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Volumn 159, Issue 6, 2016, Pages 609-618

KIAA0368-deficiency affects disassembly of 26S proteasome under oxidative stress condition

Author keywords

Oxidative stress; Proteasome; Proteasome activators; Protein degradation; Ubiquitin

Indexed keywords

PROTEASOME; ATP DEPENDENT 26S PROTEASE;

EID: 84979047223     PISSN: 0021924X     EISSN: 17562651     Source Type: Journal    
DOI: 10.1093/jb/mvw006     Document Type: Article
Times cited : (18)

References (45)
  • 2
    • 71549144988 scopus 로고    scopus 로고
    • Lipid oxidation and peroxidation in CNS health and disease: From molecular mechanisms to therapeutic opportunities
    • Adibhatla, R.M. and Hatcher, J.F. (2010) Lipid oxidation and peroxidation in CNS health and disease: from molecular mechanisms to therapeutic opportunities. Antioxid. Redox. Signal. 12, 125-169.
    • (2010) Antioxid. Redox. Signal , vol.12 , pp. 125-169
    • Adibhatla, R.M.1    Hatcher, J.F.2
  • 4
    • 0028239163 scopus 로고    scopus 로고
    • Oxidative damage to proteins: Spectrophotometric method for carbonyl assay
    • Reznick, A.Z. and Packer, L. (1998) Oxidative damage to proteins: spectrophotometric method for carbonyl assay. Methods Enzymol. 233, 357-363.
    • (1998) Methods Enzymol , vol.233 , pp. 357-363
    • Reznick, A.Z.1    Packer, L.2
  • 7
    • 79955757695 scopus 로고    scopus 로고
    • Oxidative stress-mediated regulation of proteasome complexes
    • Aiken, C.T., Kaake, R.M., Wang, X., and Huang, L. (2011) Oxidative stress-mediated regulation of proteasome complexes. Mol. Cell. Proteomics 10, R110.006924.
    • (2011) Mol. Cell. Proteomics , vol.10 , pp. R110006924
    • Aiken, C.T.1    Kaake, R.M.2    Wang, X.3    Huang, L.4
  • 8
    • 77952543118 scopus 로고    scopus 로고
    • Mitochondrial redox metabolism: Aging, longevity and dietary effects
    • Page, M.M., Robb, E.L., Salway, K.D., and Stuart, J.A. (2010) Mitochondrial redox metabolism: Aging, longevity and dietary effects. Mech. Ageing Dev. 131, 242-252.
    • (2010) Mech. Ageing Dev , vol.131 , pp. 242-252
    • Page, M.M.1    Robb, E.L.2    Salway, K.D.3    Stuart, J.A.4
  • 9
    • 0025690898 scopus 로고
    • ATP-dependent proteases in prokaryotic and eukaryotic cells
    • Goldberg, A.L. (1990) ATP-dependent proteases in prokaryotic and eukaryotic cells. Semin. Cell Biol. 1, 423-432.
    • (1990) Semin. Cell Biol , vol.1 , pp. 423-432
    • Goldberg, A.L.1
  • 11
    • 3242714839 scopus 로고    scopus 로고
    • The ultimate nanoscale mincer: Assembly, structure and active sites of the 20S proteasome core
    • Heinemeyer, W., Ramos, P.C., and Dohmen, R.J. (2004) The ultimate nanoscale mincer: Assembly, structure and active sites of the 20S proteasome core. Cell. Mol. Life Sci. 61, 1562-1578.
    • (2004) Cell. Mol. Life Sci , vol.61 , pp. 1562-1578
    • Heinemeyer, W.1    Ramos, P.C.2    Dohmen, R.J.3
  • 14
    • 0034964524 scopus 로고    scopus 로고
    • The axial channel of the proteasome core particle is gated by the Rpt2 ATPase and controls both substrate entry and product release
    • Kohhler, A., Cascio, P., Leggett, D.S., Woo, K.M., Goldberg, A.L., and Finley, D. (2001) The axial channel of the proteasome core particle is gated by the Rpt2 ATPase and controls both substrate entry and product release. Mol. Cell 7, 1143-1152.
    • (2001) Mol. Cell , vol.7 , pp. 1143-1152
    • Kohhler, A.1    Cascio, P.2    Leggett, D.S.3    Woo, K.M.4    Goldberg, A.L.5    Finley, D.6
  • 17
    • 0028235965 scopus 로고
    • A 26 S protease subunit that binds ubiquitin conjugates
    • Deveraux, Q., Ustrell, V., Pickart, C., and Rechsteiner, M. (1994) A 26 S protease subunit that binds ubiquitin conjugates. J. Biol. Chem. 269, 7059-7061.
    • (1994) J. Biol. Chem , vol.269 , pp. 7059-7061
    • Deveraux, Q.1    Ustrell, V.2    Pickart, C.3    Rechsteiner, M.4
  • 18
    • 0037129213 scopus 로고    scopus 로고
    • A proteasomal ATPase subunit recognizes the polyubiquitin degradation signal
    • Lam, Y.A., Lawson, T.G., Velayutham, M., Zweler, J.L., and Pickart, C.M. (2002) A proteasomal ATPase subunit recognizes the polyubiquitin degradation signal. Nature 416, 763-767.
    • (2002) Nature , vol.416 , pp. 763-767
    • Lam, Y.A.1    Lawson, T.G.2    Velayutham, M.3    Zweler, J.L.4    Pickart, C.M.5
  • 19
    • 0036091895 scopus 로고    scopus 로고
    • Ubiquitin chained and crosslinked
    • Finley, D. (2002) Ubiquitin chained and crosslinked. Nat. Cell. Biol. 4, E121-E123.
    • (2002) Nat. Cell. Biol , vol.4 , pp. 121-123
    • Finley, D.1
  • 25
    • 36849059755 scopus 로고    scopus 로고
    • Stability of the proteasome can be regulated allosterically through engagement of its proteolytic active sites
    • Kleijnen, M.F., Roelofs, J., Park, S., Hathaway, N.A., Glickman, M., King, R.W., and Finley, D. (2007) Stability of the proteasome can be regulated allosterically through engagement of its proteolytic active sites. Nat. Struct. Mol. Biol. 14, 1180-1188.
    • (2007) Nat. Struct. Mol. Biol , vol.14 , pp. 1180-1188
    • Kleijnen, M.F.1    Roelofs, J.2    Park, S.3    Hathaway, N.A.4    Glickman, M.5    King, R.W.6    Finley, D.7
  • 26
    • 78649980437 scopus 로고    scopus 로고
    • Regulation of the 26S proteasome complex during oxidative stress
    • Wang, X., Yen, J., Kaiser, P., and Huang, L. (2010) Regulation of the 26S proteasome complex during oxidative stress. Sci. Signal. 3, ra88.
    • (2010) Sci. Signal , vol.3 , pp. 88
    • Wang, X.1    Yen, J.2    Kaiser, P.3    Huang, L.4
  • 27
    • 80054702676 scopus 로고    scopus 로고
    • Structural defects in the regulatory particle-core particle interface of the proteasome induce a novel proteasome stress response
    • Park, S., Kim, W., Tian, G., Gygi, S.P., and Finley, D. (2011) Structural defects in the regulatory particle-core particle interface of the proteasome induce a novel proteasome stress response. J. Biol. Chem. 286, 36652-36666.
    • (2011) J. Biol. Chem. , vol.286 , pp. 36652-36666
    • Park, S.1    Kim, W.2    Tian, G.3    Gygi, S.P.4    Finley, D.5
  • 28
    • 84885586226 scopus 로고    scopus 로고
    • The proteasomeassociated protein Ecm29 inhibits proteasomal ATPase activity and in vivo protein degradation by the proteasome
    • De La Mota Peynado, A., Lee, S.Y., Pierce, B.M., Wani, P., Singh, C.R., and Roelofs, J. (2013) The proteasomeassociated protein Ecm29 inhibits proteasomal ATPase activity and in vivo protein degradation by the proteasome. J. Biol. Chem. 288, 29467-29481.
    • (2013) J. Biol. Chem. , vol.288 , pp. 29467-29481
    • De La Mota Peynado, A.1    Lee, S.Y.2    Pierce, B.M.3    Wani, P.4    Singh, C.R.5    Roelofs, J.6
  • 29
    • 77955503621 scopus 로고    scopus 로고
    • Ecm29 fulfils quality control functions in proteasome assembly
    • Lehmann, A., Niewienda, A., Jechow, K., Janek, K., and Enenkel, C. (2010) Ecm29 fulfils quality control functions in proteasome assembly. Mol. Cell 38, 879-888.
    • (2010) Mol. Cell , vol.38 , pp. 879-888
    • Lehmann, A.1    Niewienda, A.2    Jechow, K.3    Janek, K.4    Enenkel, C.5
  • 30
    • 11144225834 scopus 로고    scopus 로고
    • Characterization of mammalian Ecm29, a 26 S proteasome- Associated protein that localizes to the nucleus and membrane vesicles
    • Gorbea, C., Goellner, G.M., Teter, K., Holmes, R.K., and Rechsteiner, M. (2004) Characterization of mammalian Ecm29, a 26 S proteasome- Associated protein that localizes to the nucleus and membrane vesicles. J. Biol. Chem. 279, 54849-54861.
    • (2004) J. Biol. Chem , vol.279 , pp. 54849-54861
    • Gorbea, C.1    Goellner, G.M.2    Teter, K.3    Holmes, R.K.4    Rechsteiner, M.5
  • 31
    • 77957817388 scopus 로고    scopus 로고
    • A protein interaction network for Ecm29 links the 26 S proteasome to molecular motors and endosomal components
    • Gorbea, C., Pratt, G., Ustrell, V., Bell, R., Sahasrabudhe, S., Hughes, R.E., and Rechsteiner, M. (2010) A protein interaction network for Ecm29 links the 26 S proteasome to molecular motors and endosomal components. J. Biol. Chem. 285, 31616-31633.
    • (2010) J. Biol. Chem , vol.285 , pp. 31616-31633
    • Gorbea, C.1    Pratt, G.2    Ustrell, V.3    Bell, R.4    Sahasrabudhe, S.5    Hughes, R.E.6    Rechsteiner, M.7
  • 32
    • 84885793620 scopus 로고    scopus 로고
    • Depletion of the 26S proteasome adaptor Ecm29 increases Toll-like receptor 3 signaling
    • Gorbea, C., Rechsteiner, M., Vallejo, J.G., and Bowles, N.E. (2013) Depletion of the 26S proteasome adaptor Ecm29 increases Toll-like receptor 3 signaling. Sci. Signal. 6, ra86.
    • (2013) Sci. Signal , vol.6 , pp. 86
    • Gorbea, C.1    Rechsteiner, M.2    Vallejo, J.G.3    Bowles, N.E.4
  • 33
    • 80052981806 scopus 로고    scopus 로고
    • Ubiquitin ligase activity of Cul3-KLHL7 protein is attenuated by autosomal dominant retinitis pigmentosa causative mutation
    • Kigoshi, Y., Tsuruta, F., and Chiba, T. (2011) Ubiquitin ligase activity of Cul3-KLHL7 protein is attenuated by autosomal dominant retinitis pigmentosa causative mutation. J. Biol. Chem. 286, 33613-33621.
    • (2011) J. Biol. Chem , vol.286 , pp. 33613-33621
    • Kigoshi, Y.1    Tsuruta, F.2    Chiba, T.3
  • 37
    • 77953467032 scopus 로고    scopus 로고
    • Characterization of the brain 26S proteasome and its interacting proteins
    • Tai, H.C., Besche, H., Goldberg, A.L., Schuman, E.M. (2010) Characterization of the brain 26S proteasome and its interacting proteins. Front. Mol. Neurosci. 3, 12 38.
    • (2010) Front. Mol. Neurosci , vol.3 , Issue.12 , pp. 38
    • Tai, H.C.1    Besche, H.2    Goldberg, A.L.3    Schuman, E.M.4
  • 38
    • 33750710080 scopus 로고    scopus 로고
    • Protein oxidation and aging
    • Stadtman, E.R. (2006) Protein oxidation and aging. Free Radic. Res. 40, 1250-1258.
    • (2006) Free Radic. Res , vol.40 , pp. 1250-1258
    • Stadtman, E.R.1
  • 39
    • 0035072229 scopus 로고    scopus 로고
    • Degradation of oxidized proteins by the 20S proteasome
    • Davies, K.J. (2001) Degradation of oxidized proteins by the 20S proteasome. Biochimie 83, 301-310.
    • (2001) Biochimie , vol.83 , pp. 301-310
    • Davies, K.J.1
  • 41
    • 0030881029 scopus 로고    scopus 로고
    • Activity of ubiquitin-dependent pathway in response to oxidative stress: Ubiquitin- Activating enzyme is transiently upregulated
    • Shang, F., Gong, X., and Taylor, A. (1997) Activity of ubiquitin-dependent pathway in response to oxidative stress: ubiquitin- Activating enzyme is transiently upregulated. J. Biol. Chem. 272, 23086-23093.
    • (1997) J. Biol. Chem , vol.272 , pp. 23086-23093
    • Shang, F.1    Gong, X.2    Taylor, A.3
  • 42
    • 84861869794 scopus 로고    scopus 로고
    • Differential roles of proteasome and immunoproteasome regulators Pa28ab, Pa28g and Pa200 in the degradation of oxidized proteins
    • Pickering, A.M. and Davies, K.J. (2012) Differential roles of proteasome and immunoproteasome regulators Pa28ab, Pa28g and Pa200 in the degradation of oxidized proteins. Arch. Biochem. Biophys. 523, 181-190.
    • (2012) Arch. Biochem. Biophys , vol.523 , pp. 181-190
    • Pickering, A.M.1    Davies, K.J.2
  • 43
    • 1942489340 scopus 로고    scopus 로고
    • New HEAT-like repeat motifs in proteins regulating proteasome structure and function
    • Kajava, A.V., Gorbea, C., Ortega, J., Rechsteiner, M., and Steven, A.C. (2004) New HEAT-like repeat motifs in proteins regulating proteasome structure and function. J. Struct. Biol. 146, 425-430.
    • (2004) J. Struct. Biol. , vol.146 , pp. 425-430
    • Kajava, A.V.1    Gorbea, C.2    Ortega, J.3    Rechsteiner, M.4    Steven, A.C.5
  • 44
    • 0242522904 scopus 로고    scopus 로고
    • Blm3 is part of nascent proteasomes and is involved in a late stage of nuclear proteasome assembly
    • Fehlker, M., Wendler, P., Lehmann, A., and Enenkel, C. (2003) Blm3 is part of nascent proteasomes and is involved in a late stage of nuclear proteasome assembly. EMBO Rep. 4, 959-963.
    • (2003) EMBO Rep , vol.4 , pp. 959-963
    • Fehlker, M.1    Wendler, P.2    Lehmann, A.3    Enenkel, C.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.