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Volumn 114, Issue 26, 2017, Pages E5158-E5166

Deubiquitinating enzyme VCIP135 dictates the duration of botulinum neurotoxin type A intoxication

Author keywords

Motoneuron; Synaptic transmission; Synaptosomal Associated protein 25; Toxin persistence; USP9X

Indexed keywords

AMINO ACID; BOTULINUM TOXIN A; CELL PROTEIN; DEUBIQUITINASE; DOXYCYCLINE; EPOXOMICIN; HECTD2 PROTEIN; PROTEASOME; SYNAPTOSOMAL ASSOCIATED PROTEIN 25; UBIQUITIN LIGASE HECTD2; UBIQUITIN PROTEIN LIGASE; UNCLASSIFIED DRUG; VALOSIN CONTAINING PROTEIN; VALOSIN CONTAINING PROTEIN COMPLEX INTERACTING PROTEIN 135 KDA; ENZYME INHIBITOR; HECTD2 PROTEIN, HUMAN; HECTD2 PROTEIN, MOUSE; PROTEINASE; SNAP25 PROTEIN, HUMAN; SNAP25 PROTEIN, MOUSE; VCIP135 PROTEIN, HUMAN;

EID: 85021428174     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1621076114     Document Type: Article
Times cited : (47)

References (44)
  • 1
    • 0033731911 scopus 로고    scopus 로고
    • Identification of the characteristics that underlie botulinum toxin potency: Implications for designing novel drugs
    • Simpson LL (2000) Identification of the characteristics that underlie botulinum toxin potency: Implications for designing novel drugs. Biochimie 82:943-953.
    • (2000) Biochimie , vol.82 , pp. 943-953
    • Simpson, L.L.1
  • 2
    • 0022463687 scopus 로고
    • Clostridial neurotoxins: Handling and action at the cellular and molecular level
    • Habermann E, Dreyer F (1986) Clostridial neurotoxins: Handling and action at the cellular and molecular level. Curr Top Microbiol Immunol 129:93-179.
    • (1986) Curr Top Microbiol Immunol , vol.129 , pp. 93-179
    • Habermann, E.1    Dreyer, F.2
  • 5
    • 0029613765 scopus 로고
    • Structure and function of tetanus and botulinum neurotoxins
    • Montecucco C, Schiavo G (1995) Structure and function of tetanus and botulinum neurotoxins. Q Rev Biophys 28:423-472.
    • (1995) Q Rev Biophys , vol.28 , pp. 423-472
    • Montecucco, C.1    Schiavo, G.2
  • 6
    • 0021243873 scopus 로고
    • Acceptors for botulinum neurotoxin reside on motor nerve terminals and mediate its internalization
    • Dolly JO, Black J, Williams RS, Melling J (1984) Acceptors for botulinum neurotoxin reside on motor nerve terminals and mediate its internalization. Nature 307:457-460.
    • (1984) Nature , vol.307 , pp. 457-460
    • Dolly, J.O.1    Black, J.2    Williams, R.S.3    Melling, J.4
  • 7
    • 84893825555 scopus 로고    scopus 로고
    • The blockade of the neurotransmitter release apparatus by botulinum neurotoxins
    • Pantano S, Montecucco C (2014) The blockade of the neurotransmitter release apparatus by botulinum neurotoxins. Cell Mol Life Sci 71:793-811.
    • (2014) Cell Mol Life Sci , vol.71 , pp. 793-811
    • Pantano, S.1    Montecucco, C.2
  • 8
    • 0035961566 scopus 로고    scopus 로고
    • Botulinum toxin as a biological weapon: Medical and public health management
    • Working Group on Civilian Biodefense
    • Arnon SS, et al.; Working Group on Civilian Biodefense (2001) Botulinum toxin as a biological weapon: Medical and public health management. JAMA 285:1059-1070.
    • (2001) JAMA , vol.285 , pp. 1059-1070
    • Arnon, S.S.1
  • 9
    • 0032515187 scopus 로고    scopus 로고
    • Different time courses of recovery after poisoning with botulinum neurotoxin serotypes A and E in humans
    • Eleopra R, Tugnoli V, Rossetto O, De Grandis, D, Montecucco C (1998) Different time courses of recovery after poisoning with botulinum neurotoxin serotypes A and E in humans. Neurosci Lett 256:135-138.
    • (1998) Neurosci Lett , vol.256 , pp. 135-138
    • Eleopra, R.1    Tugnoli, V.2    Rossetto, O.3    Montecucco, C.4    De Grandis, D.5
  • 10
    • 84875814383 scopus 로고    scopus 로고
    • Persistence of Botulinum neurotoxin inactivation of nerve function
    • Shoemaker CB, Oyler GA (2013) Persistence of Botulinum neurotoxin inactivation of nerve function. Curr Top Microbiol Immunol 364:179-196.
    • (2013) Curr Top Microbiol Immunol , vol.364 , pp. 179-196
    • Shoemaker, C.B.1    Oyler, G.A.2
  • 11
    • 84904510042 scopus 로고    scopus 로고
    • Botulinum neurotoxins: Genetic, structural and mechanistic insights
    • Rossetto O, Pirazzini M, Montecucco C (2014) Botulinum neurotoxins: Genetic, structural and mechanistic insights. Nat Rev Microbiol 12:535-549.
    • (2014) Nat Rev Microbiol , vol.12 , pp. 535-549
    • Rossetto, O.1    Pirazzini, M.2    Montecucco, C.3
  • 12
    • 78049242459 scopus 로고    scopus 로고
    • Targeting botulinum neurotoxin persistence by the ubiquitinproteasome system
    • Tsai YC, et al. (2010) Targeting botulinum neurotoxin persistence by the ubiquitinproteasome system. Proc Natl Acad Sci USA 107:16554-16559.
    • (2010) Proc Natl Acad Sci USA , vol.107 , pp. 16554-16559
    • Tsai, Y.C.1
  • 13
    • 0032776446 scopus 로고    scopus 로고
    • Persistence of botulinum neurotoxin action in cultured spinal cord cells
    • Keller JE, Neale EA, Oyler G, Adler M (1999) Persistence of botulinum neurotoxin action in cultured spinal cord cells. FEBS Lett 456:137-142.
    • (1999) FEBS Lett , vol.456 , pp. 137-142
    • Keller, J.E.1    Neale, E.A.2    Oyler, G.3    Adler, M.4
  • 14
    • 84896383439 scopus 로고    scopus 로고
    • Persistence of botulinum neurotoxin a subtypes 1-5 in primary rat spinal cord cells
    • Whitemarsh RC, Tepp WH, Johnson EA, Pellett S (2014) Persistence of botulinum neurotoxin a subtypes 1-5 in primary rat spinal cord cells. PLoS One 9:e90252.
    • (2014) PLoS One , vol.9 , pp. e90252
    • Whitemarsh, R.C.1    Tepp, W.H.2    Johnson, E.A.3    Pellett, S.4
  • 15
    • 0028069674 scopus 로고
    • Proteolysis of SNAP-25 by types E and A botulinal neurotoxins
    • Binz T, et al. (1994) Proteolysis of SNAP-25 by types E and A botulinal neurotoxins. J Biol Chem 269:1617-1620.
    • (1994) J Biol Chem , vol.269 , pp. 1617-1620
    • Binz, T.1
  • 16
    • 84870495262 scopus 로고    scopus 로고
    • Differential regulation of HMG-CoA reductase and Insig-1 by enzymes of the ubiquitin-proteasome system
    • Tsai YC, et al. (2012) Differential regulation of HMG-CoA reductase and Insig-1 by enzymes of the ubiquitin-proteasome system. Mol Biol Cell 23:4484-4494.
    • (2012) Mol Biol Cell , vol.23 , pp. 4484-4494
    • Tsai, Y.C.1
  • 17
    • 0038121109 scopus 로고    scopus 로고
    • Specificity of short interfering RNA determined through gene expression signatures
    • Semizarov D, et al. (2003) Specificity of short interfering RNA determined through gene expression signatures. Proc Natl Acad Sci USA 100:6347-6352.
    • (2003) Proc Natl Acad Sci USA , vol.100 , pp. 6347-6352
    • Semizarov, D.1
  • 18
    • 0037685280 scopus 로고    scopus 로고
    • Expression profiling reveals off-Target gene regulation by RNAi
    • Jackson AL, et al. (2003) Expression profiling reveals off-Target gene regulation by RNAi. Nat Biotechnol 21:635-637.
    • (2003) Nat Biotechnol , vol.21 , pp. 635-637
    • Jackson, A.L.1
  • 19
    • 0035954743 scopus 로고    scopus 로고
    • Ubiquitination-dependent mechanisms regulate synaptic growth and function
    • DiAntonio A, 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
  • 20
    • 81755185877 scopus 로고    scopus 로고
    • Α-Synuclein fate is determined by USP9X-regulated monoubiquitination
    • Rott R, et al. (2011) α-Synuclein fate is determined by USP9X-regulated monoubiquitination. Proc Natl Acad Sci USA 108:18666-18671.
    • (2011) Proc Natl Acad Sci USA , vol.108 , pp. 18666-18671
    • Rott, R.1
  • 21
    • 79953144994 scopus 로고    scopus 로고
    • Zymophagy, a novel selective autophagy pathway mediated by VMP1-USP9x-p62, prevents pancreatic cell death
    • Grasso D, et al. (2011) Zymophagy, a novel selective autophagy pathway mediated by VMP1-USP9x-p62, prevents pancreatic cell death. J Biol Chem 286:8308-8324.
    • (2011) J Biol Chem , vol.286 , pp. 8308-8324
    • Grasso, D.1
  • 22
    • 84887566614 scopus 로고    scopus 로고
    • MCL1 is critical for mitochondrial function and autophagy in the heart
    • Thomas RL, Gustafsson AB (2013) MCL1 is critical for mitochondrial function and autophagy in the heart. Autophagy 9:1902-1903.
    • (2013) Autophagy , vol.9 , pp. 1902-1903
    • Thomas, R.L.1    Gustafsson, A.B.2
  • 23
    • 78751621004 scopus 로고    scopus 로고
    • MCL-1 is a stress sensor that regulates autophagy in a developmentally regulated manner
    • Germain M, et al. (2011) MCL-1 is a stress sensor that regulates autophagy in a developmentally regulated manner. EMBO J 30:395-407.
    • (2011) EMBO J , vol.30 , pp. 395-407
    • Germain, M.1
  • 24
    • 73849083434 scopus 로고    scopus 로고
    • Deubiquitinase USP9X stabilizes MCL1 and promotes tumour cell survival
    • Schwickart M, et al. (2010) Deubiquitinase USP9X stabilizes MCL1 and promotes tumour cell survival. Nature 463:103-107.
    • (2010) Nature , vol.463 , pp. 103-107
    • Schwickart, M.1
  • 25
    • 71449117666 scopus 로고    scopus 로고
    • Ubiquitin-like sequence in ASK1 plays critical roles in the recognition and stabilization by USP9X and oxidative stress-induced cell death
    • Nagai H, et al. (2009) Ubiquitin-like sequence in ASK1 plays critical roles in the recognition and stabilization by USP9X and oxidative stress-induced cell death. Mol Cell 36:805-818.
    • (2009) Mol Cell , vol.36 , pp. 805-818
    • Nagai, H.1
  • 26
    • 84907192654 scopus 로고    scopus 로고
    • Regulation of proximal T cell receptor signaling and tolerance induction by deubiquitinase Usp9X
    • Naik E, et al. (2014) Regulation of proximal T cell receptor signaling and tolerance induction by deubiquitinase Usp9X. J Exp Med 211:1947-1955.
    • (2014) J Exp Med , vol.211 , pp. 1947-1955
    • Naik, E.1
  • 27
    • 1842509180 scopus 로고    scopus 로고
    • VCIP135 acts as a deubiquitinating enzyme during p97-p47-mediated reassembly of mitotic Golgi fragments
    • Wang Y, Satoh A, Warren G, Meyer HH (2004) VCIP135 acts as a deubiquitinating enzyme during p97-p47-mediated reassembly of mitotic Golgi fragments. J Cell Biol 164:973-978.
    • (2004) J Cell Biol , vol.164 , pp. 973-978
    • Wang, Y.1    Satoh, A.2    Warren, G.3    Meyer, H.H.4
  • 28
    • 0037049466 scopus 로고    scopus 로고
    • VCIP135, a novel essential factor for p97/p47-mediated membrane fusion, is required for Golgi and ER assembly in vivo
    • Uchiyama K, et al. (2002) VCIP135, a novel essential factor for p97/p47-mediated membrane fusion, is required for Golgi and ER assembly in vivo. J Cell Biol 159: 855-866.
    • (2002) J Cell Biol , vol.159 , pp. 855-866
    • Uchiyama, K.1
  • 29
    • 26044483546 scopus 로고    scopus 로고
    • NSF/SNAPs and p97/p47/VCIP135 are sequentially required for cell cycle-dependent reformation of the ER network
    • Kano F, et al. (2005) NSF/SNAPs and p97/p47/VCIP135 are sequentially required for cell cycle-dependent reformation of the ER network. Genes Cells 10:989-999.
    • (2005) Genes Cells , vol.10 , pp. 989-999
    • Kano, F.1
  • 30
    • 80052262926 scopus 로고    scopus 로고
    • VCIP135 deubiquitinase and its binding protein, WAC, in p97ATPase-mediated membrane fusion
    • Totsukawa G, et al. (2011) VCIP135 deubiquitinase and its binding protein, WAC, in p97ATPase-mediated membrane fusion. EMBO J 30:3581-3593.
    • (2011) EMBO J , vol.30 , pp. 3581-3593
    • Totsukawa, G.1
  • 31
    • 79955433958 scopus 로고    scopus 로고
    • Association of botulinum neurotoxin serotype A light chain with plasma membrane-bound SNAP-25
    • Chen S, Barbieri JT (2011) Association of botulinum neurotoxin serotype A light chain with plasma membrane-bound SNAP-25. J Biol Chem 286:15067-15072.
    • (2011) J Biol Chem , vol.286 , pp. 15067-15072
    • Chen, S.1    Barbieri, J.T.2
  • 32
    • 84937112097 scopus 로고    scopus 로고
    • The proinflammatory role of HECTD2 in innate immunity and experimental lung injury
    • 295ra109
    • Coon TA, et al. (2015) The proinflammatory role of HECTD2 in innate immunity and experimental lung injury. Sci Transl Med 7:295ra109.
    • (2015) Sci Transl Med , vol.7
    • Coon, T.A.1
  • 33
    • 61449198575 scopus 로고    scopus 로고
    • HECTD2 is associated with susceptibility to mouse and human prion disease
    • Lloyd SE, et al. (2009) HECTD2 is associated with susceptibility to mouse and human prion disease. PLoS Genet 5:e1000383.
    • (2009) PLoS Genet , vol.5 , pp. e1000383
    • Lloyd, S.E.1
  • 34
    • 70349758644 scopus 로고    scopus 로고
    • HECTD2, a candidate susceptibility gene for Alzheimer's disease on 10q
    • Lloyd SE, Rossor M, Fox N, Mead S, Collinge J (2009) HECTD2, a candidate susceptibility gene for Alzheimer's disease on 10q. BMC Med Genet 10:90.
    • (2009) BMC Med Genet , vol.10 , pp. 90
    • Lloyd, S.E.1    Rossor, M.2    Fox, N.3    Mead, S.4    Collinge, J.5
  • 35
    • 84949033508 scopus 로고    scopus 로고
    • Snake and spider toxins induce a rapid recovery of function of botulinum neurotoxin paralysed neuromuscular junction
    • Duregotti E, et al. (2015) Snake and spider toxins induce a rapid recovery of function of botulinum neurotoxin paralysed neuromuscular junction. Toxins (Basel) 7: 5322-5336.
    • (2015) Toxins (Basel) , vol.7 , pp. 5322-5336
    • Duregotti, E.1
  • 36
    • 0037428398 scopus 로고    scopus 로고
    • Evaluation of the therapeutic usefulness of botulinum neurotoxin B, C1, E, and F compared with the long lasting type A. Basis for distinct durations of inhibition of exocytosis in central neurons
    • Foran PG, et al. (2003) Evaluation of the therapeutic usefulness of botulinum neurotoxin B, C1, E, and F compared with the long lasting type A. Basis for distinct durations of inhibition of exocytosis in central neurons. in J Biol Chem 278:1363-1371.
    • (2003) J Biol Chem , vol.278 , pp. 1363-1371
    • Foran, P.G.1
  • 37
    • 0033601298 scopus 로고    scopus 로고
    • Rescue of exocytosis in botulinum toxin A-poisoned chromaffin cells by expression of cleavageresistant SNAP-25. Identification of the minimal essential C-Terminal residues
    • O'Sullivan GA, Mohammed N, Foran PG, Lawrence GW, Oliver Dolly J (1999) Rescue of exocytosis in botulinum toxin A-poisoned chromaffin cells by expression of cleavageresistant SNAP-25. Identification of the minimal essential C-Terminal residues. J Biol Chem 274:36897-36904.
    • (1999) J Biol Chem , vol.274 , pp. 36897-36904
    • O'Sullivan, G.A.1    Mohammed, N.2    Foran, P.G.3    Lawrence, G.W.4    Oliver, D.J.5
  • 38
    • 79955023053 scopus 로고    scopus 로고
    • Embryonic stem cell-derived motoneurons provide a highly sensitive cell culture model for botulinum neurotoxin studies, with implications for highthroughput drug discovery
    • Kiris E, et al. (2011) Embryonic stem cell-derived motoneurons provide a highly sensitive cell culture model for botulinum neurotoxin studies, with implications for highthroughput drug discovery. Stem Cell Res (Amst) 6:195-205.
    • (2011) Stem Cell Res (Amst) , vol.6 , pp. 195-205
    • Kiris, E.1
  • 39
    • 0018425620 scopus 로고
    • Toxicity of botulinum toxin: A stoichiometric model for the locus of its extraordinary potency and persistence at the neuromuscular junction
    • Hanig JP, Lamanna C (1979) Toxicity of botulinum toxin: A stoichiometric model for the locus of its extraordinary potency and persistence at the neuromuscular junction. J Theor Biol 77:107-113.
    • (1979) J Theor Biol , vol.77 , pp. 107-113
    • Hanig, J.P.1    Lamanna, C.2
  • 40
    • 3242797403 scopus 로고    scopus 로고
    • Is the light chain subcellular localization an important factor in botulinum toxin duration of action?
    • Fernández-Salas E, Ho H, Garay P, Steward LE, Aoki KR (2004) Is the light chain subcellular localization an important factor in botulinum toxin duration of action? Mov Disord 19:S23-S34.
    • (2004) Mov Disord , vol.19 , pp. S23-S34
    • Fernández-Salas, E.1    Ho, H.2    Garay, P.3    Steward, L.E.4    Aoki, K.R.5
  • 41
    • 12144291021 scopus 로고    scopus 로고
    • Plasma membrane localization signals in the light chain of botulinum neurotoxin
    • Fernández-Salas E, et al. (2004) Plasma membrane localization signals in the light chain of botulinum neurotoxin. Proc Natl Acad Sci USA 101:3208-3213.
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 3208-3213
    • Fernández-Salas, E.1
  • 42
    • 79956353397 scopus 로고    scopus 로고
    • Accelerated neuronal cell recovery from Botulinum neurotoxin intoxication by targeted ubiquitination
    • Kuo CL, Oyler GA, Shoemaker CB (2011) Accelerated neuronal cell recovery from Botulinum neurotoxin intoxication by targeted ubiquitination. PLoS One 6:e20352.
    • (2011) PLoS One , vol.6 , pp. e20352
    • Kuo, C.L.1    Oyler, G.A.2    Shoemaker, C.B.3
  • 43
    • 67649634849 scopus 로고    scopus 로고
    • Defining the human deubiquitinating enzyme interaction landscape
    • Sowa ME, Bennett EJ, Gygi SP, Harper JW (2009) Defining the human deubiquitinating enzyme interaction landscape. Cell 138:389-403.
    • (2009) Cell , vol.138 , pp. 389-403
    • Sowa, M.E.1    Bennett, E.J.2    Gygi, S.P.3    Harper, J.W.4
  • 44
    • 0030919433 scopus 로고    scopus 로고
    • Subcellular localization and ubiquitinconjugating enzyme (E2) interactions of mammalian HECT family ubiquitin protein ligases
    • Hatakeyama S, Jensen JP, Weissman AM (1997) Subcellular localization and ubiquitinconjugating enzyme (E2) interactions of mammalian HECT family ubiquitin protein ligases. J Biol Chem 272:15085-15092.
    • (1997) J Biol Chem , vol.272 , pp. 15085-15092
    • Hatakeyama, S.1    Jensen, J.P.2    Weissman, A.M.3


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