메뉴 건너뛰기




Volumn 31, Issue 19, 2011, Pages 3997-4006

Pirh2 E3 ubiquitin ligase monoubiquitinates DNA polymerase eta to suppress translesion DNA synthesis

Author keywords

[No Author keywords available]

Indexed keywords

DNA DIRECTED DNA POLYMERASE ETA; LYSINE; UBIQUITIN PROTEIN LIGASE E3;

EID: 80053579178     PISSN: 02707306     EISSN: 10985549     Source Type: Journal    
DOI: 10.1128/MCB.05808-11     Document Type: Article
Times cited : (47)

References (30)
  • 1
    • 29144499065 scopus 로고    scopus 로고
    • Ubiquitin-binding domains in Y-family polymerases regulate translesion synthesis
    • Bienko, M., et al. 2005. Ubiquitin-binding domains in Y-family polymerases regulate translesion synthesis. Science 310:1821-1824.
    • (2005) Science , vol.310 , pp. 1821-1824
    • Bienko, M.1
  • 2
    • 75949122886 scopus 로고    scopus 로고
    • Regulation of translesion synthesis DNA polymerase eta by monoubiquitination
    • Bienko, M., et al. 2010. Regulation of translesion synthesis DNA polymerase eta by monoubiquitination. Mol. Cell 37:396-407.
    • (2010) Mol. Cell , vol.37 , pp. 396-407
    • Bienko, M.1
  • 3
    • 34447523329 scopus 로고    scopus 로고
    • Regulation of Pax3 by proteasomal degradation of monoubiquitinated protein in skeletal muscle progenitors
    • Boutet, S. C., M. H. Disatnik, L. S. Chan, K. Iori, and T. A. Rando. 2007. Regulation of Pax3 by proteasomal degradation of monoubiquitinated protein in skeletal muscle progenitors. Cell 130:349-362.
    • (2007) Cell , vol.130 , pp. 349-362
    • Boutet, S.C.1    Disatnik, M.H.2    Chan, L.S.3    Iori, K.4    Rando, T.A.5
  • 4
    • 66349089861 scopus 로고    scopus 로고
    • Masking of a nuclear signal motif by monoubiquitination leads to mislocalization and degradation of the regulatory enzyme cytidylyltransferase
    • Chen, B. B., and R. K. Mallampalli. 2009. Masking of a nuclear signal motif by monoubiquitination leads to mislocalization and degradation of the regulatory enzyme cytidylyltransferase. Mol. Cell. Biol. 29:3062-3075.
    • (2009) Mol. Cell. Biol. , vol.29 , pp. 3062-3075
    • Chen, B.B.1    Mallampalli, R.K.2
  • 5
    • 55949125726 scopus 로고    scopus 로고
    • Human DNA polymerase eta activity and translocation is regulated by phosphorylation
    • Chen, Y. W., et al. 2008. Human DNA polymerase eta activity and translocation is regulated by phosphorylation. Proc. Natl. Acad. Sci. U. S. A. 105:16578-16583.
    • (2008) Proc. Natl. Acad. Sci. U. S. A. , vol.105 , pp. 16578-16583
    • Chen, Y.W.1
  • 6
    • 70350065725 scopus 로고    scopus 로고
    • Disorders of nucleotide excision repair: the genetic and molecular basis of heterogeneity
    • Cleaver, J. E., E. T. Lam, and I. Revet. 2009. Disorders of nucleotide excision repair: the genetic and molecular basis of heterogeneity. Nat. Rev. Genet. 10:756-768.
    • (2009) Nat. Rev. Genet. , vol.10 , pp. 756-768
    • Cleaver, J.E.1    Lam, E.T.2    Revet, I.3
  • 7
    • 9744227111 scopus 로고    scopus 로고
    • Expression of Pirh2, a newly identified ubiquitin protein ligase, in lung cancer
    • Duan, W., et al. 2004. Expression of Pirh2, a newly identified ubiquitin protein ligase, in lung cancer. J. Natl. Cancer Inst. 96:1718-1721.
    • (2004) J. Natl. Cancer Inst. , vol.96 , pp. 1718-1721
    • Duan, W.1
  • 8
    • 0037205001 scopus 로고    scopus 로고
    • Specialized DNA polymerases, cellular survival, and the genesis of mutations
    • Friedberg, E. C., R. Wagner, and M. Radman. 2002. Specialized DNA polymerases, cellular survival, and the genesis of mutations. Science 296: 1627-1630.
    • (2002) Science , vol.296 , pp. 1627-1630
    • Friedberg, E.C.1    Wagner, R.2    Radman, M.3
  • 10
    • 0037068455 scopus 로고    scopus 로고
    • RAD6-dependent DNA repair is linked to modification of PCNA by ubiquitin and SUMO
    • Hoege, C., B. Pfander, G. L. Moldovan, G. Pyrowolakis, and S. Jentsch. 2002. RAD6-dependent DNA repair is linked to modification of PCNA by ubiquitin and SUMO. Nature 419:135-141.
    • (2002) Nature , vol.419 , pp. 135-141
    • Hoege, C.1    Pfander, B.2    Moldovan, G.L.3    Pyrowolakis, G.4    Jentsch, S.5
  • 11
    • 0035902108 scopus 로고    scopus 로고
    • Genome maintenance mechanisms for preventing cancer
    • Hoeijmakers, J. H. 2001. Genome maintenance mechanisms for preventing cancer. Nature 411:366-374.
    • (2001) Nature , vol.411 , pp. 366-374
    • Hoeijmakers, J.H.1
  • 12
    • 77953113655 scopus 로고    scopus 로고
    • Monoubiquitination of RPN10 regulates substrate recruitment to the proteasome
    • Isasa, M., et al. 2010. Monoubiquitination of RPN10 regulates substrate recruitment to the proteasome. Mol. Cell 38:733-745.
    • (2010) Mol. Cell , vol.38 , pp. 733-745
    • Isasa, M.1
  • 13
    • 0029119522 scopus 로고
    • A proteolytic pathway that recognizes ubiquitin as a degradation signal
    • Johnson, E. S., P. C. Ma, I. M. Ota, and A. Varshavsky. 1995. A proteolytic pathway that recognizes ubiquitin as a degradation signal. J. Biol. Chem. 270:17442-17456.
    • (1995) J. Biol. Chem. , vol.270 , pp. 17442-17456
    • Johnson, E.S.1    Ma, P.C.2    Ota, I.M.3    Varshavsky, A.4
  • 14
    • 0033538470 scopus 로고    scopus 로고
    • hRAD30 mutations in the variant form of xeroderma pigmentosum
    • Johnson, R. E., C. M. Kondratick, S. Prakash, and L. Prakash. 1999. hRAD30 mutations in the variant form of xeroderma pigmentosum. Science 285:263-265.
    • (1999) Science , vol.285 , pp. 263-265
    • Johnson, R.E.1    Kondratick, C.M.2    Prakash, S.3    Prakash, L.4
  • 15
    • 38149045848 scopus 로고    scopus 로고
    • Physical interactions and functional coupling between Daxx and sodium hydrogen exchanger 1 in ischemic cell death
    • Jung, Y. S., et al. 2008. Physical interactions and functional coupling between Daxx and sodium hydrogen exchanger 1 in ischemic cell death. J. Biol. Chem. 283:1018-1025.
    • (2008) J. Biol. Chem. , vol.283 , pp. 1018-1025
    • Jung, Y.S.1
  • 16
    • 75749108557 scopus 로고    scopus 로고
    • Pirh2 E3 ubiquitin ligase targets DNA polymerase eta for 20S proteasomal degradation
    • Jung, Y. S., G. Liu, and X. Chen. 2010. Pirh2 E3 ubiquitin ligase targets DNA polymerase eta for 20S proteasomal degradation. Mol. Cell. Biol. 30:1041-1048.
    • (2010) Mol. Cell. Biol. , vol.30 , pp. 1041-1048
    • Jung, Y.S.1    Liu, G.2    Chen, X.3
  • 17
    • 2442417331 scopus 로고    scopus 로고
    • Interaction of human DNA polymerase eta with monoubiquitinated PCNA: a possible mechanism for the polymerase switch in response to DNA damage
    • Kannouche, P. L., J. Wing, and A. R. Lehmann. 2004. Interaction of human DNA polymerase eta with monoubiquitinated PCNA: a possible mechanism for the polymerase switch in response to DNA damage. Mol. Cell 14:491-500.
    • (2004) Mol. Cell , vol.14 , pp. 491-500
    • Kannouche, P.L.1    Wing, J.2    Lehmann, A.R.3
  • 18
    • 33745742269 scopus 로고    scopus 로고
    • Quantitative analysis of in vitro ubiquitinated cyclin B1 reveals complex chain topology
    • Kirkpatrick, D. S., et al. 2006. Quantitative analysis of in vitro ubiquitinated cyclin B1 reveals complex chain topology. Nat. Cell Biol. 8:700-710.
    • (2006) Nat. Cell Biol. , vol.8 , pp. 700-710
    • Kirkpatrick, D.S.1
  • 19
    • 0042674380 scopus 로고    scopus 로고
    • Recapitulation of the cellular xeroderma pigmentosum-variant phenotypes using short interfering RNA for DNA polymerase H
    • Laposa, R. R., L. Feeney, and J. E. Cleaver. 2003. Recapitulation of the cellular xeroderma pigmentosum-variant phenotypes using short interfering RNA for DNA polymerase H. Cancer Res. 63:3909-3912.
    • (2003) Cancer Res , vol.63 , pp. 3909-3912
    • Laposa, R.R.1    Feeney, L.2    Cleaver, J.E.3
  • 20
    • 0037459377 scopus 로고    scopus 로고
    • Pirh2, a p53-induced ubiquitin-protein ligase, promotes p53 degradation
    • Leng, R. P., et al. 2003. Pirh2, a p53-induced ubiquitin-protein ligase, promotes p53 degradation. Cell 112:779-791.
    • (2003) Cell , vol.112 , pp. 779-791
    • Leng, R.P.1
  • 21
    • 32044449228 scopus 로고    scopus 로고
    • DNA polymerase eta, the product of the xeroderma pigmentosum variant gene and a target of p53, modulates the DNA damage checkpoint and p53 activation
    • Liu, G., and X. Chen. 2006. DNA polymerase eta, the product of the xeroderma pigmentosum variant gene and a target of p53, modulates the DNA damage checkpoint and p53 activation. Mol. Cell. Biol. 26:1398-1413.
    • (2006) Mol. Cell. Biol. , vol.26 , pp. 1398-1413
    • Liu, G.1    Chen, X.2
  • 22
    • 33747780741 scopus 로고    scopus 로고
    • Human PIRH2 enhances androgen receptor signaling through inhibition of histone deacetylase 1 and is overexpressed in prostate cancer
    • Logan, I. R., et al. 2006. Human PIRH2 enhances androgen receptor signaling through inhibition of histone deacetylase 1 and is overexpressed in prostate cancer. Mol. Cell. Biol. 26:6502-6510.
    • (2006) Mol. Cell. Biol. , vol.26 , pp. 6502-6510
    • Logan, I.R.1
  • 23
    • 1642523726 scopus 로고    scopus 로고
    • Control of human PIRH2 protein stability: involvement of TIP60 and the proteosome
    • Logan, I. R., V. Sapountzi, L. Gaughan, D. E. Neal, and C. N. Robson. 2004. Control of human PIRH2 protein stability: involvement of TIP60 and the proteosome. J. Biol. Chem. 279:11696-11704.
    • (2004) J. Biol. Chem. , vol.279 , pp. 11696-11704
    • Logan, I.R.1    Sapountzi, V.2    Gaughan, L.3    Neal, D.E.4    Robson, C.N.5
  • 24
    • 0033578040 scopus 로고    scopus 로고
    • The XPV (xeroderma pigmentosum variant) gene encodes human DNA polymerase eta
    • Masutani, C., et al. 1999. The XPV (xeroderma pigmentosum variant) gene encodes human DNA polymerase eta. Nature 399:700-704.
    • (1999) Nature , vol.399 , pp. 700-704
    • Masutani, C.1
  • 25
    • 33646036373 scopus 로고    scopus 로고
    • Crystal structure of the ubiquitin binding domains of rabex-5 reveals two modes of interaction with ubiquitin
    • Penengo, L., et al. 2006. Crystal structure of the ubiquitin binding domains of rabex-5 reveals two modes of interaction with ubiquitin. Cell 124:1183-1195.
    • (2006) Cell , vol.124 , pp. 1183-1195
    • Penengo, L.1
  • 26
    • 33745581677 scopus 로고    scopus 로고
    • Controlling the subcellular localization of DNA polymerases iota and eta via interactions with ubiquitin
    • Plosky, B. S., et al. 2006. Controlling the subcellular localization of DNA polymerases iota and eta via interactions with ubiquitin. EMBO J. 25:2847-2855.
    • (2006) EMBO J , vol.25 , pp. 2847-2855
    • Plosky, B.S.1
  • 27
    • 21244506437 scopus 로고    scopus 로고
    • Eukaryotic translesion synthesis DNA polymerases: specificity of structure and function
    • Prakash, S., R. E. Johnson, and L. Prakash. 2005. Eukaryotic translesion synthesis DNA polymerases: specificity of structure and function. Annu. Rev. Biochem. 74:317-353.
    • (2005) Annu. Rev. Biochem. , vol.74 , pp. 317-353
    • Prakash, S.1    Johnson, R.E.2    Prakash, L.3
  • 28
    • 57149120085 scopus 로고    scopus 로고
    • Molecular basis of Pirh2-mediated p53 ubiquitylation
    • Sheng, Y., et al. 2008. Molecular basis of Pirh2-mediated p53 ubiquitylation. Nat. Struct. Mol. Biol. 15:1334-1342.
    • (2008) Nat. Struct. Mol. Biol. , vol.15 , pp. 1334-1342
    • Sheng, Y.1
  • 29
    • 65349157682 scopus 로고    scopus 로고
    • High expression of Pirh2, an E3 ligase for p27, is associated with low expression of p27 and poor prognosis in head and neck cancers
    • Shimada, M., et al. 2009. High expression of Pirh2, an E3 ligase for p27, is associated with low expression of p27 and poor prognosis in head and neck cancers. Cancer Sci. 100:866-872.
    • (2009) Cancer Sci , vol.100 , pp. 866-872
    • Shimada, M.1
  • 30
    • 78651089988 scopus 로고    scopus 로고
    • Interplay between MDM2, MDMX, Pirh2 and COP1: the negative regulators of p53
    • Wang, L., et al. 2011. Interplay between MDM2, MDMX, Pirh2 and COP1: the negative regulators of p53. Mol. Biol. Rep. 38:229-236.
    • (2011) Mol. Biol. Rep. , vol.38 , pp. 229-236
    • Wang, L.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.