메뉴 건너뛰기




Volumn 449, Issue 7158, 2007, Pages 105-108

p53 is regulated by the lysine demethylase LSD1

Author keywords

[No Author keywords available]

Indexed keywords

BINDING PROTEIN; HISTONE; LYSINE; LYSINE DEMETHYLASE 1; METHYLTRANSFERASE; P53 BINDING PROTEIN 1; PROTEIN P53; UNCLASSIFIED DRUG;

EID: 34548513035     PISSN: 00280836     EISSN: 14764687     Source Type: Journal    
DOI: 10.1038/nature06092     Document Type: Article
Times cited : (676)

References (28)
  • 1
    • 9244247669 scopus 로고    scopus 로고
    • Regulation of p53 activity through lysine methylation
    • Chuikov, S. et al. Regulation of p53 activity through lysine methylation. Nature 432, 353-360 (2004).
    • (2004) Nature , vol.432 , pp. 353-360
    • Chuikov, S.1
  • 2
    • 33845204856 scopus 로고    scopus 로고
    • Repression of p53 activity by Smyd2-mediated methylation
    • Huang, J. et al. Repression of p53 activity by Smyd2-mediated methylation. Nature 444, 629-632 (2006).
    • (2006) Nature , vol.444 , pp. 629-632
    • Huang, J.1
  • 3
    • 0037470142 scopus 로고    scopus 로고
    • A candidate X-linked mental retardation gene is a component of a new family of histone deacetylase-containing complexes
    • Hakimi, M. A., Dong, Y., Lane, W. S., Speicher, D. W. & Shiekhattar, R. A candidate X-linked mental retardation gene is a component of a new family of histone deacetylase-containing complexes. J. Biol. Chem. 278, 7234-7239 (2003).
    • (2003) J. Biol. Chem , vol.278 , pp. 7234-7239
    • Hakimi, M.A.1    Dong, Y.2    Lane, W.S.3    Speicher, D.W.4    Shiekhattar, R.5
  • 4
    • 11144332565 scopus 로고    scopus 로고
    • Histone demethylation mediated by the nuclear amine oxidase homolog LSD1
    • Shi, Y. et al. Histone demethylation mediated by the nuclear amine oxidase homolog LSD1. Cell 119, 941-953 (2004).
    • (2004) Cell , vol.119 , pp. 941-953
    • Shi, Y.1
  • 5
    • 25144519737 scopus 로고    scopus 로고
    • An essential role for CoREST in nucleosomal histone 3 lysine 4 demethylation
    • Lee, M. G., Wynder, C., Cooch, N. & Shiekhattar, R. An essential role for CoREST in nucleosomal histone 3 lysine 4 demethylation. Nature 437, 432-435 (2005).
    • (2005) Nature , vol.437 , pp. 432-435
    • Lee, M.G.1    Wynder, C.2    Cooch, N.3    Shiekhattar, R.4
  • 6
    • 24144462170 scopus 로고    scopus 로고
    • LSD1 demethylates repressive histone marks to promote androgen-receptor-dependent transcription
    • Metzger, E. et al. LSD1 demethylates repressive histone marks to promote androgen-receptor-dependent transcription. Nature 437, 436-439 (2005).
    • (2005) Nature , vol.437 , pp. 436-439
    • Metzger, E.1
  • 7
    • 0032567967 scopus 로고    scopus 로고
    • Reconstitution of telomerase activity in normal human cells leads to elongation of telomeres and extended replicative life span
    • Vaziri, H. & Benchimol, S. Reconstitution of telomerase activity in normal human cells leads to elongation of telomeres and extended replicative life span. Curr. Biol. 8, 279-282 (1998).
    • (1998) Curr. Biol , vol.8 , pp. 279-282
    • Vaziri, H.1    Benchimol, S.2
  • 8
    • 0026446686 scopus 로고
    • Identification of a minimal transforming domain of p53: Negative dominance through abrogation of sequence-specific DNA binding
    • Shaulian, E., Zauberman, A., Ginsberg, D. & Oren, M. Identification of a minimal transforming domain of p53: negative dominance through abrogation of sequence-specific DNA binding. Mol. Cell. Biol. 12, 5581-5592 (1992).
    • (1992) Mol. Cell. Biol , vol.12 , pp. 5581-5592
    • Shaulian, E.1    Zauberman, A.2    Ginsberg, D.3    Oren, M.4
  • 9
    • 32844454603 scopus 로고    scopus 로고
    • Histone demethylation by a family of JmjC domain-containing proteins
    • Tsukada, Y. et al. Histone demethylation by a family of JmjC domain-containing proteins. Nature 439, 811-816 (2006).
    • (2006) Nature , vol.439 , pp. 811-816
    • Tsukada, Y.1
  • 10
    • 33646138230 scopus 로고    scopus 로고
    • JHDM2A, a JmjC-containing H3K9 demethylase, facilitates transcription activation by androgen receptor
    • Yamane, K. et al. JHDM2A, a JmjC-containing H3K9 demethylase, facilitates transcription activation by androgen receptor. Cell 125, 483-495 (2006).
    • (2006) Cell , vol.125 , pp. 483-495
    • Yamane, K.1
  • 11
    • 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
  • 12
    • 0030797585 scopus 로고    scopus 로고
    • Activation of p53 sequence-specific DNA binding by acetylation of the p53 C-terminal domain
    • Gu, W. & Roeder, R. G. Activation of p53 sequence-specific DNA binding by acetylation of the p53 C-terminal domain. Cell 90, 595-606 (1997).
    • (1997) Cell , vol.90 , pp. 595-606
    • Gu, W.1    Roeder, R.G.2
  • 13
    • 20444417108 scopus 로고    scopus 로고
    • WDR5 associates with histone H3 methylated at K4 and is essential for H3 K4 methylation and vertebrate development
    • Wysocka, J. et al. WDR5 associates with histone H3 methylated at K4 and is essential for H3 K4 methylation and vertebrate development. Cell 121, 859-872 (2005).
    • (2005) Cell , vol.121 , pp. 859-872
    • Wysocka, J.1
  • 14
    • 33745839365 scopus 로고    scopus 로고
    • A PHD finger of NURF couples histone H3 lysine 4 trimethylation with chromatin remodelling
    • Wysocka, J. et al. A PHD finger of NURF couples histone H3 lysine 4 trimethylation with chromatin remodelling. Nature 442, 86-90 (2006).
    • (2006) Nature , vol.442 , pp. 86-90
    • Wysocka, J.1
  • 15
    • 33745868054 scopus 로고    scopus 로고
    • ING2 PHD domain links histone H3 lysine 4 methylation to active gene repression
    • Shi, X. et al. ING2 PHD domain links histone H3 lysine 4 methylation to active gene repression. Nature 442, 96-99 (2006).
    • (2006) Nature , vol.442 , pp. 96-99
    • Shi, X.1
  • 16
    • 33745818717 scopus 로고    scopus 로고
    • Molecular mechanism of histone H3K4me3 recognition by plant homeodomain of ING2
    • Pena, P. V. et al. Molecular mechanism of histone H3K4me3 recognition by plant homeodomain of ING2. Nature 442, 100-103 (2006).
    • (2006) Nature , vol.442 , pp. 100-103
    • Pena, P.V.1
  • 17
    • 33745809637 scopus 로고    scopus 로고
    • Molecular basis for site-specific read-out of histone H3K4me3 by the BPTF PHD finger of NURF
    • Li, H. et al. Molecular basis for site-specific read-out of histone H3K4me3 by the BPTF PHD finger of NURF. Nature 442, 91-95 (2006).
    • (2006) Nature , vol.442 , pp. 91-95
    • Li, H.1
  • 18
    • 33645502395 scopus 로고    scopus 로고
    • Tudor, MBT and chromo domains gauge the degree of lysine methylation
    • 397-403
    • Kim, J. et al. Tudor, MBT and chromo domains gauge the degree of lysine methylation. EMBO Rep. 7, 397-403 (2006).
    • (2006) EMBO Rep , vol.7
    • Kim, J.1
  • 19
    • 9244252580 scopus 로고    scopus 로고
    • Methylated lysine 79 of histone H3 targets 53BP1 to DNA double-strand breaks
    • Huyen, Y. et al. Methylated lysine 79 of histone H3 targets 53BP1 to DNA double-strand breaks. Nature 432, 406-411 (2004).
    • (2004) Nature , vol.432 , pp. 406-411
    • Huyen, Y.1
  • 20
    • 33845666681 scopus 로고    scopus 로고
    • Structural basis for the methylation state-specific recognition of histone H4-K20 by 53BP1 and Crb2 in DNA repair
    • Botuyan, M. V. et al. Structural basis for the methylation state-specific recognition of histone H4-K20 by 53BP1 and Crb2 in DNA repair. Cell 127, 1361-1373 (2006).
    • (2006) Cell , vol.127 , pp. 1361-1373
    • Botuyan, M.V.1
  • 22
    • 4544235194 scopus 로고    scopus 로고
    • Functional interaction between BLM helicase and 53BP1 in a Chk1-mediated pathway during S-phase arrest
    • Sengupta, S. et al. Functional interaction between BLM helicase and 53BP1 in a Chk1-mediated pathway during S-phase arrest. J. Cell Biol. 166, 801-813 (2004).
    • (2004) J. Cell Biol , vol.166 , pp. 801-813
    • Sengupta, S.1
  • 23
    • 33846015507 scopus 로고    scopus 로고
    • The tandem BRCT domain of 53BP1 is not required for its repair function
    • Ward, I. et al. The tandem BRCT domain of 53BP1 is not required for its repair function. J. Biol. Chem. 281, 38472-38477 (2006).
    • (2006) J. Biol. Chem , vol.281 , pp. 38472-38477
    • Ward, I.1
  • 24
    • 0032475885 scopus 로고    scopus 로고
    • Stimulation of p53-mediated transcriptional activation by the p53-binding proteins, 53BP1 and 53BP2
    • Iwabuchi, K. et al. Stimulation of p53-mediated transcriptional activation by the p53-binding proteins, 53BP1 and 53BP2. J. Biol. Chem. 273, 26061-26068 (1998).
    • (1998) J. Biol. Chem , vol.273 , pp. 26061-26068
    • Iwabuchi, K.1
  • 25
    • 33646343474 scopus 로고    scopus 로고
    • An shRNA barcode screen provides insight into cancer cell vulnerability to MDM2 inhibitors
    • Brummelkamp, T. R. et al. An shRNA barcode screen provides insight into cancer cell vulnerability to MDM2 inhibitors. Nature Chem. Biol. 2, 202-206 (2006).
    • (2006) Nature Chem. Biol , vol.2 , pp. 202-206
    • Brummelkamp, T.R.1
  • 26
    • 33845270990 scopus 로고    scopus 로고
    • Regulating the p53 pathway: In vitro hypotheses, in vivo veritas
    • Toledo, F. & Wahl, G. M. Regulating the p53 pathway: in vitro hypotheses, in vivo veritas. Nature Rev. Cancer 6, 909-923 (2006).
    • (2006) Nature Rev. Cancer , vol.6 , pp. 909-923
    • Toledo, F.1    Wahl, G.M.2
  • 27
    • 30744471717 scopus 로고    scopus 로고
    • 53BP1 and p53 synergize to suppress genomic instability and lymphomagenesis
    • Morales, J. C. et al. 53BP1 and p53 synergize to suppress genomic instability and lymphomagenesis. Proc. Natl Acad. Sci. USA 103, 3310-3315 (2006).
    • (2006) Proc. Natl Acad. Sci. USA , vol.103 , pp. 3310-3315
    • Morales, J.C.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.