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Volumn 67, Issue 1, 2013, Pages 67-73

Neuronal Ubiquitin Homeostasis

Author keywords

Deubiquitinating; Enzymes; Proteasome; Synapse; Ubiquitin

Indexed keywords

UBIQUITIN; UBIQUITIN THIOLESTERASE; USP14 PROTEIN, HUMAN;

EID: 84883451270     PISSN: 10859195     EISSN: None     Source Type: Journal    
DOI: 10.1007/s12013-013-9634-4     Document Type: Article
Times cited : (44)

References (53)
  • 1
    • 33847410541 scopus 로고    scopus 로고
    • Emerging roles for ubiquitin and protein degradation in neuronal function
    • Yi, J. J., & Ehlers, M. D. (2007). Emerging roles for ubiquitin and protein degradation in neuronal function. Pharmacological Reviews, 59, 14-39.
    • (2007) Pharmacological Reviews , vol.59 , pp. 14-39
    • Yi, J.J.1    Ehlers, M.D.2
  • 2
    • 0035954743 scopus 로고    scopus 로고
    • Ubiquitination-dependent mechanisms regulate synaptic growth and function
    • DiAntonio, A., Haghighi, A. P., Portman, S. L., Lee, J. D., Amaranto, A. M., et al. (2001). Ubiquitination-dependent mechanisms regulate synaptic growth and function. Nature, 412, 449-452.
    • (2001) Nature , vol.412 , pp. 449-452
    • DiAntonio, A.1    Haghighi, A.P.2    Portman, S.L.3    Lee, J.D.4    Amaranto, A.M.5
  • 3
    • 34548044548 scopus 로고    scopus 로고
    • Spatial regulation of an E3 ubiquitin ligase directs selective synapse elimination
    • Ding, M., Chao, D., Wang, G., & Shen, K. (2007). Spatial regulation of an E3 ubiquitin ligase directs selective synapse elimination. Science, 317, 947-951.
    • (2007) Science , vol.317 , pp. 947-951
    • Ding, M.1    Chao, D.2    Wang, G.3    Shen, K.4
  • 4
    • 0037014445 scopus 로고    scopus 로고
    • Ubiquitin and AP180 regulate the abundance of GLR-1 glutamate receptors at postsynaptic elements in C-elegans
    • Burbea, M., Dreier, L., Dittman, J. S., Grunwald, M. E., & Kaplan, J. M. (2002). Ubiquitin and AP180 regulate the abundance of GLR-1 glutamate receptors at postsynaptic elements in C-elegans. Neuron, 35, 107-120.
    • (2002) Neuron , vol.35 , pp. 107-120
    • Burbea, M.1    Dreier, L.2    Dittman, J.S.3    Grunwald, M.E.4    Kaplan, J.M.5
  • 5
    • 0345119031 scopus 로고    scopus 로고
    • Ubiquitination regulates PSD-95 degradation and AMPA receptor surface expression
    • Colledge, M., Snyder, E. M., Crozier, R. A., Soderling, J. A., Jin, Y., et al. (2003). Ubiquitination regulates PSD-95 degradation and AMPA receptor surface expression. Neuron, 40, 595-607.
    • (2003) Neuron , vol.40 , pp. 595-607
    • Colledge, M.1    Snyder, E.M.2    Crozier, R.A.3    Soderling, J.A.4    Jin, Y.5
  • 6
    • 0025847597 scopus 로고
    • Axonal transport of two major components of the ubiquitin system: free ubiquitin and ubiquitin carboxyl-terminal hydrolase PGP 9.5
    • Bizzi, A., Schaetzle, B., Patton, A., Gambetti, P., & Autilio-Gambetti, L. (1991). Axonal transport of two major components of the ubiquitin system: free ubiquitin and ubiquitin carboxyl-terminal hydrolase PGP 9. 5. Brain Research, 548, 292-299.
    • (1991) Brain Research , vol.548 , pp. 292-299
    • Bizzi, A.1    Schaetzle, B.2    Patton, A.3    Gambetti, P.4    Autilio-Gambetti, L.5
  • 8
    • 0019174693 scopus 로고
    • Ubiquitin is the ATP-dependent proteolysis factor I of rabbit reticulocytes
    • Wilkinson, K. D., Urban, M. K., & Haas, A. L. (1980). Ubiquitin is the ATP-dependent proteolysis factor I of rabbit reticulocytes. Journal of Biological Chemistry, 255, 7529-7532.
    • (1980) Journal of Biological Chemistry , vol.255 , pp. 7529-7532
    • Wilkinson, K.D.1    Urban, M.K.2    Haas, A.L.3
  • 9
    • 0020479850 scopus 로고
    • Immunochemical analysis of the turnover of ubiquitin-protein conjugates in intact cells. Relationship to the breakdown of abnormal proteins
    • Hershko, A., Eytan, E., Ciechanover, A., & Haas, A. L. (1982). Immunochemical analysis of the turnover of ubiquitin-protein conjugates in intact cells. Relationship to the breakdown of abnormal proteins. Journal of Biological Chemistry, 257, 13964-13970.
    • (1982) Journal of Biological Chemistry , vol.257 , pp. 13964-13970
    • Hershko, A.1    Eytan, E.2    Ciechanover, A.3    Haas, A.L.4
  • 10
    • 0018187738 scopus 로고
    • A heat-stable polypeptide component of an ATP-dependent proteolytic system from reticulocytes
    • Ciehanover, A., Hod, Y., & Hershko, A. (1978). A heat-stable polypeptide component of an ATP-dependent proteolytic system from reticulocytes. Biochemical and Biophysical Research Communications, 81, 1100-1105.
    • (1978) Biochemical and Biophysical Research Communications , vol.81 , pp. 1100-1105
    • Ciehanover, A.1    Hod, Y.2    Hershko, A.3
  • 11
    • 79961000536 scopus 로고    scopus 로고
    • Protein standard absolute quantification (PSAQ) method for the measurement of cellular ubiquitin pools
    • Kaiser, S. E., Riley, B. E., Shaler, T. A., Trevino, R. S., Becker, C. H., et al. (2011). Protein standard absolute quantification (PSAQ) method for the measurement of cellular ubiquitin pools. Nature Methods, 8, 691-696.
    • (2011) Nature Methods , vol.8 , pp. 691-696
    • Kaiser, S.E.1    Riley, B.E.2    Shaler, T.A.3    Trevino, R.S.4    Becker, C.H.5
  • 13
    • 0022999212 scopus 로고
    • The chicken ubiquitin gene contains a heat shock promoter and expresses an unstable mRNA in heat-shocked cells
    • Bond, U., & Schlesinger, M. J. (1986). The chicken ubiquitin gene contains a heat shock promoter and expresses an unstable mRNA in heat-shocked cells. Molecular and Cellular Biology, 6, 4602-4610.
    • (1986) Molecular and Cellular Biology , vol.6 , pp. 4602-4610
    • Bond, U.1    Schlesinger, M.J.2
  • 14
    • 0028823598 scopus 로고
    • Metabolism of the polyubiquitin degradation signal: Structure, mechanism, and role of isopeptidase T
    • Wilkinson, K. D., Tashayev, V. L., O'Connor, L. B., Larsen, C. N., Kasperek, E., et al. (1995). Metabolism of the polyubiquitin degradation signal: Structure, mechanism, and role of isopeptidase T. Biochemistry, 34, 14535-14546.
    • (1995) Biochemistry , vol.34 , pp. 14535-14546
    • Wilkinson, K.D.1    Tashayev, V.L.2    O'Connor, L.B.3    Larsen, C.N.4    Kasperek, E.5
  • 16
    • 34250007128 scopus 로고    scopus 로고
    • The mouse polyubiquitin gene UbC is essential for fetal liver development, cell-cycle progression and stress tolerance
    • Ryu, K. Y., Maehr, R., Gilchrist, C. A., Long, M. A., Bouley, D. M., et al. (2007). The mouse polyubiquitin gene UbC is essential for fetal liver development, cell-cycle progression and stress tolerance. EMBO Journal, 26, 2693-2706.
    • (2007) EMBO Journal , vol.26 , pp. 2693-2706
    • Ryu, K.Y.1    Maehr, R.2    Gilchrist, C.A.3    Long, M.A.4    Bouley, D.M.5
  • 18
    • 84863260703 scopus 로고    scopus 로고
    • Perturbation of the hematopoietic system during embryonic liver development due to disruption of polyubiquitin gene Ubc in mice
    • Ryu, K. Y., Park, H., Rossi, D. J., Weissman, I. L., & Kopito, R. R. (2012). Perturbation of the hematopoietic system during embryonic liver development due to disruption of polyubiquitin gene Ubc in mice. PLoS ONE, 7, e32956.
    • (2012) PLoS ONE , vol.7
    • Ryu, K.Y.1    Park, H.2    Rossi, D.J.3    Weissman, I.L.4    Kopito, R.R.5
  • 19
    • 0020478717 scopus 로고
    • Ubiquitin-activating enzyme. Mechanism and role in protein-ubiquitin conjugation
    • Haas, A. L., Warms, J. V., Hershko, A., & Rose, I. A. (1982). Ubiquitin-activating enzyme. Mechanism and role in protein-ubiquitin conjugation. Journal of Biological Chemistry, 257, 2543-2548.
    • (1982) Journal of Biological Chemistry , vol.257 , pp. 2543-2548
    • Haas, A.L.1    Warms, J.V.2    Hershko, A.3    Rose, I.A.4
  • 20
    • 0021099710 scopus 로고
    • Components of ubiquitin-protein ligase system. Resolution, affinity purification, and role in protein breakdown
    • Hershko, A., Heller, H., Elias, S., & Ciechanover, A. (1983). Components of ubiquitin-protein ligase system. Resolution, affinity purification, and role in protein breakdown. Journal of Biological Chemistry, 258, 8206-8214.
    • (1983) Journal of Biological Chemistry , vol.258 , pp. 8206-8214
    • Hershko, A.1    Heller, H.2    Elias, S.3    Ciechanover, A.4
  • 21
    • 0021996450 scopus 로고
    • Functional heterogeneity of ubiquitin carrier proteins
    • Pickart, C. M., & Rose, I. A. (1985). Functional heterogeneity of ubiquitin carrier proteins. Journal of Biological Chemistry, 260, 1573-1581.
    • (1985) Journal of Biological Chemistry , vol.260 , pp. 1573-1581
    • Pickart, C.M.1    Rose, I.A.2
  • 22
    • 27144495057 scopus 로고    scopus 로고
    • E2 conjugating enzymes must disengage from their E1 enzymes before E3-dependent ubiquitin and ubiquitin-like transfer
    • Eletr, Z. M., Huang, D. T., Duda, D. M., Schulman, B. A., & Kuhlman, B. (2005). E2 conjugating enzymes must disengage from their E1 enzymes before E3-dependent ubiquitin and ubiquitin-like transfer. Nature Structural & Molecular Biology, 12, 933-934.
    • (2005) Nature Structural & Molecular Biology , vol.12 , pp. 933-934
    • Eletr, Z.M.1    Huang, D.T.2    Duda, D.M.3    Schulman, B.A.4    Kuhlman, B.5
  • 23
    • 84866006042 scopus 로고    scopus 로고
    • Governance of endocytic trafficking and signaling by reversible ubiquitylation
    • Clague, M. J., Liu, H., & Urbe, S. (2012). Governance of endocytic trafficking and signaling by reversible ubiquitylation. Developmental Cell, 23, 457-467.
    • (2012) Developmental Cell , vol.23 , pp. 457-467
    • Clague, M.J.1    Liu, H.2    Urbe, S.3
  • 24
    • 0024514688 scopus 로고
    • A multiubiquitin chain is confined to specific lysine in a targeted short-lived protein
    • Chau, V., Tobias, J. W., Bachmair, A., Marriott, D., Ecker, D. J., et al. (1989). A multiubiquitin chain is confined to specific lysine in a targeted short-lived protein. Science, 243, 1576-1583.
    • (1989) Science , vol.243 , pp. 1576-1583
    • Chau, V.1    Tobias, J.W.2    Bachmair, A.3    Marriott, D.4    Ecker, D.J.5
  • 25
    • 0028146192 scopus 로고
    • Inhibition of proteolysis and cell cycle progression in a multiubiquitination-deficient yeast mutant
    • Finley, D., Sadis, S., Monia, B. P., Boucher, P., Ecker, D. J., et al. (1994). Inhibition of proteolysis and cell cycle progression in a multiubiquitination-deficient yeast mutant. Molecular and Cellular Biology, 14, 5501-5509.
    • (1994) Molecular and Cellular Biology , vol.14 , pp. 5501-5509
    • Finley, D.1    Sadis, S.2    Monia, B.P.3    Boucher, P.4    Ecker, D.J.5
  • 27
    • 34548225910 scopus 로고    scopus 로고
    • Coordinated regulation of Toll-like receptor and NOD2 signaling by K63-linked polyubiquitin chains
    • Abbott, D. W., Yang, Y., Hutti, J. E., Madhavarapu, S., Kelliher, M. A., et al. (2007). Coordinated regulation of Toll-like receptor and NOD2 signaling by K63-linked polyubiquitin chains. Molecular and Cellular Biology, 27, 6012-6025.
    • (2007) Molecular and Cellular Biology , vol.27 , pp. 6012-6025
    • Abbott, D.W.1    Yang, Y.2    Hutti, J.E.3    Madhavarapu, S.4    Kelliher, M.A.5
  • 28
    • 0034890328 scopus 로고    scopus 로고
    • Defining polyubiquitin chain topology
    • Chan, N. L., & Hill, C. P. (2001). Defining polyubiquitin chain topology. Natural Structural Biology, 8, 650-652.
    • (2001) Natural Structural Biology , vol.8 , pp. 650-652
    • Chan, N.L.1    Hill, C.P.2
  • 29
    • 0035903635 scopus 로고    scopus 로고
    • Sorting of proteins into multivesicular bodies: Ubiquitin-dependent and -independent targeting
    • Reggiori, F., & Pelham, H. R. B. (2001). Sorting of proteins into multivesicular bodies: Ubiquitin-dependent and -independent targeting. EMBO Journal, 20, 5176-5186.
    • (2001) EMBO Journal , vol.20 , pp. 5176-5186
    • Reggiori, F.1    Pelham, H.R.B.2
  • 31
    • 84858146420 scopus 로고    scopus 로고
    • Non-canonical ubiquitin-based signals for proteasomal degradation
    • Kravtsova-Ivantsiv, Y., & Ciechanover, A. (2012). Non-canonical ubiquitin-based signals for proteasomal degradation. Journal of Cell Science, 125, 539-548.
    • (2012) Journal of Cell Science , vol.125 , pp. 539-548
    • Kravtsova-Ivantsiv, Y.1    Ciechanover, A.2
  • 32
    • 0035947372 scopus 로고    scopus 로고
    • Impairment of the ubiquitin-proteasome system by protein aggregation
    • Bence, N. F., Sampat, R. M., & Kopito, R. R. (2001). Impairment of the ubiquitin-proteasome system by protein aggregation. Science, 292, 1552-1555.
    • (2001) Science , vol.292 , pp. 1552-1555
    • Bence, N.F.1    Sampat, R.M.2    Kopito, R.R.3
  • 33
    • 38449094180 scopus 로고    scopus 로고
    • Role of the ubiquitin proteasome system in Alzheimer's disease
    • Upadhya, S. C., & Hegde, A. N. (2007). Role of the ubiquitin proteasome system in Alzheimer's disease. BMC Biochemistry, 8(Suppl 1), S12.
    • (2007) BMC Biochemistry , vol.8 , Issue.SUPPL. 1
    • Upadhya, S.C.1    Hegde, A.N.2
  • 34
    • 0242363670 scopus 로고    scopus 로고
    • Molecular pathways of neurodegeneration in Parkinson's disease
    • Dawson, T. M., & Dawson, V. L. (2003). Molecular pathways of neurodegeneration in Parkinson's disease. Science, 302, 819-822.
    • (2003) Science , vol.302 , pp. 819-822
    • Dawson, T.M.1    Dawson, V.L.2
  • 35
    • 10744224825 scopus 로고    scopus 로고
    • Ubiquitin carboxy-terminal hydrolase L1 binds to and stabilizes monoubiquitin in neuron
    • Osaka, H., Wang, Y. L., Takada, K., Takizawa, S., Setsuie, R., et al. (2003). Ubiquitin carboxy-terminal hydrolase L1 binds to and stabilizes monoubiquitin in neuron. Human Molecular Genetics, 12, 1945-1958.
    • (2003) Human Molecular Genetics , vol.12 , pp. 1945-1958
    • Osaka, H.1    Wang, Y.L.2    Takada, K.3    Takizawa, S.4    Setsuie, R.5
  • 37
    • 77951919509 scopus 로고    scopus 로고
    • Degradation of ubiquitin: The fate of the cellular reaper
    • Shabek, N., & Ciechanover, A. (2010). Degradation of ubiquitin: The fate of the cellular reaper. Cell Cycle, 9, 523-530.
    • (2010) Cell Cycle , vol.9 , pp. 523-530
    • Shabek, N.1    Ciechanover, A.2
  • 38
    • 0032190090 scopus 로고    scopus 로고
    • The ubiquitin pathway in Parkinson's disease
    • Leroy, E., Boyer, R., Auburger, G., Leube, B., Ulm, G., et al. (1998). The ubiquitin pathway in Parkinson's disease. Nature, 395, 451-452.
    • (1998) Nature , vol.395 , pp. 451-452
    • Leroy, E.1    Boyer, R.2    Auburger, G.3    Leube, B.4    Ulm, G.5
  • 39
    • 0032846416 scopus 로고    scopus 로고
    • Intragenic deletion in the gene encoding ubiquitin carboxy-terminal hydrolase in gad mice
    • Saigoh, K., Wang, Y. L., Suh, J. G., Yamanishi, T., Sakai, Y., et al. (1999). Intragenic deletion in the gene encoding ubiquitin carboxy-terminal hydrolase in gad mice. Nature Genetics, 23, 47-51.
    • (1999) Nature Genetics , vol.23 , pp. 47-51
    • Saigoh, K.1    Wang, Y.L.2    Suh, J.G.3    Yamanishi, T.4    Sakai, Y.5
  • 40
    • 0037374587 scopus 로고    scopus 로고
    • Activity level controls postsynaptic composition and signaling via the ubiquitin-proteasome system
    • Ehlers, M. D. (2003). Activity level controls postsynaptic composition and signaling via the ubiquitin-proteasome system. Nature Neuroscience, 6, 231-242.
    • (2003) Nature Neuroscience , vol.6 , pp. 231-242
    • Ehlers, M.D.1
  • 41
    • 39049093652 scopus 로고    scopus 로고
    • Reduction in memory in passive avoidance learning, exploratory behaviour and synaptic plasticity in mice with a spontaneous deletion in the ubiquitin C-terminal hydrolase L1 gene
    • Sakurai, M., Sekiguchi, M., Zushida, K., Yamada, K., Nagamine, S., et al. (2008). Reduction in memory in passive avoidance learning, exploratory behaviour and synaptic plasticity in mice with a spontaneous deletion in the ubiquitin C-terminal hydrolase L1 gene. European Journal of Neuroscience, 27, 691-701.
    • (2008) European Journal of Neuroscience , vol.27 , pp. 691-701
    • Sakurai, M.1    Sekiguchi, M.2    Zushida, K.3    Yamada, K.4    Nagamine, S.5
  • 43
    • 0035903538 scopus 로고    scopus 로고
    • A novel active site-directed probe specific for deubiquitylating enzymes reveals proteasome association of USP14
    • Borodovsky, A., Kessler, B. M., Casagrande, R., Overkleeft, H. S., Wilkinson, K. D., et al. (2001). A novel active site-directed probe specific for deubiquitylating enzymes reveals proteasome association of USP14. EMBO Journal, 20, 5187-5196.
    • (2001) EMBO Journal , vol.20 , pp. 5187-5196
    • Borodovsky, A.1    Kessler, B.M.2    Casagrande, R.3    Overkleeft, H.S.4    Wilkinson, K.D.5
  • 44
    • 27744516748 scopus 로고    scopus 로고
    • Structure and mechanisms of the proteasome-associated deubiquitinating enzyme USP14
    • Hu, M., Li, P., Song, L., Jeffrey, P. D., Chenova, T. A., et al. (2005). Structure and mechanisms of the proteasome-associated deubiquitinating enzyme USP14. EMBO Journal, 24, 3747-3756.
    • (2005) EMBO Journal , vol.24 , pp. 3747-3756
    • Hu, M.1    Li, P.2    Song, L.3    Jeffrey, P.D.4    Chenova, T.A.5
  • 45
    • 77956527159 scopus 로고    scopus 로고
    • Enhancement of proteasome activity by a small-molecule inhibitor of USP14
    • Lee, B. H., Lee, M. J., Park, S., Oh, D. C., Elsasser, S., et al. (2010). Enhancement of proteasome activity by a small-molecule inhibitor of USP14. Nature, 467, 179-184.
    • (2010) Nature , vol.467 , pp. 179-184
    • Lee, B.H.1    Lee, M.J.2    Park, S.3    Oh, D.C.4    Elsasser, S.5
  • 46
    • 0036842130 scopus 로고    scopus 로고
    • Synaptic defects in ataxia mice result from a mutation in Usp14, encoding a ubiquitin-specific protease
    • Wilson, S. M., Bhattacharyya, B., Rachel, R. A., Coppola, V., Tessarollo, L., et al. (2002). Synaptic defects in ataxia mice result from a mutation in Usp14, encoding a ubiquitin-specific protease. Nature Genetics, 32, 420-425.
    • (2002) Nature Genetics , vol.32 , pp. 420-425
    • Wilson, S.M.1    Bhattacharyya, B.2    Rachel, R.A.3    Coppola, V.4    Tessarollo, L.5
  • 47
    • 69749110327 scopus 로고    scopus 로고
    • The proteasome-associated deubiquitinating enzyme Usp14 is essential for the maintenance of synaptic ubiquitin levels and the development of neuromuscular junctions
    • Chen, P. C., Qin, L. N., Li, X. M., Walters, B. J., Wilson, J. A., et al. (2009). The proteasome-associated deubiquitinating enzyme Usp14 is essential for the maintenance of synaptic ubiquitin levels and the development of neuromuscular junctions. Journal of Neuroscience, 29, 10909-10919.
    • (2009) Journal of Neuroscience , vol.29 , pp. 10909-10919
    • Chen, P.C.1    Qin, L.N.2    Li, X.M.3    Walters, B.J.4    Wilson, J.A.5
  • 48
    • 33750935146 scopus 로고    scopus 로고
    • Transgenic rescue of ataxia mice with neuronal-specific expression of ubiquitin-specific protease 14
    • Crimmins, S., Jin, Y., Wheeler, C., Huffman, A. K., Chapman, C., et al. (2006). Transgenic rescue of ataxia mice with neuronal-specific expression of ubiquitin-specific protease 14. Journal of Neuroscience, 26, 11423-11431.
    • (2006) Journal of Neuroscience , vol.26 , pp. 11423-11431
    • Crimmins, S.1    Jin, Y.2    Wheeler, C.3    Huffman, A.K.4    Chapman, C.5
  • 50
    • 34249007126 scopus 로고    scopus 로고
    • A ubiquitin stress response induces altered proteasome composition
    • Hanna, J., Meides, A., Zhang, D. P., & Finley, D. (2007). A ubiquitin stress response induces altered proteasome composition. Cell, 129, 747-759.
    • (2007) Cell , vol.129 , pp. 747-759
    • Hanna, J.1    Meides, A.2    Zhang, D.P.3    Finley, D.4
  • 51
    • 78650962524 scopus 로고    scopus 로고
    • Deconstruction for reconstruction: The role of proteolysis in neural plasticity and disease
    • Bingol, B., & Sheng, M. (2011). Deconstruction for reconstruction: The role of proteolysis in neural plasticity and disease. Neuron, 69, 22-32.
    • (2011) Neuron , vol.69 , pp. 22-32
    • Bingol, B.1    Sheng, M.2
  • 53
    • 77749323170 scopus 로고    scopus 로고
    • Ubiquitination acutely regulates presynaptic neurotransmitter release in mammalian neurons
    • Rinetti, G. V., & Schweizer, F. E. (2010). Ubiquitination acutely regulates presynaptic neurotransmitter release in mammalian neurons. Journal of Neuroscience, 30, 3157-3166.
    • (2010) Journal of Neuroscience , vol.30 , pp. 3157-3166
    • Rinetti, G.V.1    Schweizer, F.E.2


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