메뉴 건너뛰기




Volumn 9, Issue 3, 2007, Pages 331-338

Intrinsic ubiquitination activity of PCAF controls the stability of the oncoprotein Hdm2

Author keywords

[No Author keywords available]

Indexed keywords

HISTONE ACETYLTRANSFERASE PCAF; ONCOPROTEIN; PROTEIN MDM2; PROTEIN P53; UBIQUITIN PROTEIN LIGASE E3;

EID: 33847388041     PISSN: 14657392     EISSN: None     Source Type: Journal    
DOI: 10.1038/ncb1545     Document Type: Article
Times cited : (150)

References (31)
  • 1
    • 0034719683 scopus 로고    scopus 로고
    • The PCAF acetylase complex as a potential tumor suppressor
    • Schiltz, R. L. & Nakatani, Y. The PCAF acetylase complex as a potential tumor suppressor. Biochim. Biophys. Acta 1470, M37-M53 (2000).
    • (2000) Biochim. Biophys. Acta , vol.1470
    • Schiltz, R.L.1    Nakatani, Y.2
  • 2
  • 4
    • 14644437751 scopus 로고    scopus 로고
    • MDM2 is a central node in the p53 pathway: 12 years and counting
    • Bond, G. L., Hu, W. & Levine, A. J. MDM2 is a central node in the p53 pathway: 12 years and counting. Curr. Cancer Drug Targets 5, 3-8 (2005).
    • (2005) Curr. Cancer Drug Targets , vol.5 , pp. 3-8
    • Bond, G.L.1    Hu, W.2    Levine, A.J.3
  • 5
    • 0032906633 scopus 로고    scopus 로고
    • p53 sites acetylated in vitro by PCAF and p300 are acetylated in vivo in response to DNA damage
    • Liu, L. et al. p53 sites acetylated in vitro by PCAF and p300 are acetylated in vivo in response to DNA damage. Mol. Cell. Biol. 19, 1202-1209 (1999).
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 1202-1209
    • Liu, L.1
  • 6
    • 0034708458 scopus 로고    scopus 로고
    • Mdm2 is a RING finger-dependent ubiquitin protein ligase for itself and p53
    • Fang, S., Jensen, J. P., Ludwig, R. L., Vousden, K. H. & Weissman, A. M. Mdm2 is a RING finger-dependent ubiquitin protein ligase for itself and p53. J. Biol. Chem. 275, 8945-8951 (2000).
    • (2000) J. Biol. Chem. , vol.275 , pp. 8945-8951
    • Fang, S.1    Jensen, J.P.2    Ludwig, R.L.3    Vousden, K.H.4    Weissman, A.M.5
  • 9
    • 25444482673 scopus 로고    scopus 로고
    • A new twist in the feedback loop: Stress-activated MDM2 destabilization is required for p53 activation
    • Stommel, J. M. & Wahl, G. M. A new twist in the feedback loop: stress-activated MDM2 destabilization is required for p53 activation. Cell Cycle 4, 411-417 (2005).
    • (2005) Cell Cycle , vol.4 , pp. 411-417
    • Stommel, J.M.1    Wahl, G.M.2
  • 10
    • 0033613222 scopus 로고    scopus 로고
    • RING fingers mediate ubiquitin-conjugating enzyme (E2)-dependent ubiquitination
    • Lorick, K. L. et al. RING fingers mediate ubiquitin-conjugating enzyme (E2)-dependent ubiquitination. Proc. Natl Acad. Sci. USA 96, 11364-11369 (1999).
    • (1999) Proc. Natl Acad. Sci. USA , vol.96 , pp. 11364-11369
    • Lorick, K.L.1
  • 11
    • 17844385784 scopus 로고    scopus 로고
    • Regulatory cross-talk between lysine acetylation and ubiquitination: Role in the control of protein stability
    • Caron, C., Boyault, C. & Khochbin, S. Regulatory cross-talk between lysine acetylation and ubiquitination: Role in the control of protein stability. Bioessays 27, 408-415 (2005).
    • (2005) Bioessays , vol.27 , pp. 408-415
    • Caron, C.1    Boyault, C.2    Khochbin, S.3
  • 12
    • 0037432773 scopus 로고    scopus 로고
    • Polyubiquitination of p53 by a ubiquitin ligase activity of p300
    • Grossman, S. R. et al. Polyubiquitination of p53 by a ubiquitin ligase activity of p300. Science 300, 342-344 (2003).
    • (2003) Science , vol.300 , pp. 342-344
    • Grossman, S.R.1
  • 13
    • 3943054838 scopus 로고    scopus 로고
    • De-ubiquitination and ubiquitin ligase domains of A20 downregulate NF-κB signalling
    • Wertz, I. E. et al. De-ubiquitination and ubiquitin ligase domains of A20 downregulate NF-κB signalling. Nature 430, 694-699 (2004).
    • (2004) Nature , vol.430 , pp. 694-699
    • Wertz, I.E.1
  • 14
    • 9444295347 scopus 로고    scopus 로고
    • Ubiquitin-protein ligases
    • Robinson, P. A. & Ardley, H. C. Ubiquitin-protein ligases. J. Cell Sci. 117, 5191-5194 (2004).
    • (2004) J. Cell Sci. , vol.117 , pp. 5191-5194
    • Robinson, P.A.1    Ardley, H.C.2
  • 15
    • 2342567852 scopus 로고    scopus 로고
    • Accelerated MDM2 auto-degradation induced by DNA-damage kinases is required for p53 activation
    • Stommel, J. M. & Wahl, G. M. Accelerated MDM2 auto-degradation induced by DNA-damage kinases is required for p53 activation. EMBO J. 23, 1547-1556 (2004).
    • (2004) EMBO J. , vol.23 , pp. 1547-1556
    • Stommel, J.M.1    Wahl, G.M.2
  • 16
    • 0033582821 scopus 로고    scopus 로고
    • Inducible degradation of IκBα by the proteasome requires interaction with the F-box protein h-βTrCP
    • Kroll, M. et al. Inducible degradation of IκBα by the proteasome requires interaction with the F-box protein h-βTrCP. J. Biol. Chem. 274, 7941-7945 (1999).
    • (1999) J. Biol. Chem. , vol.274 , pp. 7941-7945
    • Kroll, M.1
  • 17
    • 1542358136 scopus 로고    scopus 로고
    • Inhibition of p53 degradation by Mdm2 acetylation
    • Wang, X., Taplick, J., Geva, N. & Oren, M. Inhibition of p53 degradation by Mdm2 acetylation. FEBS Lett. 561, 195-201 (2004).
    • (2004) FEBS Lett. , vol.561 , pp. 195-201
    • Wang, X.1    Taplick, J.2    Geva, N.3    Oren, M.4
  • 18
  • 19
    • 0037329056 scopus 로고    scopus 로고
    • The p53-Mdm2 module and the ubiquitin system
    • Michael, D. & Oren, M. The p53-Mdm2 module and the ubiquitin system. Semin. Cancer Biol. 13, 49-58 (2003).
    • (2003) Semin. Cancer Biol. , vol.13 , pp. 49-58
    • Michael, D.1    Oren, M.2
  • 20
    • 0033552595 scopus 로고    scopus 로고
    • Regulation of p53 in response to DNA damage
    • Lakin, N. D. & Jackson, S. P. Regulation of p53 in response to DNA damage. Oncogene 18, 7644-7655 (1999).
    • (1999) Oncogene , vol.18 , pp. 7644-7655
    • Lakin, N.D.1    Jackson, S.P.2
  • 21
    • 0035970025 scopus 로고    scopus 로고
    • Complete switch from Mdm2 to human papillomavirus E6-mediated degradation of p53 in cervical cancer cells
    • Hengstermann, A., Linares, L. K., Ciechanover, A., Whitaker, N. J. & Scheffner, M. Complete switch from Mdm2 to human papillomavirus E6-mediated degradation of p53 in cervical cancer cells. Proc. Natl Acad. Sci, USA 98, 1218-1223 (2001).
    • (2001) Proc. Natl Acad. Sci. USA , vol.98 , pp. 1218-1223
    • Hengstermann, A.1    Linares, L.K.2    Ciechanover, A.3    Whitaker, N.J.4    Scheffner, M.5
  • 22
    • 0035694469 scopus 로고    scopus 로고
    • Acetylation of p53 activates transcription through recruitment of coactivators/histone acetyltransferases
    • Barlev, N. A. et al. Acetylation of p53 activates transcription through recruitment of coactivators/histone acetyltransferases. Mol. Cell 8, 1243-1254 (2001).
    • (2001) Mol. Cell , vol.8 , pp. 1243-1254
    • Barlev, N.A.1
  • 23
    • 33745163907 scopus 로고    scopus 로고
    • Regulation of transactivation-independent proapoptotic activity of p53 by FOXO3a
    • You, H., Yamamoto, K. & Mak, T. W. Regulation of transactivation-independent proapoptotic activity of p53 by FOXO3a. Proc. Natl Acad. Sci. USA 103, 9051-9056 (2006).
    • (2006) Proc. Natl Acad. Sci. USA , vol.103 , pp. 9051-9056
    • You, H.1    Yamamoto, K.2    Mak, T.W.3
  • 24
    • 31544457877 scopus 로고    scopus 로고
    • p53 Ubiquitination: Mdm2 and beyond
    • Brooks, C. L. & Gu, W. p53 Ubiquitination: Mdm2 and beyond. Mol. Cell 21, 307-315 (2006).
    • (2006) Mol. Cell , vol.21 , pp. 307-315
    • Brooks, C.L.1    Gu, W.2
  • 25
    • 2442544457 scopus 로고    scopus 로고
    • MDM2 mediates p300/CREB-binding protein-associated factor ubiquitination and degradation
    • Jin, Y., Zeng, S. X., Lee, H. & Lu, H. MDM2 mediates p300/CREB-binding protein-associated factor ubiquitination and degradation. J. Biol. Chem. 279, 20035-20043 (2004).
    • (2004) J. Biol. Chem. , vol.279 , pp. 20035-20043
    • Jin, Y.1    Zeng, S.X.2    Lee, H.3    Lu, H.4
  • 26
    • 0037163085 scopus 로고    scopus 로고
    • MDM2 inhibits PCAF (p300/CREB-binding protein-associated factor)-mediated p53 acetylation
    • Jin, Y., Zeng, S. X., Dai, M. S., Yang, X. J. & Lu, H. MDM2 inhibits PCAF (p300/CREB-binding protein-associated factor)-mediated p53 acetylation. J. Biol. Chem. 277, 30838-30843 (2002).
    • (2002) J. Biol. Chem. , vol.277 , pp. 30838-30843
    • Jin, Y.1    Zeng, S.X.2    Dai, M.S.3    Yang, X.J.4    Lu, H.5
  • 27
    • 4944255743 scopus 로고    scopus 로고
    • Post-translational modification of p53 in tumorigenesis
    • Bode, A. M. & Dong, Z. Post-translational modification of p53 in tumorigenesis. Nature Rev. Cancer 4, 793-805 (2004).
    • (2004) Nature Rev. Cancer , vol.4 , pp. 793-805
    • Bode, A.M.1    Dong, Z.2
  • 28
    • 11844293427 scopus 로고    scopus 로고
    • p53 and prognosis: New insights and further complexity
    • Vousden, K. H. & Prives, C. p53 and prognosis: New insights and further complexity. Cell 120, 7-10 (2005).
    • (2005) Cell , vol.120 , pp. 7-10
    • Vousden, K.H.1    Prives, C.2
  • 29
    • 12244271066 scopus 로고    scopus 로고
    • Differential acetylation of Tat coordinates its interaction with the coactivators cyclin T1 and PCAF
    • Bres, V. et al. Differential acetylation of Tat coordinates its interaction with the coactivators cyclin T1 and PCAF. EMBO J. 21, 6811-6819 (2002).
    • (2002) EMBO J. , vol.21 , pp. 6811-6819
    • Bres, V.1
  • 30
    • 2142749540 scopus 로고    scopus 로고
    • Purification of recombinant p53 from Sf9 insect cells
    • Sun, X. Z., Nguyen, J. & Momand, J. Purification of recombinant p53 from Sf9 insect cells. Methods Mol. Biol. 234, 17-28 (2003).
    • (2003) Methods Mol. Biol. , vol.234 , pp. 17-28
    • Sun, X.Z.1    Nguyen, J.2    Momand, J.3
  • 31
    • 0036189045 scopus 로고    scopus 로고
    • Identification of a multicopy chromatin boundary element at the borders of silenced chromosomal domains
    • Cuvier, O., Hart, C. M., Kas, E. & Laemmli, U. K. Identification of a multicopy chromatin boundary element at the borders of silenced chromosomal domains. Chromosoma 110, 519-531 (2002).
    • (2002) Chromosoma , vol.110 , pp. 519-531
    • Cuvier, O.1    Hart, C.M.2    Kas, E.3    Laemmli, U.K.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.