메뉴 건너뛰기




Volumn 167, Issue 6, 2007, Pages 663-674

Proteasomes and proteasome activator 200 kDa (PA200) accumulate on chromatin in response to ionizing radiation

Author keywords

[No Author keywords available]

Indexed keywords

MESSENGER RNA; PROTEASOME; PROTEASOME ACTIVATOR 200 KDA PROTEIN; PROTEIN; UNCLASSIFIED DRUG; NUCLEAR PROTEIN; PROTEASOME ACTIVATOR 200 KDA, HUMAN;

EID: 34447549100     PISSN: 00337587     EISSN: None     Source Type: Journal    
DOI: 10.1667/RR0690.1     Document Type: Article
Times cited : (48)

References (46)
  • 1
    • 0032867676 scopus 로고    scopus 로고
    • The 26S proteasome: A molecular machine designed for controlled proteolysis
    • D. Voges, P. Zwickl and W. Baumeister, The 26S proteasome: A molecular machine designed for controlled proteolysis. Annu. Rev. Biochem. 68, 1015-1068 (1999).
    • (1999) Annu. Rev. Biochem , vol.68 , pp. 1015-1068
    • Voges, D.1    Zwickl, P.2    Baumeister, W.3
  • 2
    • 0032919345 scopus 로고    scopus 로고
    • The role of the ubiquitin-proteasome pathway in apoptosis
    • R. Z. Orlowski, The role of the ubiquitin-proteasome pathway in apoptosis. Cell Death. Differ. 6, 303-313 (1999).
    • (1999) Cell Death. Differ , vol.6 , pp. 303-313
    • Orlowski, R.Z.1
  • 3
    • 0033011162 scopus 로고    scopus 로고
    • The role of the proteasome system and the proteasome activator PA28 complex in the cellular immune response
    • P. M. Kloetzel, A. Soza and R. Stohwasser, The role of the proteasome system and the proteasome activator PA28 complex in the cellular immune response. Biol. Chem. 380, 293-297 (1999).
    • (1999) Biol. Chem , vol.380 , pp. 293-297
    • Kloetzel, P.M.1    Soza, A.2    Stohwasser, R.3
  • 4
    • 0029186274 scopus 로고
    • Roles of proteasomes in cell growth
    • A. Ichihara and K. Tanaka, Roles of proteasomes in cell growth. Mol. Biol. Rep. 21, 49-52 (1995).
    • (1995) Mol. Biol. Rep , vol.21 , pp. 49-52
    • Ichihara, A.1    Tanaka, K.2
  • 5
    • 0030016595 scopus 로고    scopus 로고
    • Structure and functions of the 20S and 26S proteasomes
    • O. Coux, K. Tanaka and A. L. Goldberg, Structure and functions of the 20S and 26S proteasomes. Annu. Rev. Biochem. 65, 801-847 (1996).
    • (1996) Annu. Rev. Biochem , vol.65 , pp. 801-847
    • Coux, O.1    Tanaka, K.2    Goldberg, A.L.3
  • 7
    • 0031973736 scopus 로고    scopus 로고
    • Immunoproteasome assembly: Cooperative incorporation of interferon gamma (IFN-gamma)-inducible subunits
    • T. A. Griffin, D. Nandi, M. Cruz, H. J. Fehling, L. V. Kaer, J. J. Monaco and R. A. Colbert, Immunoproteasome assembly: Cooperative incorporation of interferon gamma (IFN-gamma)-inducible subunits. J. Exp. Med. 187, 97-104 (1998).
    • (1998) J. Exp. Med , vol.187 , pp. 97-104
    • Griffin, T.A.1    Nandi, D.2    Cruz, M.3    Fehling, H.J.4    Kaer, L.V.5    Monaco, J.J.6    Colbert, R.A.7
  • 8
    • 0026498493 scopus 로고
    • Purification of an 11 S regulator of the multicatalytic protease
    • W. Dubiel, G. Pratt, K. Ferrell and M. Rechsteiner, Purification of an 11 S regulator of the multicatalytic protease. J. Biol. Chem. 267, 22369-22377 (1992).
    • (1992) J. Biol. Chem , vol.267 , pp. 22369-22377
    • Dubiel, W.1    Pratt, G.2    Ferrell, K.3    Rechsteiner, M.4
  • 9
    • 0027214605 scopus 로고
    • Gamma-interferon and expression of MHC genes regulate peptide hydrolysis by proteasomes
    • M. Gaczynska, K. L. Rock and A. L. Goldberg, Gamma-interferon and expression of MHC genes regulate peptide hydrolysis by proteasomes. Nature 365, 264-267 (1993).
    • (1993) Nature , vol.365 , pp. 264-267
    • Gaczynska, M.1    Rock, K.L.2    Goldberg, A.L.3
  • 10
    • 0029186274 scopus 로고
    • Roles of proteasomes in cell growth
    • A. Ichihara and K. Tanaka, Roles of proteasomes in cell growth. Mol. Biol. Rep. 21, 49-52 (1995).
    • (1995) Mol. Biol. Rep , vol.21 , pp. 49-52
    • Ichihara, A.1    Tanaka, K.2
  • 11
    • 0041496232 scopus 로고    scopus 로고
    • Regulation of repair by the 26S proteasome
    • K. Sweder and K. Madura, Regulation of repair by the 26S proteasome. J. Biomed. Biotechnol. 2, 94-105 (2002).
    • (2002) J. Biomed. Biotechnol , vol.2 , pp. 94-105
    • Sweder, K.1    Madura, K.2
  • 12
    • 0036646488 scopus 로고    scopus 로고
    • PA200, a nuclear proteasome activator involved in DNA repair
    • V. Ustrell, L. Hoffman, G. Pratt and M. Rechsteiner, PA200, a nuclear proteasome activator involved in DNA repair. EMBO J. 21, 3516-3525 (2002).
    • (2002) EMBO J , vol.21 , pp. 3516-3525
    • Ustrell, V.1    Hoffman, L.2    Pratt, G.3    Rechsteiner, M.4
  • 14
    • 0035253721 scopus 로고    scopus 로고
    • A role for calnexin in the assembly of the MHC class I loading complex in the endoplasmic reticulum
    • G. Diedrich, N. Bangia, M. Pan and P. Cresswell, A role for calnexin in the assembly of the MHC class I loading complex in the endoplasmic reticulum. J. Immunol. 166, 1703-1709 (2001).
    • (2001) J. Immunol , vol.166 , pp. 1703-1709
    • Diedrich, G.1    Bangia, N.2    Pan, M.3    Cresswell, P.4
  • 15
    • 12444276104 scopus 로고
    • Prediction of the coding sequences of unidentified human genes. II. The coding sequences of 40 new genes (KIAA0041-KIAA0080) deduced by analysis of cDNA clones from human cell line KG-1
    • N. Nomura, T. Nagase, N. Miyajima, T. Sazuka, A. Tanaka, S. Sato, N. Seki, Y. Kawarabayasi, K. Ishikawa and S. Tabata, Prediction of the coding sequences of unidentified human genes. II. The coding sequences of 40 new genes (KIAA0041-KIAA0080) deduced by analysis of cDNA clones from human cell line KG-1. DNA Res. 1, 223-229 (1994).
    • (1994) DNA Res , vol.1 , pp. 223-229
    • Nomura, N.1    Nagase, T.2    Miyajima, N.3    Sazuka, T.4    Tanaka, A.5    Sato, S.6    Seki, N.7    Kawarabayasi, Y.8    Ishikawa, K.9    Tabata, S.10
  • 16
    • 0021167161 scopus 로고
    • Homozygous deletions that simultaneously eliminate expressions of class I and class II antigens of EBV-transformed B-lymphoblastoid cells. I. Reduced proliferative responses of autologous and allogeneic T cells to mutant cells that have decreased expression of class II antigens
    • R. DeMars, C. C. Chang, S. Shaw, P. J. Reitnauer and P. M. Sondel, Homozygous deletions that simultaneously eliminate expressions of class I and class II antigens of EBV-transformed B-lymphoblastoid cells. I. Reduced proliferative responses of autologous and allogeneic T cells to mutant cells that have decreased expression of class II antigens. Hum. Immunol. 11, 77-97 (1984).
    • (1984) Hum. Immunol , vol.11 , pp. 77-97
    • DeMars, R.1    Chang, C.C.2    Shaw, S.3    Reitnauer, P.J.4    Sondel, P.M.5
  • 17
    • 0026070217 scopus 로고
    • Second proteasome-related gene in the human MHC class II region
    • A. Kelly, S. H. Powis, R. Glynne, E. Radley, S. Beck and J. Trowsdale, Second proteasome-related gene in the human MHC class II region. Nature 353, 667-668 (1991).
    • (1991) Nature , vol.353 , pp. 667-668
    • Kelly, A.1    Powis, S.H.2    Glynne, R.3    Radley, E.4    Beck, S.5    Trowsdale, J.6
  • 18
    • 0025771623 scopus 로고
    • A proteasome-related gene between the two ABC transporter loci in the class II region of the human MHC
    • R. Glynne, S. H. Powis, S. Beck, A. Kelly, L. A. Kerr and J. Trowsdale, A proteasome-related gene between the two ABC transporter loci in the class II region of the human MHC. Nature 353, 357-360 (1991).
    • (1991) Nature , vol.353 , pp. 357-360
    • Glynne, R.1    Powis, S.H.2    Beck, S.3    Kelly, A.4    Kerr, L.A.5    Trowsdale, J.6
  • 19
    • 0030217926 scopus 로고    scopus 로고
    • Roles for calreticulin and a novel glycoprotein, tapasin, in the interaction of MHC class I molecules with TAP
    • B. Sadasivan, P. J. Lehner, B. Ortmann, T. Spies and P. Cresswell, Roles for calreticulin and a novel glycoprotein, tapasin, in the interaction of MHC class I molecules with TAP. Immunity 5, 103-114 (1996).
    • (1996) Immunity , vol.5 , pp. 103-114
    • Sadasivan, B.1    Lehner, P.J.2    Ortmann, B.3    Spies, T.4    Cresswell, P.5
  • 20
    • 0025845432 scopus 로고
    • Restored expression of major histocompatibility class I molecules by gene transfer of a putative peptide transporter
    • T. Spies and R. DeMars, Restored expression of major histocompatibility class I molecules by gene transfer of a putative peptide transporter. Nature 351, 323-324 (1991).
    • (1991) Nature , vol.351 , pp. 323-324
    • Spies, T.1    DeMars, R.2
  • 21
    • 0026498673 scopus 로고
    • Monoclonal antibodies to the human multicatalytic proteinase (proteasome)
    • M. B. Kaltoft, C. Koch, W. Uerkvitz and K. B. Hendil, Monoclonal antibodies to the human multicatalytic proteinase (proteasome). Hybridoma 11, 507-517 (1992).
    • (1992) Hybridoma , vol.11 , pp. 507-517
    • Kaltoft, M.B.1    Koch, C.2    Uerkvitz, W.3    Hendil, K.B.4
  • 22
    • 0036166431 scopus 로고    scopus 로고
    • Disulfide bond isomerization and the assembly of MHC class I-peptide complexes
    • T. P. Dick, N. Bangia, D. R. Peaper and P. Cresswell, Disulfide bond isomerization and the assembly of MHC class I-peptide complexes. Immunity 16, 87-98 (2002).
    • (2002) Immunity , vol.16 , pp. 87-98
    • Dick, T.P.1    Bangia, N.2    Peaper, D.R.3    Cresswell, P.4
  • 23
    • 0033060098 scopus 로고    scopus 로고
    • The N-terminal region of tapasin is required to stabilize the MHC class I loading complex
    • N. Bangia, P. J. Lehner, E. A. Hughes, M. Surman and P. Cresswell, The N-terminal region of tapasin is required to stabilize the MHC class I loading complex. Eur. J. Immunol. 29, 1858-1870 (1999).
    • (1999) Eur. J. Immunol , vol.29 , pp. 1858-1870
    • Bangia, N.1    Lehner, P.J.2    Hughes, E.A.3    Surman, M.4    Cresswell, P.5
  • 24
    • 0025270026 scopus 로고
    • Core filaments of the nuclear matrix
    • D. C. He, J. A. Nickerson and S. Penman, Core filaments of the nuclear matrix. J. Cell Biol. 110, 569-580 (1990).
    • (1990) J. Cell Biol , vol.110 , pp. 569-580
    • He, D.C.1    Nickerson, J.A.2    Penman, S.3
  • 25
    • 0030956629 scopus 로고    scopus 로고
    • The nuclear matrix revealed by eluting chromatin from a cross-linked nucleus
    • J. A. Nickerson, G. Krockmalnic, K. M. Wan and S. Penman, The nuclear matrix revealed by eluting chromatin from a cross-linked nucleus. Proc. Natl. Acad. Sci. USA 94, 4446-4450 (1997).
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 4446-4450
    • Nickerson, J.A.1    Krockmalnic, G.2    Wan, K.M.3    Penman, S.4
  • 26
    • 21644488542 scopus 로고    scopus 로고
    • Hairless contains a novel nuclear matrix targeting signal and associates with histone deacetylase 3 in nuclear speckles
    • K. Djabali and A. M. Christiano, Hairless contains a novel nuclear matrix targeting signal and associates with histone deacetylase 3 in nuclear speckles. Differentiation 72, 410-418 (2004).
    • (2004) Differentiation , vol.72 , pp. 410-418
    • Djabali, K.1    Christiano, A.M.2
  • 27
    • 0027980319 scopus 로고
    • Inhibitors of the proteasome block the degradation of most cell proteins and the generation of peptides presented on MHC class I molecules
    • K. L. Rock, C. Gramm, L. Rothstein, K. Clark, R. Stein, L. Dick, D. Hwang and A. L. Goldberg, Inhibitors of the proteasome block the degradation of most cell proteins and the generation of peptides presented on MHC class I molecules. Cell 78, 761-771 (1994).
    • (1994) Cell , vol.78 , pp. 761-771
    • Rock, K.L.1    Gramm, C.2    Rothstein, L.3    Clark, K.4    Stein, R.5    Dick, L.6    Hwang, D.7    Goldberg, A.L.8
  • 29
    • 0027223877 scopus 로고
    • MHC-linked LMP gene products specifically alter peptidase activities of the proteasome
    • J. Driscoll, M. G. Brown, D. Finley and J. J. Monaco, MHC-linked LMP gene products specifically alter peptidase activities of the proteasome. Nature 365, 262-264 (1993).
    • (1993) Nature , vol.365 , pp. 262-264
    • Driscoll, J.1    Brown, M.G.2    Finley, D.3    Monaco, J.J.4
  • 30
    • 1942489340 scopus 로고    scopus 로고
    • New HEAT-like repeat motifs in proteins regulating proteasome structure and function
    • A. V. Kajava, C. Gorbea, J. Ortega, M. Rechsteiner and A. C. Steven, New HEAT-like repeat motifs in proteins regulating proteasome structure and function. J. Struct. Biol. 146, 425-430 (2004).
    • (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
  • 31
    • 0037462453 scopus 로고    scopus 로고
    • The ATRs, ATMs, and TORs are giant HEAT repeat proteins
    • J. Perry and N. Kleckner, The ATRs, ATMs, and TORs are giant HEAT repeat proteins. Cell 112, 151-155 (2003).
    • (2003) Cell , vol.112 , pp. 151-155
    • Perry, J.1    Kleckner, N.2
  • 32
    • 0031470630 scopus 로고    scopus 로고
    • Evolutionary specialization of the nuclear targeting apparatus
    • H. S. Malik, T. H. Eickbush and D. S. Goldfarb, Evolutionary specialization of the nuclear targeting apparatus. Proc. Natl. Acad. Sci. USA 94, 13738-13742 (1997).
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 13738-13742
    • Malik, H.S.1    Eickbush, T.H.2    Goldfarb, D.S.3
  • 34
    • 0031800886 scopus 로고    scopus 로고
    • Cell-cycle-dependent nuclear translocation of HSP70 in amphibian embryonic cells
    • N. Moreau, C. Prudhomme and N. Angelier, Cell-cycle-dependent nuclear translocation of HSP70 in amphibian embryonic cells. Int. J. Dev. Biol. 42, 633-636 (1998).
    • (1998) Int. J. Dev. Biol , vol.42 , pp. 633-636
    • Moreau, N.1    Prudhomme, C.2    Angelier, N.3
  • 35
    • 0021398211 scopus 로고
    • hsp70: Nuclear concentration during environmental stress and cytoplasmic storage during recovery
    • J. M. Velazquez and S. Lindquist, hsp70: nuclear concentration during environmental stress and cytoplasmic storage during recovery. Cell 36, 655-662 (1984).
    • (1984) Cell , vol.36 , pp. 655-662
    • Velazquez, J.M.1    Lindquist, S.2
  • 36
    • 0025878391 scopus 로고
    • Further characterizations of bleomycin-sensitive (blm) mutants of Saccharomyces cerevisiae with implications for a radio-mimetic model
    • C. W. Moore, Further characterizations of bleomycin-sensitive (blm) mutants of Saccharomyces cerevisiae with implications for a radio-mimetic model. J. Bacteriol. 173, 3605-3608 (1991).
    • (1991) J. Bacteriol , vol.173 , pp. 3605-3608
    • Moore, C.W.1
  • 38
    • 0035093737 scopus 로고    scopus 로고
    • Signaling, repair and the cancer connection
    • DNA double-strand breaks
    • K. K. Khanna and S. P. Jackson, DNA double-strand breaks: Signaling, repair and the cancer connection. Nat Genet. 27, 247-254 (2001).
    • (2001) Nat Genet , vol.27 , pp. 247-254
    • Khanna, K.K.1    Jackson, S.P.2
  • 39
    • 0242522904 scopus 로고    scopus 로고
    • Blm3 is part of nascent proteasomes and is involved in a late stage of nuclear proteasome assembly
    • 959-963
    • M. Fehlker, P. Wendler, A. Lehmann and C. Enenkel, Blm3 is part of nascent proteasomes and is involved in a late stage of nuclear proteasome assembly. EMBO Rep. 4, 959-963 (2003).
    • (2003) EMBO Rep , vol.4
    • Fehlker, M.1    Wendler, P.2    Lehmann, A.3    Enenkel, C.4
  • 40
  • 41
    • 22744449724 scopus 로고    scopus 로고
    • Interaction and colocalization of Rad9/Rad1/Hus1 checkpoint complex with replication protein A in human cells
    • X. Wu, S. M. Shell and Y. Zou, Interaction and colocalization of Rad9/Rad1/Hus1 checkpoint complex with replication protein A in human cells. Oncogene 24, 4728-4735 (2005).
    • (2005) Oncogene , vol.24 , pp. 4728-4735
    • Wu, X.1    Shell, S.M.2    Zou, Y.3
  • 45
    • 0035337151 scopus 로고    scopus 로고
    • Ionizing radiation affects 26s proteasome function and associated molecular responses, even at low doses
    • F. Pajonk and W. H. McBride, Ionizing radiation affects 26s proteasome function and associated molecular responses, even at low doses. Radiother. Oncol. 59, 203-212 (2001).
    • (2001) Radiother. Oncol , vol.59 , pp. 203-212
    • Pajonk, F.1    McBride, W.H.2
  • 46
    • 22944480581 scopus 로고    scopus 로고
    • Proteasome structures affected by ionizing radiation
    • M. Pervan, K. S. Iwamoto and W. H. McBride, Proteasome structures affected by ionizing radiation. Mol. Cancer Res. 3, 381-390 (2005).
    • (2005) Mol. Cancer Res , vol.3 , pp. 381-390
    • Pervan, M.1    Iwamoto, K.S.2    McBride, W.H.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.