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Volumn 23, Issue 2, 2015, Pages 322-331

An acetyl-methyl switch drives a conformational change in p53

Author keywords

[No Author keywords available]

Indexed keywords

53BP1 PROTEIN; BINDING PROTEIN; DNA; E1A ASSOCIATED P300 PROTEIN; PROTEIN P53; SERINE; THREONINE; UNCLASSIFIED DRUG; LIGAND; LYSINE;

EID: 84930189594     PISSN: 09692126     EISSN: 18784186     Source Type: Journal    
DOI: 10.1016/j.str.2014.12.010     Document Type: Article
Times cited : (23)

References (37)
  • 1
    • 33847328747 scopus 로고    scopus 로고
    • FBXO11 promotes the Neddylation of p53 and inhibits its transcriptional activity
    • W.M. Abida, A. Nikolaev, W. Zhao, W. Zhang, and W. Gu FBXO11 promotes the Neddylation of p53 and inhibits its transcriptional activity J. Biol. Chem. 282 2007 1797 1804
    • (2007) J. Biol. Chem. , vol.282 , pp. 1797-1804
    • Abida, W.M.1    Nikolaev, A.2    Zhao, W.3    Zhang, W.4    Gu, W.5
  • 2
    • 0035694469 scopus 로고    scopus 로고
    • Acetylation of p53 activates transcription through recruitment of coactivators/histone acetyltransferases
    • N.A. Barlev, L. Liu, N.H. Chehab, K. Mansfield, K.G. Harris, T.D. Halazonetis, and S.L. Berger Acetylation of p53 activates transcription through recruitment of coactivators/histone acetyltransferases Mol. Cell 8 2001 1243 1254
    • (2001) Mol. Cell , vol.8 , pp. 1243-1254
    • Barlev, N.A.1    Liu, L.2    Chehab, N.H.3    Mansfield, K.4    Harris, K.G.5    Halazonetis, T.D.6    Berger, S.L.7
  • 3
    • 42949171936 scopus 로고    scopus 로고
    • Recurrent initiation: A mechanism for triggering p53 pulses in response to DNA damage
    • E. Batchelor, C.S. Mock, I. Bhan, A. Loewer, and G. Lahav Recurrent initiation: a mechanism for triggering p53 pulses in response to DNA damage Mol. Cell 30 2008 277 289
    • (2008) Mol. Cell , vol.30 , pp. 277-289
    • Batchelor, E.1    Mock, C.S.2    Bhan, I.3    Loewer, A.4    Lahav, G.5
  • 4
    • 77954273218 scopus 로고    scopus 로고
    • Keeping p53 in check: A high-stakes balancing act
    • S.L. Berger Keeping p53 in check: a high-stakes balancing act Cell 142 2010 17 19
    • (2010) Cell , vol.142 , pp. 17-19
    • Berger, S.L.1
  • 5
    • 33845666681 scopus 로고    scopus 로고
    • Structural basis for the methylation state-specific recognition of histone H4-K20 by 53BP1 and Crb2 in DNA repair
    • M.V. Botuyan, J. Lee, I.M. Ward, J.E. Kim, J.R. Thompson, J. Chen, and G. Mer Structural basis for the methylation state-specific recognition of histone H4-K20 by 53BP1 and Crb2 in DNA repair Cell 127 2006 1361 1373
    • (2006) Cell , vol.127 , pp. 1361-1373
    • Botuyan, M.V.1    Lee, J.2    Ward, I.M.3    Kim, J.E.4    Thompson, J.R.5    Chen, J.6    Mer, G.7
  • 7
    • 84865790047 scopus 로고    scopus 로고
    • An integrated encyclopedia of DNA elements in the human genome
    • ENCODE Project Consortium
    • ENCODE Project Consortium B.E. Bernstein, E. Birney, I. Dunham, E.D. Green, C. Gunter, and M. Snyder An integrated encyclopedia of DNA elements in the human genome Nature 489 2012 57 74
    • (2012) Nature , vol.489 , pp. 57-74
    • Bernstein, B.E.1    Birney, E.2    Dunham, I.3    Green, E.D.4    Gunter, C.5    Snyder, M.6
  • 9
    • 78049302116 scopus 로고    scopus 로고
    • P53 post-translational modification: Deregulated in tumorigenesis
    • C. Dai, and W. Gu p53 post-translational modification: deregulated in tumorigenesis Trends Mol. Med. 16 2010 528 536
    • (2010) Trends Mol. Med. , vol.16 , pp. 528-536
    • Dai, C.1    Gu, W.2
  • 10
    • 79960125489 scopus 로고    scopus 로고
    • Peptide-protein interactions suggest that acetylation of lysines 381 and 382 of p53 is important for positive coactivator 4-p53 interaction
    • S. Debnath, S. Chatterjee, M. Arif, T.K. Kundu, and S. Roy Peptide-protein interactions suggest that acetylation of lysines 381 and 382 of p53 is important for positive coactivator 4-p53 interaction J. Biol. Chem. 286 2011 25076 25087
    • (2011) J. Biol. Chem. , vol.286 , pp. 25076-25087
    • Debnath, S.1    Chatterjee, S.2    Arif, M.3    Kundu, T.K.4    Roy, S.5
  • 11
    • 84891762808 scopus 로고    scopus 로고
    • Extensive post-translational modification of active and inactivated forms of endogenous p53
    • C.J. DeHart, J.S. Chahal, S.J. Flint, and D.H. Perlman Extensive post-translational modification of active and inactivated forms of endogenous p53 Mol. Cell. Proteomics 13 2014 1 17
    • (2014) Mol. Cell. Proteomics , vol.13 , pp. 1-17
    • Dehart, C.J.1    Chahal, J.S.2    Flint, S.J.3    Perlman, D.H.4
  • 12
    • 40549112996 scopus 로고    scopus 로고
    • Specific inhibition of Mdm2-mediated neddylation by Tip60
    • C. Dohmesen, M. Koeppel, and M. Dobbelstein Specific inhibition of Mdm2-mediated neddylation by Tip60 Cell Cycle 7 2008 222 231
    • (2008) Cell Cycle , vol.7 , pp. 222-231
    • Dohmesen, C.1    Koeppel, M.2    Dobbelstein, M.3
  • 13
    • 84877976173 scopus 로고    scopus 로고
    • Histone H4 deacetylation facilitates 53BP1 DNA damage signaling and double-strand break repair
    • K.Y. Hsiao, and C.A. Mizzen Histone H4 deacetylation facilitates 53BP1 DNA damage signaling and double-strand break repair J. Mol. Cell Biol. 5 2013 157 165
    • (2013) J. Mol. Cell Biol. , vol.5 , pp. 157-165
    • Hsiao, K.Y.1    Mizzen, C.A.2
  • 14
    • 44349108499 scopus 로고    scopus 로고
    • The emerging field of dynamic lysine methylation of non-histone proteins
    • J. Huang, and S.L. Berger The emerging field of dynamic lysine methylation of non-histone proteins Curr. Opin. Genet. Dev. 18 2008 152 158
    • (2008) Curr. Opin. Genet. Dev. , vol.18 , pp. 152-158
    • Huang, J.1    Berger, S.L.2
  • 19
    • 64149108150 scopus 로고    scopus 로고
    • P53 Oligomerization is essential for its C-terminal lysine acetylation
    • Y. Itahana, H. Ke, and Y. Zhang p53 Oligomerization is essential for its C-terminal lysine acetylation J. Biol. Chem. 284 2009 5158 5164
    • (2009) J. Biol. Chem. , vol.284 , pp. 5158-5164
    • Itahana, Y.1    Ke, H.2    Zhang, Y.3
  • 22
    • 33644990074 scopus 로고    scopus 로고
    • Charge modification at multiple C-terminal lysine residues regulates p53 oligomerization and its nucleus-cytoplasm trafficking
    • Y. Kawaguchi, A. Ito, E. Appella, and T.P. Yao Charge modification at multiple C-terminal lysine residues regulates p53 oligomerization and its nucleus-cytoplasm trafficking J. Biol. Chem. 281 2006 1394 1400
    • (2006) J. Biol. Chem. , vol.281 , pp. 1394-1400
    • Kawaguchi, Y.1    Ito, A.2    Appella, E.3    Yao, T.P.4
  • 25
    • 84862777719 scopus 로고    scopus 로고
    • Distinct regulatory mechanisms and functions for p53-activated and p53-repressed DNA damage response genes in embryonic stem cells
    • M. Li, Y. He, W. Dubois, X. Wu, J. Shi, and J. Huang Distinct regulatory mechanisms and functions for p53-activated and p53-repressed DNA damage response genes in embryonic stem cells Mol. Cell 46 2012 30 42
    • (2012) Mol. Cell , vol.46 , pp. 30-42
    • Li, M.1    He, Y.2    Dubois, W.3    Wu, X.4    Shi, J.5    Huang, J.6
  • 26
    • 77954312224 scopus 로고    scopus 로고
    • Basal dynamics of p53 reveal transcriptionally attenuated pulses in cycling cells
    • A. Loewer, E. Batchelor, G. Gaglia, and G. Lahav Basal dynamics of p53 reveal transcriptionally attenuated pulses in cycling cells Cell 142 2010 89 100
    • (2010) Cell , vol.142 , pp. 89-100
    • Loewer, A.1    Batchelor, E.2    Gaglia, G.3    Lahav, G.4
  • 27
    • 1442330508 scopus 로고    scopus 로고
    • Acetylation of p53 augments its site-specific DNA binding both in vitro and in vivo
    • J. Luo, M. Li, Y. Tang, M. Laszkowska, R.G. Roeder, and W. Gu Acetylation of p53 augments its site-specific DNA binding both in vitro and in vivo Proc. Natl. Acad. Sci. U S A 101 2004 2259 2264
    • (2004) Proc. Natl. Acad. Sci. U S A , vol.101 , pp. 2259-2264
    • Luo, J.1    Li, M.2    Tang, Y.3    Laszkowska, M.4    Roeder, R.G.5    Gu, W.6
  • 29
    • 16344381702 scopus 로고    scopus 로고
    • P53 C-terminal phosphorylation by CHK1 and CHK2 participates in the regulation of DNA-damage-induced C-terminal acetylation
    • Y.H. Ou, P.H. Chung, T.P. Sun, and S.Y. Shieh p53 C-terminal phosphorylation by CHK1 and CHK2 participates in the regulation of DNA-damage-induced C-terminal acetylation Mol. Biol. Cell 16 2005 1684 1695
    • (2005) Mol. Biol. Cell , vol.16 , pp. 1684-1695
    • Ou, Y.H.1    Chung, P.H.2    Sun, T.P.3    Shieh, S.Y.4
  • 32
    • 43049163953 scopus 로고    scopus 로고
    • Acetylation is indispensable for p53 activation
    • Y. Tang, W. Zhao, Y. Chen, Y. Zhao, and W. Gu Acetylation is indispensable for p53 activation Cell 133 2008 612 626
    • (2008) Cell , vol.133 , pp. 612-626
    • Tang, Y.1    Zhao, W.2    Chen, Y.3    Zhao, Y.4    Gu, W.5
  • 37
    • 41449114497 scopus 로고    scopus 로고
    • Structural basis of site-specific histone recognition by the bromodomains of human coactivators PCAF and CBP/p300
    • L. Zeng, Q. Zhang, G. Gerona-Navarro, N. Moshkina, and M.M. Zhou Structural basis of site-specific histone recognition by the bromodomains of human coactivators PCAF and CBP/p300 Structure 16 2008 643 652
    • (2008) Structure , vol.16 , pp. 643-652
    • Zeng, L.1    Zhang, Q.2    Gerona-Navarro, G.3    Moshkina, N.4    Zhou, M.M.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.