolases
    • Larsen C.N., Krantz B.A., Wilkinson K.D. Substrate specificity of deubiquitinating enzymes: ubiquitin C-terminal hydrolases. Biochemistry 1998, 37:3358-3368.
    • (1998) Biochemistry , vol.37 , pp. 3358-3368
    • Larsen, C.N.1    Krantz, B.A.2    Wilkinson, K.D.3
  • 28
    • 0029999683 scopus 로고    scopus 로고
    • Substrate binding and catalysis by ubiquitin C-terminal hydrolases: identification of two active site residues
    • Larsen C.N., Price J.S., Wilkinson K.D. Substrate binding and catalysis by ubiquitin C-terminal hydrolases: identification of two active site residues. Biochemistry 1996, 35:6735-6744.
    • (1996) Biochemistry , vol.35 , pp. 6735-6744
    • Larsen, C.N.1    Price, J.S.2    Wilkinson, K.D.3
  • 30
    • 3042616595 scopus 로고    scopus 로고
    • A membrane protein required for dislocation of misfolded proteins from the ER
    • Lilley B.N., Ploegh H.L. A membrane protein required for dislocation of misfolded proteins from the ER. Nature 2004, 429:834-840.
    • (2004) Nature , vol.429 , pp. 834-840
    • Lilley, B.N.1    Ploegh, H.L.2
  • 32
    • 0037821846 scopus 로고    scopus 로고
    • Inhibition of proteasome activity induces concerted expression of proteasome genes and de novo formation of Mammalian proteasomes
    • Meiners S., Heyken D., Weller A., Ludwig A., Stangl K., Kloetzel P.M., Kruger E. Inhibition of proteasome activity induces concerted expression of proteasome genes and de novo formation of Mammalian proteasomes. J. Biol. Chem. 2003, 278:21517-21525.
    • (2003) J. Biol. Chem. , vol.278 , pp. 21517-21525
    • Meiners, S.1    Heyken, D.2    Weller, A.3    Ludwig, A.4    Stangl, K.5    Kloetzel, P.M.6    Kruger, E.7
  • 35
    • 44849094781 scopus 로고    scopus 로고
    • Proteotoxic stress and inducible chaperone networks in neurodegenerative disease and aging
    • Morimoto R.I. Proteotoxic stress and inducible chaperone networks in neurodegenerative disease and aging. Genes Dev. 2008, 22:1427-1438.
    • (2008) Genes Dev. , vol.22 , pp. 1427-1438
    • Morimoto, R.I.1
  • 36
    • 56449095862 scopus 로고    scopus 로고
    • The involvement of the ubiquitin proteasome system in human skeletal muscle remodelling and atrophy
    • Murton A.J., Constantin D., Greenhaff P.L. The involvement of the ubiquitin proteasome system in human skeletal muscle remodelling and atrophy. Biochim. Biophys. Acta 2008, 1782:730-743.
    • (2008) Biochim. Biophys. Acta , vol.1782 , pp. 730-743
    • Murton, A.J.1    Constantin, D.2    Greenhaff, P.L.3
  • 37
    • 34548479943 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress increases myofiber formation in vitro
    • Nakanishi K., Dohmae N., Morishima N. Endoplasmic reticulum stress increases myofiber formation in vitro. FASEB J. 2007, 21:2994-3003.
    • (2007) FASEB J. , vol.21 , pp. 2994-3003
    • Nakanishi, K.1    Dohmae, N.2    Morishima, N.3
  • 38
    • 22344455409 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress signaling transmitted by ATF6 mediates apoptosis during muscle development
    • Nakanishi K., Sudo T., Morishima N. Endoplasmic reticulum stress signaling transmitted by ATF6 mediates apoptosis during muscle development. J. Cell Biol. 2005, 169:555-560.
    • (2005) J. Cell Biol. , vol.169 , pp. 555-560
    • Nakanishi, K.1    Sudo, T.2    Morishima, N.3
  • 41
    • 63649131003 scopus 로고    scopus 로고
    • Substrate filtering by the active site crossover loop in UCHL3 revealed by sortagging and gain-of-function mutations
    • Popp M.W., Artavanis-Tsakonas K., Ploegh H.L. Substrate filtering by the active site crossover loop in UCHL3 revealed by sortagging and gain-of-function mutations. J. Biol. Chem. 2009, 284:3593-3602.
    • (2009) J. Biol. Chem. , vol.284 , pp. 3593-3602
    • Popp, M.W.1    Artavanis-Tsakonas, K.2    Ploegh, H.L.3
  • 42
    • 33845713194 scopus 로고    scopus 로고
    • HRpn13/ADRM1/GP110 is a novel proteasome subunit that binds the deubiquitinating enzyme, UCH37
    • Qiu X.B., Ouyang S.Y., Li C.J., Miao S., Wang L., Goldberg A.L. hRpn13/ADRM1/GP110 is a novel proteasome subunit that binds the deubiquitinating enzyme, UCH37. EMBO J. 2006, 25:5742-5753.
    • (2006) EMBO J. , vol.25 , pp. 5742-5753
    • Qiu, X.B.1    Ouyang, S.Y.2    Li, C.J.3    Miao, S.4    Wang, L.5    Goldberg, A.L.6
  • 43
    • 67650620318 scopus 로고    scopus 로고
    • Regulation and cellular roles of ubiquitin-specific deubiquitinating enzymes
    • Reyes-Turcu F.E., Ventii K.H., Wilkinson K.D. Regulation and cellular roles of ubiquitin-specific deubiquitinating enzymes. Annu. Rev. Biochem. 2009, 78:363-397.
    • (2009) Annu. Rev. Biochem. , vol.78 , pp. 363-397
    • Reyes-Turcu, F.E.1    Ventii, K.H.2    Wilkinson, K.D.3
  • 46
    • 0038683341 scopus 로고    scopus 로고
    • An engineered 800 kilobase deletion of Uchl3 and Lmo7 on mouse chromosome 14 causes defects in viability, postnatal growth and degeneration of muscle and retina
    • Semenova E., Wang X., Jablonski M.M., Levorse J., Tilghman S.M. An engineered 800 kilobase deletion of Uchl3 and Lmo7 on mouse chromosome 14 causes defects in viability, postnatal growth and degeneration of muscle and retina. Hum. Mol. Genet. 2003, 12:1301-1312.
    • (2003) Hum. Mol. Genet. , vol.12 , pp. 1301-1312
    • Semenova, E.1    Wang, X.2    Jablonski, M.M.3    Levorse, J.4    Tilghman, S.M.5
  • 47
    • 61449129071 scopus 로고    scopus 로고
    • Ubiquitin dimers control the hydrolase activity of UCH-L3
    • Setsuie R., Sakurai M., Sakaguchi Y., Wada K. Ubiquitin dimers control the hydrolase activity of UCH-L3. Neurochem. Int. 2009, 54:314-321.
    • (2009) Neurochem. Int. , vol.54 , pp. 314-321
    • Setsuie, R.1    Sakurai, M.2    Sakaguchi, Y.3    Wada, K.4
  • 48
    • 72749112595 scopus 로고    scopus 로고
    • Ubiquitin C-terminal hydrolase-L3-knockout mice are resistant to diet-induced obesity and show increased activation of AMP-activated protein kinase in skeletal muscle
    • Setsuie R., Suzuki M., Kabuta T., Fujita H., Miura S., Ichihara N., Yamada D., Wang Y.L., Ezaki O., Suzuki Y., Wada K. Ubiquitin C-terminal hydrolase-L3-knockout mice are resistant to diet-induced obesity and show increased activation of AMP-activated protein kinase in skeletal muscle. FASEB J. 2009, 23:4148-4157.
    • (2009) FASEB J. , vol.23 , pp. 4148-4157
    • Setsuie, R.1    Suzuki, M.2    Kabuta, T.3    Fujita, H.4    Miura, S.5    Ichihara, N.6    Yamada, D.7    Wang, Y.L.8    Ezaki, O.9    Suzuki, Y.10    Wada, K.11
  • 49
    • 71949103907 scopus 로고    scopus 로고
    • Ubiquitin carboxyl-terminal hydrolase L3 promotes insulin signaling and adipogenesis
    • Suzuki M., Setsuie R., Wada K. Ubiquitin carboxyl-terminal hydrolase L3 promotes insulin signaling and adipogenesis. Endocrinology 2009, 150:5230-5239.
    • (2009) Endocrinology , vol.150 , pp. 5230-5239
    • Suzuki, M.1    Setsuie, R.2    Wada, K.3
  • 50
    • 1542784578 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress and unfolded protein response in inclusion body myositis muscle
    • Vattemi G., Engel W.K., McFerrin J., Askanas V. Endoplasmic reticulum stress and unfolded protein response in inclusion body myositis muscle. Am. J. Pathol. 2004, 164:1-7.
    • (2004) Am. J. Pathol. , vol.164 , pp. 1-7
    • Vattemi, G.1    Engel, W.K.2    McFerrin, J.3    Askanas, V.4
  • 52
    • 27944498719 scopus 로고    scopus 로고
    • The deubiquitinating enzyme UCH37 interacts with Smads and regulates TGF-beta signalling
    • Wicks S.J., Haros K., Millard M., Song L., Cohen R.E., Dijke P.T., Chantry A. The deubiquitinating enzyme UCH37 interacts with Smads and regulates TGF-beta signalling. Oncogene 2005, 24:8080-8084.
    • (2005) Oncogene , vol.24 , pp. 8080-8084
    • Wicks, S.J.1    Haros, K.2    Millard, M.3    Song, L.4    Cohen, R.E.5    Dijke, P.T.6    Chantry, A.7
  • 55
    • 34548172495 scopus 로고    scopus 로고
    • Transcriptional induction of mammalian ER quality control proteins is mediated by single or combined action of ATF6alpha and XBP1
    • Yamamoto K., Sato T., Matsui T., Sato M., Okada T., Yoshida H., Harada A., Mori K. Transcriptional induction of mammalian ER quality control proteins is mediated by single or combined action of ATF6alpha and XBP1. Dev. Cell 2007, 13:365-376.
    • (2007) Dev. Cell , vol.13 , pp. 365-376
    • Yamamoto, K.1    Sato, T.2    Matsui, T.3    Sato, M.4    Okada, T.5    Yoshida, H.6    Harada, A.7    Mori, K.8
  • 57
    • 47949099916 scopus 로고    scopus 로고
    • From endoplasmic-reticulum stress to the inflammatory response
    • Zhang K., Kaufman R.J. From endoplasmic-reticulum stress to the inflammatory response. Nature 2008, 454:455-462.
    • (2008) Nature , vol.454 , pp. 455-462
    • Zhang, K.1    Kaufman, R.J.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.