메뉴 건너뛰기




Volumn 9, Issue APR, 2016, Pages

Subcellular clearance and accumulation of huntington disease protein: A mini-review

Author keywords

Aggregation; Autophagy; Huntingtin; Neurodegeneration; Proteasome

Indexed keywords

HISTONE DEACETYLASE 6; PROTEASOME; UBIQUITIN;

EID: 84975295233     PISSN: 16625099     EISSN: None     Source Type: Journal    
DOI: 10.3389/fnmol.2016.00027     Document Type: Review
Times cited : (42)

References (35)
  • 1
    • 84902975772 scopus 로고    scopus 로고
    • Phototransformable fluorescent proteins: Future challenges
    • Adam, V., Berardozzi, R., Byrdin, M., and Bourgeois, D. (2014). Phototransformable fluorescent proteins: future challenges. Curr. Opin. Chem. Biol. 20, 92-102. doi: 10.1016/j.cbpa.2014.05.016
    • (2014) Curr. Opin. Chem. Biol. , vol.20 , pp. 92-102
    • Adam, V.1    Berardozzi, R.2    Byrdin, M.3    Bourgeois, D.4
  • 2
    • 0035947372 scopus 로고    scopus 로고
    • Impairment of the ubiquitinproteasome system by protein aggregation
    • Bence, N. F., Sampat, R. M., and Kopito, R. R. (2001). Impairment of the ubiquitinproteasome system by protein aggregation. Science 292, 1552-1555. doi: 10. 1126/science.292.5521.1552
    • (2001) Science , vol.292 , pp. 1552-1555
    • Bence, N.F.1    Sampat, R.M.2    Kopito, R.R.3
  • 3
    • 65249181587 scopus 로고    scopus 로고
    • The ubiquitinproteasome reporter GFPu does not accumulate in neurons of the R6/2 transgenic mouse model of Huntington’s disease
    • Bett, J. S., Cook, C., Petrucelli, L., and Bates, G. P. (2009). The ubiquitinproteasome reporter GFPu does not accumulate in neurons of the R6/2 transgenic mouse model of Huntington’s disease. PLoS One 4: e5128. doi: 10. 1371/journal.pone.0005128
    • (2009) PLoS One , vol.4 , pp. 5128
    • Bett, J.S.1    Cook, C.2    Petrucelli, L.3    Bates, G.P.4
  • 4
    • 84898814706 scopus 로고    scopus 로고
    • Differential ubiquitination and degradation of huntingtin fragments modulated by ubiquitin-protein ligase E3A
    • Bhat, K. P., Yan, S., Wang, C. E., Li, S., and Li, X. J. (2014). Differential ubiquitination and degradation of huntingtin fragments modulated by ubiquitin-protein ligase E3A. Proc. Natl. Acad. Sci. U S A 111, 5706-5711. doi: 10.1073/pnas.1402215111
    • (2014) Proc. Natl. Acad. Sci. U S A , vol.111 , pp. 5706-5711
    • Bhat, K.P.1    Yan, S.2    Wang, C.E.3    Li, S.4    Li, X.J.5
  • 5
    • 34548181882 scopus 로고    scopus 로고
    • Tracking intracellular protein movements using photoswitchable fluorescent proteins PS-CFP2 and Dendra2
    • Chudakov, D. M., Lukyanov, S., and Lukyanov, K. A. (2007). Tracking intracellular protein movements using photoswitchable fluorescent proteins PS-CFP2 and Dendra2. Nat. Protoc. 2, 2024-2032. doi: 10.1038/nprot.2007.291
    • (2007) Nat. Protoc. , vol.2 , pp. 2024-2032
    • Chudakov, D.M.1    Lukyanov, S.2    Lukyanov, K.A.3
  • 6
    • 18544410106 scopus 로고    scopus 로고
    • Formation of neuronal intranuclear inclusions underlies the neurological dysfunction in mice transgenic for the HD mutation
    • Davies, S. W., Turmaine, M., Cozens, B. A., DiFiglia, M., Sharp, A. H., Ross, C. A., et al. (1997). Formation of neuronal intranuclear inclusions underlies the neurological dysfunction in mice transgenic for the HD mutation. Cell 90, 537-548. doi: 10.1016/s0092-8674(00)80513-9
    • (1997) Cell , vol.90 , pp. 537-548
    • Davies, S.W.1    Turmaine, M.2    Cozens, B.A.3    DiFiglia, M.4    Sharp, A.H.5    Ross, C.A.6
  • 7
    • 0030752709 scopus 로고    scopus 로고
    • Aggregation of huntingtin in neuronal intranuclear inclusions and dystrophic neurites in brain
    • DiFiglia, M., Sapp, E., Chase, K. O., Davies, S. W., Bates, G. P., Vonsattel, J. P., et al. (1997). Aggregation of huntingtin in neuronal intranuclear inclusions and dystrophic neurites in brain. Science 277, 1990-1993. doi: 10.1126/science.277. 5334.1990
    • (1997) Science , vol.277 , pp. 1990-1993
    • DiFiglia, M.1    Sapp, E.2    Chase, K.O.3    Davies, S.W.4    Bates, G.P.5    Vonsattel, J.P.6
  • 8
    • 0033119123 scopus 로고    scopus 로고
    • Nuclear and neuropil aggregates in Huntington’s disease: Relationship to neuropathology
    • Gutekunst, C. A., Li, S. H., Yi, H., Mulroy, J. S., Kuemmerle, S., Jones, R., et al. (1999). Nuclear and neuropil aggregates in Huntington’s disease: relationship to neuropathology. J. Neurosci. 19, 2522-2534. doi: 10.1093/hmg/8.7.1227
    • (1999) J. Neurosci. , vol.19 , pp. 2522-2534
    • Gutekunst, C.A.1    Li, S.H.2    Yi, H.3    Mulroy, J.S.4    Kuemmerle, S.5    Jones, R.6
  • 9
    • 84884567375 scopus 로고    scopus 로고
    • Expanded polyglutamine-containing N-terminal huntingtin fragments are entirely degraded by mammalian proteasomes
    • Juenemann, K., Schipper-Krom, S., Wiemhoefer, A., Kloss, A., Sanz Sanz, A., and Reits, E. A. (2013). Expanded polyglutamine-containing N-terminal huntingtin fragments are entirely degraded by mammalian proteasomes. J. Biol. Chem. 288, 27068-27084. doi: 10.1074/jbc.M113.486076
    • (2013) J. Biol. Chem. , vol.288 , pp. 27068-27084
    • Juenemann, K.1    Schipper-Krom, S.2    Wiemhoefer, A.3    Kloss, A.4    Sanz Sanz, A.5    Reits, E.A.6
  • 10
    • 1242338856 scopus 로고    scopus 로고
    • Huntingtin-protein interactions and the pathogenesis of Huntington’s disease
    • Li, S. H., and Li, X. J. (2004). Huntingtin-protein interactions and the pathogenesis of Huntington’s disease. Trends Genet. 20, 146-154. doi: 10.1016/j.tig.2004. 01.008
    • (2004) Trends Genet. , vol.20 , pp. 146-154
    • Li, S.H.1    Li, X.J.2
  • 11
    • 0035503511 scopus 로고    scopus 로고
    • Huntingtin aggregate-associated axonal degeneration is an early pathological event in Huntington’s disease mice
    • Li, H., Li, S. H., Yu, Z. X., Shelbourne, P. F., and Li, X. J. (2001). Huntingtin aggregate-associated axonal degeneration is an early pathological event in Huntington’s disease mice. J. Neurosci. 21, 8473-8481.
    • (2001) J. Neurosci. , vol.21 , pp. 8473-8481
    • Li, H.1    Li, S.H.2    Yu, Z.X.3    Shelbourne, P.F.4    Li, X.J.5
  • 13
    • 77951665859 scopus 로고    scopus 로고
    • Cargo recognition failure is responsible for inefficient autophagy in Huntington’s disease
    • Martinez-Vicente, M., Talloczy, Z., Wong, E., Tang, G., Koga, H., Kaushik, S., et al. (2010). Cargo recognition failure is responsible for inefficient autophagy in Huntington’s disease. Nat. Neurosci. 13, 567-576. doi: 10.1038/nn.2528
    • (2010) Nat. Neurosci. , vol.13 , pp. 567-576
    • Martinez-Vicente, M.1    Talloczy, Z.2    Wong, E.3    Tang, G.4    Koga, H.5    Kaushik, S.6
  • 14
    • 2342485108 scopus 로고    scopus 로고
    • Proteasome degrades soluble expanded polyglutamine completely and efficiently
    • Michalik, A., and Van Broeckhoven, C. (2004). Proteasome degrades soluble expanded polyglutamine completely and efficiently. Neurobiol. Dis. 16, 202-211. doi: 10.1016/j.nbd.2003.12.020
    • (2004) Neurobiol. Dis. , vol.16 , pp. 202-211
    • Michalik, A.1    Van Broeckhoven, C.2
  • 15
    • 79551554590 scopus 로고    scopus 로고
    • The importance of integrating basic and clinical research toward the development of new therapies for Huntington’s disease
    • Munoz-Sanjuan, I., and Bates, G. P. (2011). The importance of integrating basic and clinical research toward the development of new therapies for Huntington’s disease. J. Clin. Invest. 121, 476-483. doi: 10.1172/JCI45364
    • (2011) J. Clin. Invest. , vol.121 , pp. 476-483
    • Munoz-Sanjuan, I.1    Bates, G.P.2
  • 16
    • 40849147435 scopus 로고    scopus 로고
    • N-terminal mutant huntingtin associates with mitochondria and impairs mitochondrial trafficking
    • Orr, A. L., Li, S., Wang, C. E., Li, H., Wang, J., Rong, J., et al. (2008). N-terminal mutant huntingtin associates with mitochondria and impairs mitochondrial trafficking. J. Neurosci. 28, 2783-2792. doi: 10.1523/JNEUROSCI.0106-08.2008
    • (2008) J. Neurosci. , vol.28 , pp. 2783-2792
    • Orr, A.L.1    Li, S.2    Wang, C.E.3    Li, H.4    Wang, J.5    Rong, J.6
  • 17
    • 34250183177 scopus 로고    scopus 로고
    • HDAC6 rescues neurodegeneration and provides an essential link between autophagy and the UPS
    • Pandey, U. B., Nie, Z., Batlevi, Y., McCray, B. A., Ritson, G. P., Nedelsky, N. B., et al. (2007). HDAC6 rescues neurodegeneration and provides an essential link between autophagy and the UPS. Nature 447, 859-863. doi: 10. 1038/nature05853
    • (2007) Nature , vol.447 , pp. 859-863
    • Pandey, U.B.1    Nie, Z.2    Batlevi, Y.3    McCray, B.A.4    Ritson, G.P.5    Nedelsky, N.B.6
  • 18
    • 0348013126 scopus 로고    scopus 로고
    • Autophagy regulates the processing of amino terminal huntingtin fragments
    • Qin, Z. H., Wang, Y., Kegel, K. B., Kazantsev, A., Apostol, B. L., Thompson, L. M., et al. (2003). Autophagy regulates the processing of amino terminal huntingtin fragments. Hum. Mol. Genet. 12, 3231-3244. doi: 10.1093/hmg/ddg346
    • (2003) Hum. Mol. Genet. , vol.12 , pp. 3231-3244
    • Qin, Z.H.1    Wang, Y.2    Kegel, K.B.3    Kazantsev, A.4    Apostol, B.L.5    Thompson, L.M.6
  • 19
    • 2642586352 scopus 로고    scopus 로고
    • Inhibition of mTOR induces autophagy and reduces toxicity of polyglutamine expansions in fly and mouse models of Huntington’s disease
    • Ravikumar, B., Vacher, C., Berger, Z., Davies, J. E., Luo, S., Oroz, L. G., et al. (2004). Inhibition of mTOR induces autophagy and reduces toxicity of polyglutamine expansions in fly and mouse models of Huntington’s disease. Nat. Genet. 36, 585-595. doi: 10.1038/ng1362
    • (2004) Nat. Genet. , vol.36 , pp. 585-595
    • Ravikumar, B.1    Vacher, C.2    Berger, Z.3    Davies, J.E.4    Luo, S.5    Oroz, L.G.6
  • 20
    • 84855165944 scopus 로고    scopus 로고
    • Mutant huntingtin, abnormal mitochondrial dynamics, defective axonal transport of mitochondria and selective synaptic degeneration in Huntington’s disease
    • Reddy, P. H., and Shirendeb, U. P. (2012). Mutant huntingtin, abnormal mitochondrial dynamics, defective axonal transport of mitochondria and selective synaptic degeneration in Huntington’s disease. Biochim. Biophys. Acta 1822, 101-110. doi: 10.1016/j.bbadis.2011.10.016
    • (2012) Biochim. Biophys. Acta , vol.1822 , pp. 101-110
    • Reddy, P.H.1    Shirendeb, U.P.2
  • 22
    • 0029586383 scopus 로고
    • Preferential loss of preproenkephalin versus preprotachykinin neurons from the striatum of Huntington’s disease patients
    • Richfield, E. K., Maguire-Zeiss, K. A., Vonkeman, H. E., and Voorn, P. (1995). Preferential loss of preproenkephalin versus preprotachykinin neurons from the striatum of Huntington’s disease patients. Ann. Neurol. 38, 852-861. doi: 10. 1002/ana.410380605
    • (1995) Ann. Neurol. , vol.38 , pp. 852-861
    • Richfield, E.K.1    Maguire-Zeiss, K.A.2    Vonkeman, H.E.3    Voorn, P.4
  • 23
    • 84898017417 scopus 로고    scopus 로고
    • Huntington disease: Natural history, biomarkers and prospects for therapeutics
    • Ross, C. A., Aylward, E. H., Wild, E. J., Langbehn, D. R., Long, J. D., Warner, J. H., et al. (2014). Huntington disease: natural history, biomarkers and prospects for therapeutics. Nat. Rev. Neurol. 10, 204-216. doi: 10.1038/nrneurol.2014.24
    • (2014) Nat. Rev. Neurol. , vol.10 , pp. 204-216
    • Ross, C.A.1    Aylward, E.H.2    Wild, E.J.3    Langbehn, D.R.4    Long, J.D.5    Warner, J.H.6
  • 24
    • 84925004049 scopus 로고    scopus 로고
    • Conophylline protects cells in cellular models of neurodegenerative diseases by inducing mammalian target of rapamycin (mTOR)-independent autophagy
    • Sasazawa, Y., Sato, N., Umezawa, K., and Simizu, S. (2015). Conophylline protects cells in cellular models of neurodegenerative diseases by inducing mammalian target of rapamycin (mTOR)-independent autophagy. J. Biol. Chem. 290, 6168-6178. doi: 10.1074/jbc.m114.606293
    • (2015) J. Biol. Chem. , vol.290 , pp. 6168-6178
    • Sasazawa, Y.1    Sato, N.2    Umezawa, K.3    Simizu, S.4
  • 25
    • 0033054555 scopus 로고    scopus 로고
    • Intranuclear inclusions and neuritic aggregates in transgenic mice expressing a mutant N-terminal fragment of huntingtin
    • Schilling, G., Becher, M. W., Sharp, A. H., Jinnah, H. A., Duan, K., Kotzuk, J. A., et al. (1999). Intranuclear inclusions and neuritic aggregates in transgenic mice expressing a mutant N-terminal fragment of huntingtin. Hum. Mol. Genet. 8, 397-407. doi: 10.1093/hmg/8.3.397
    • (1999) Hum. Mol. Genet. , vol.8 , pp. 397-407
    • Schilling, G.1    Becher, M.W.2    Sharp, A.H.3    Jinnah, H.A.4    Duan, K.5    Kotzuk, J.A.6
  • 26
  • 27
    • 84863833900 scopus 로고    scopus 로고
    • Network organization of the huntingtin proteomic interactome in mammalian brain
    • Shirasaki, D. I., Greiner, E. R., Al-Ramahi, I., Gray, M., Boontheung, P., Geschwind, D. H., et al. (2012). Network organization of the huntingtin proteomic interactome in mammalian brain. Neuron 75, 41-57. doi: 10.1016/j. neuron.2012.05.024
    • (2012) Neuron , vol.75 , pp. 41-57
    • Shirasaki, D.I.1    Greiner, E.R.2    Al-Ramahi, I.3    Gray, M.4    Boontheung, P.5    Geschwind, D.H.6
  • 28
    • 38349114036 scopus 로고    scopus 로고
    • Lysine 63-linked ubiquitination promotes the formation and autophagic clearance of protein inclusions associated with neurodegenerative diseases
    • Tan, J. M., Wong, E. S., Kirkpatrick, D. S., Pletnikova, O., Ko, H. S., Tay, S. P., et al. (2008). Lysine 63-linked ubiquitination promotes the formation and autophagic clearance of protein inclusions associated with neurodegenerative diseases. Hum. Mol. Genet. 17, 431-439. doi: 10.1093/hmg/ddm320
    • (2008) Hum. Mol. Genet. , vol.17 , pp. 431-439
    • Tan, J.M.1    Wong, E.S.2    Kirkpatrick, D.S.3    Pletnikova, O.4    Ko, H.S.5    Tay, S.P.6
  • 29
    • 84883204078 scopus 로고    scopus 로고
    • Proteostasis of polyglutamine varies among neurons and predicts neurodegeneration
    • Tsvetkov, A. S., Arrasate, M., Barmada, S., Ando, D. M., Sharma, P., Shaby, B. A., et al. (2013). Proteostasis of polyglutamine varies among neurons and predicts neurodegeneration. Nat. Chem. Biol. 9, 586-592. doi: 10.1038/nchembio.1308
    • (2013) Nat. Chem. Biol. , vol.9 , pp. 586-592
    • Tsvetkov, A.S.1    Arrasate, M.2    Barmada, S.3    Ando, D.M.4    Sharma, P.5    Shaby, B.A.6
  • 30
    • 1842766144 scopus 로고    scopus 로고
    • Eukaryotic proteasomes cannot digest polyglutamine sequences and release them during degradation of polyglutamine-containing proteins
    • Venkatraman, P., Wetzel, R., Tanaka, M., Nukina, N., and Goldberg, A. L. (2004). Eukaryotic proteasomes cannot digest polyglutamine sequences and release them during degradation of polyglutamine-containing proteins. Mol. Cell 14, 95-104. doi: 10.1016/s1097-2765(04)00151-0
    • (2004) Mol. Cell , vol.14 , pp. 95-104
    • Venkatraman, P.1    Wetzel, R.2    Tanaka, M.3    Nukina, N.4    Goldberg, A.L.5
  • 32
    • 41549129945 scopus 로고    scopus 로고
    • Impaired ubiquitin-proteasome system activity in the synapses of Huntington’s disease mice
    • Wang, J., Wang, C. E., Orr, A., Tydlacka, S., Li, S. H., and Li, X. J. (2008a). Impaired ubiquitin-proteasome system activity in the synapses of Huntington’s disease mice. J. Cell Biol. 180, 1177-1189. doi: 10.1083/jcb.200709080
    • (2008) J. Cell Biol. , vol.180 , pp. 1177-1189
    • Wang, J.1    Wang, C.E.2    Orr, A.3    Tydlacka, S.4    Li, S.H.5    Li, X.J.6
  • 33
    • 44649113841 scopus 로고    scopus 로고
    • Suppression of neuropil aggregates and neurological symptoms by an intracellular antibody implicates the cytoplasmic toxicity of mutant huntingtin
    • Wang, C. E., Zhou, H., McGuire, J. R., Cerullo, V., Lee, B., Li, S. H., et al. (2008b). Suppression of neuropil aggregates and neurological symptoms by an intracellular antibody implicates the cytoplasmic toxicity of mutant huntingtin. J. Cell Biol. 181, 803-816. doi: 10.1083/jcb.200710158
    • (2008) J. Cell Biol. , vol.181 , pp. 803-816
    • Wang, C.E.1    Zhou, H.2    McGuire, J.R.3    Cerullo, V.4    Lee, B.5    Li, S.H.6
  • 34
    • 0034163497 scopus 로고    scopus 로고
    • Long glutamine tracts cause nuclear localization of a novel form of huntingtin in medium spiny striatal neurons in HdhQ92 and HdhQ111 knockin mice
    • Wheeler, V. C., White, J. K., Gutekunst, C. A., Vrbanac, V., Weaver, M., Li, X. J., et al. (2000). Long glutamine tracts cause nuclear localization of a novel form of huntingtin in medium spiny striatal neurons in HdhQ92 and HdhQ111 knockin mice. Hum. Mol. Genet. 9, 503-513. doi: 10.1093/hmg/9.4.503
    • (2000) Hum. Mol. Genet. , vol.9 , pp. 503-513
    • Wheeler, V.C.1    White, J.K.2    Gutekunst, C.A.3    Vrbanac, V.4    Weaver, M.5    Li, X.J.6
  • 35
    • 84892755229 scopus 로고    scopus 로고
    • The regulation of autophagosome dynamics by huntingtin and HAP1 is disrupted by expression of mutant huntingtin, leading to defective cargo degradation
    • Wong, Y. C., and Holzbaur, E. L. (2014). The regulation of autophagosome dynamics by huntingtin and HAP1 is disrupted by expression of mutant huntingtin, leading to defective cargo degradation. J. Neurosci. 34, 1293-1305. doi: 10.1523/JNEUROSCI.1870-13.2014
    • (2014) J. Neurosci. , vol.34 , pp. 1293-1305
    • Wong, Y.C.1    Holzbaur, E.L.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.