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Volumn 400, Issue 3, 2010, Pages 389-395

Regulation of the Polycomb protein RING1B ubiquitination by USP7

Author keywords

Deubiquitinating enzymes; Polycomb; RING1B; Ubiquitin; USP7

Indexed keywords

POLYCOMB GROUP PROTEIN; PROTEIN RING1B; PROTEIN USP7; UBIQUITIN; UNCLASSIFIED DRUG; BMI1 PROTEIN; DNA BINDING PROTEIN; RNF2 PROTEIN, HUMAN; UBIQUITIN PROTEIN LIGASE; UBIQUITIN THIOLESTERASE; USP7 PROTEIN, HUMAN;

EID: 77956899405     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2010.08.082     Document Type: Article
Times cited : (60)

References (24)
  • 1
    • 40849106789 scopus 로고    scopus 로고
    • Histone ubiquitination: triggering gene activity
    • Weake V.M., Workman J.L. Histone ubiquitination: triggering gene activity. Mol. Cell 2008, 29:653-663.
    • (2008) Mol. Cell , vol.29 , pp. 653-663
    • Weake, V.M.1    Workman, J.L.2
  • 2
    • 70349469565 scopus 로고    scopus 로고
    • Mechanisms of polycomb gene silencing: knowns and unknowns
    • Simon J.A., Kingston R.E. Mechanisms of polycomb gene silencing: knowns and unknowns. Nat. Rev. Mol. Cell. Biol. 2009, 10:697-708.
    • (2009) Nat. Rev. Mol. Cell. Biol. , vol.10 , pp. 697-708
    • Simon, J.A.1    Kingston, R.E.2
  • 3
    • 1942503942 scopus 로고    scopus 로고
    • The functions of E(Z)/EZH2-mediated methylation of lysine 27 in histone H3
    • Cao R., Zhang Y. The functions of E(Z)/EZH2-mediated methylation of lysine 27 in histone H3. Curr. Opin. Genet. Dev. 2004, 14:155-164.
    • (2004) Curr. Opin. Genet. Dev. , vol.14 , pp. 155-164
    • Cao, R.1    Zhang, Y.2
  • 6
    • 33750379420 scopus 로고    scopus 로고
    • Polycomb silencers control cell fate, development and cancer
    • Sparmann A., van Lohuizen M. Polycomb silencers control cell fate, development and cancer. Nat. Rev. Cancer 2006, 6:846-856.
    • (2006) Nat. Rev. Cancer , vol.6 , pp. 846-856
    • Sparmann, A.1    van Lohuizen, M.2
  • 7
    • 29144487990 scopus 로고    scopus 로고
    • Role of Bmi-1 and Ring1A in H2A ubiquitylation and Hox gene silencing
    • Cao R., Tsukada Y., Zhang Y. Role of Bmi-1 and Ring1A in H2A ubiquitylation and Hox gene silencing. Mol. Cell 2005, 20:845-854.
    • (2005) Mol. Cell , vol.20 , pp. 845-854
    • Cao, R.1    Tsukada, Y.2    Zhang, Y.3
  • 8
    • 33751515474 scopus 로고    scopus 로고
    • The polycomb protein Ring1B generates self atypical mixed ubiquitin chains required for its in vitro histone H2A ligase activity
    • Ben-Saadon R., Zaaroor D., Ziv T., Ciechanover A. The polycomb protein Ring1B generates self atypical mixed ubiquitin chains required for its in vitro histone H2A ligase activity. Mol. Cell 2006, 24:701-711.
    • (2006) Mol. Cell , vol.24 , pp. 701-711
    • Ben-Saadon, R.1    Zaaroor, D.2    Ziv, T.3    Ciechanover, A.4
  • 11
    • 77449155637 scopus 로고    scopus 로고
    • The multiple levels of regulation by p53 ubiquitination
    • Lee J.T., Gu W. The multiple levels of regulation by p53 ubiquitination. Cell Death Differ. 2010, 17:86-92.
    • (2010) Cell Death Differ. , vol.17 , pp. 86-92
    • Lee, J.T.1    Gu, W.2
  • 12
    • 4644352805 scopus 로고    scopus 로고
    • A RING finger ubiquitin ligase is protected from autocatalyzed ubiquitination and degradation by binding to ubiquitin-specific protease USP7
    • Canning M., Boutell C., Parkinson J., Everett R.D. A RING finger ubiquitin ligase is protected from autocatalyzed ubiquitination and degradation by binding to ubiquitin-specific protease USP7. J. Biol. Chem. 2004, 279:38160-38168.
    • (2004) J. Biol. Chem. , vol.279 , pp. 38160-38168
    • Canning, M.1    Boutell, C.2    Parkinson, J.3    Everett, R.D.4
  • 13
    • 46349110469 scopus 로고    scopus 로고
    • The ubiquitin E3 ligase MARCH7 is differentially regulated by the deubiquitylating enzymes USP7 and USP9X
    • Nathan J.A., Sengupta S., Wood S.A., Admon A., Markson G., Sanderson C., Lehner P.J. The ubiquitin E3 ligase MARCH7 is differentially regulated by the deubiquitylating enzymes USP7 and USP9X. Traffic 2008, 9:1130-1145.
    • (2008) Traffic , vol.9 , pp. 1130-1145
    • Nathan, J.A.1    Sengupta, S.2    Wood, S.A.3    Admon, A.4    Markson, G.5    Sanderson, C.6    Lehner, P.J.7
  • 15
    • 77955419051 scopus 로고    scopus 로고
    • Ubiquitin-specific proteases 7 and 11 modulate Polycomb regulation of the INK4a tumour suppressor
    • Maertens G.N., El Messaoudi-Aubert S., Elderkin S., Hiom K., Peters G. Ubiquitin-specific proteases 7 and 11 modulate Polycomb regulation of the INK4a tumour suppressor. EMBO J. 2010.
    • (2010) EMBO J.
    • Maertens, G.N.1    El Messaoudi-Aubert, S.2    Elderkin, S.3    Hiom, K.4    Peters, G.5
  • 16
    • 0042317328 scopus 로고    scopus 로고
    • The BRCA1/BARD1 heterodimer assembles polyubiquitin chains through an unconventional linkage involving lysine residue K6 of ubiquitin
    • Wu-Baer F., Lagrazon K., Yuan W., Baer R. The BRCA1/BARD1 heterodimer assembles polyubiquitin chains through an unconventional linkage involving lysine residue K6 of ubiquitin. J. Biol. Chem. 2003, 278:34743-34746.
    • (2003) J. Biol. Chem. , vol.278 , pp. 34743-34746
    • Wu-Baer, F.1    Lagrazon, K.2    Yuan, W.3    Baer, R.4
  • 17
    • 0037184113 scopus 로고    scopus 로고
    • Proteasome-mediated degradation of Smac during apoptosis: XIAP promotes Smac ubiquitination in vitro
    • MacFarlane M., Merrison W., Bratton S.B., Cohen G.M. Proteasome-mediated degradation of Smac during apoptosis: XIAP promotes Smac ubiquitination in vitro. J. Biol. Chem. 2002, 277:36611-36616.
    • (2002) J. Biol. Chem. , vol.277 , pp. 36611-36616
    • MacFarlane, M.1    Merrison, W.2    Bratton, S.B.3    Cohen, G.M.4
  • 20
    • 47349129727 scopus 로고    scopus 로고
    • RAWUL: a new ubiquitin-like domain in PRC1 ring finger proteins that unveils putative plant and worm PRC1 orthologs
    • Sanchez-Pulido L., Devos D., Sung Z.R., Calonje M. RAWUL: a new ubiquitin-like domain in PRC1 ring finger proteins that unveils putative plant and worm PRC1 orthologs. BMC Genomics 2008, 9:308.
    • (2008) BMC Genomics , vol.9 , pp. 308
    • Sanchez-Pulido, L.1    Devos, D.2    Sung, Z.R.3    Calonje, M.4
  • 24
    • 34247625135 scopus 로고    scopus 로고
    • Pharmacologic disruption of Polycomb-repressive complex 2-mediated gene repression selectively induces apoptosis in cancer cells
    • Tan J., Yang X., Zhuang L., Jiang X., Chen W., Lee P.L., Karuturi R.K., Tan P.B., Liu E.T., Yu Q. Pharmacologic disruption of Polycomb-repressive complex 2-mediated gene repression selectively induces apoptosis in cancer cells. Genes Dev. 2007, 21:1050-1063.
    • (2007) Genes Dev. , vol.21 , pp. 1050-1063
    • Tan, J.1    Yang, X.2    Zhuang, L.3    Jiang, X.4    Chen, W.5    Lee, P.L.6    Karuturi, R.K.7    Tan, P.B.8    Liu, E.T.9    Yu, Q.10


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.