메뉴 건너뛰기




Volumn 106, Issue 34, 2009, Pages 14327-14332

Ultraslow oligomerization equilibria of p53 and its implications

Author keywords

Mass spectrometry; Protein protein interactions; Slow association; Tetramerization domain

Indexed keywords

DNA; PROTEIN BAX; PROTEIN P21; PROTEIN P53; TETRAMER;

EID: 70149100002     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.0907840106     Document Type: Article
Times cited : (49)

References (36)
  • 1
    • 47649096991 scopus 로고    scopus 로고
    • Structural biology of the tumor suppressor p53
    • Joerger AC, Fersht AR (2008) Structural biology of the tumor suppressor p53. Annu Rev Biochem 77:557-582.
    • (2008) Annu Rev Biochem , vol.77 , pp. 557-582
    • Joerger, A.C.1    Fersht, A.R.2
  • 2
    • 34248379012 scopus 로고    scopus 로고
    • Impact of mutant p53 functional properties on TP53 mutation patterns and tumor phenotype: Lessons from recent developments in the IARC TP53 database
    • DOI 10.1002/humu.20495
    • Petitjean A, et al. (2007) Impact of mutant p53 functional properties on TP53 mutation patterns and tumor phenotype: Lessons from recent developments in the IARC TP53 database. Hum Mutat 28:622-629. (Pubitemid 46744292)
    • (2007) Human Mutation , vol.28 , Issue.6 , pp. 622-629
    • Petitjean, A.1    Mathe, E.2    Kato, S.3    Ishioka, C.4    Tavtigian, S.V.5    Hainaut, P.6    Olivier, M.7
  • 4
    • 34047224955 scopus 로고    scopus 로고
    • Structure-function-rescue: The diverse nature of common p53 cancer mutants
    • Joerger AC, Fersht AR (2007) Structure-function-rescue: The diverse nature of common p53 cancer mutants. Oncogene 26:2226-2242.
    • (2007) Oncogene , vol.26 , pp. 2226-2242
    • Joerger, A.C.1    Fersht, A.R.2
  • 5
    • 43249104714 scopus 로고    scopus 로고
    • Different mutant/wild-type p53 combinations cause a spectrum of increased invasive potential in nonmalignant immortalized human mammary epithelial cells
    • Junk DJ, et al. (2008) Different mutant/wild-type p53 combinations cause a spectrum of increased invasive potential in nonmalignant immortalized human mammary epithelial cells. Neoplasia 10:450-461.
    • (2008) Neoplasia , vol.10 , pp. 450-461
    • Junk, D.J.1
  • 6
    • 0037066755 scopus 로고    scopus 로고
    • Biogenesis of p53 involves cotranslational dimerization of monomers and posttranslational dimerization of dimers. Implications on the dominant negative effect
    • Nicholls CD, McLure KG, Shields MA, Lee PW (2002) Biogenesis of p53 involves cotranslational dimerization of monomers and posttranslational dimerization of dimers. Implications on the dominant negative effect. J Biol Chem 277:12937-12945.
    • (2002) J Biol Chem , vol.277 , pp. 12937-12945
    • Nicholls, C.D.1    McLure, K.G.2    Shields, M.A.3    Lee, P.W.4
  • 9
    • 33847326819 scopus 로고    scopus 로고
    • Inactive full-length p53 mutants lacking dominant wild-type p53 inhibition highlight loss of heterozygosity as an important aspect of p53 status in human cancers
    • Dearth LR, et al. (2007) Inactive full-length p53 mutants lacking dominant wild-type p53 inhibition highlight loss of heterozygosity as an important aspect of p53 status in human cancers. Carcinogenesis 28:289-298.
    • (2007) Carcinogenesis , vol.28 , pp. 289-298
    • Dearth, L.R.1
  • 10
    • 67649389852 scopus 로고    scopus 로고
    • Modulation of the oligomerization state of p53 by differential binding of proteins of the S100 family to p53 monomers and tetramers
    • van Dieck J, Fernandez-Fernandez MR, Veprintsev DB, Fersht AR (2009) Modulation of the oligomerization state of p53 by differential binding of proteins of the S100 family to p53 monomers and tetramers. J Biol Chem 284:13804-13811.
    • (2009) J Biol Chem , vol.284 , pp. 13804-13811
    • Van Dieck, J.1    Fernandez-Fernandez, M.R.2    Veprintsev, D.B.3    Fersht, A.R.4
  • 11
    • 64549154804 scopus 로고    scopus 로고
    • Functional four-base A/T gap core sequence CATTAG of P53 response elements specifically bound tetrameric P53 differently than two-base A/T gap core sequence CATG bound both dimeric and tetrameric P53
    • Cai BH, et al. (2009) Functional four-base A/T gap core sequence CATTAG of P53 response elements specifically bound tetrameric P53 differently than two-base A/T gap core sequence CATG bound both dimeric and tetrameric P53. Nucleic Acids Res 37:1984-1990.
    • (2009) Nucleic Acids Res , vol.37 , pp. 1984-1990
    • Cai, B.H.1
  • 13
    • 0033523015 scopus 로고    scopus 로고
    • Oligomerization is required for p53 to be efficiently ubiquitinated by MDM2
    • Maki CG (1999) Oligomerization is required for p53 to be efficiently ubiquitinated by MDM2. J Biol Chem 274:16531-16535. (Pubitemid 129526411)
    • (1999) Journal of Biological Chemistry , vol.274 , Issue.23 , pp. 16531-16535
    • Maki, C.G.1
  • 14
    • 0033559256 scopus 로고    scopus 로고
    • A leucine-rich nuclear export signal in the p53 tetramerization domain: Regulation of subcellular localization and p53 activity by NES masking
    • Stommel JM, et al. (1999) A leucine-rich nuclear export signal in the p53 tetramerization domain: Regulation of subcellular localization and p53 activity by NES masking. EMBO J 18:1660-1672.
    • (1999) EMBO J , vol.18 , pp. 1660-1672
    • Stommel, J.M.1
  • 15
    • 64149108150 scopus 로고    scopus 로고
    • P53 oligomerization is essential for its C-terminal lysine acetylation
    • Itahana Y, Ke H, Zhang Y (2008) p53 oligomerization is essential for its C-terminal lysine acetylation. J Biol Chem 284:5158-5164.
    • (2008) J Biol Chem , vol.284 , pp. 5158-5164
    • Itahana, Y.1    Ke, H.2    Zhang, Y.3
  • 16
    • 0024438708 scopus 로고
    • Electrospray ionization for mass spectrometry of large biomolecules
    • Fenn JB, Mann M, Meng CK, Wong SF, Whitehouse CM (1989) Electrospray ionization for mass spectrometry of large biomolecules. Science 246:64-71. (Pubitemid 19252085)
    • (1989) Science , vol.246 , Issue.4926 , pp. 64-71
    • Fenn, J.B.1    Mann, M.2    Meng, C.K.3    Wong, S.F.4    Whitehouse, C.M.5
  • 17
    • 34548426979 scopus 로고    scopus 로고
    • The role of mass spectrometry in structure elucidation of dynamic protein complexes
    • Sharon M, Robinson CV (2007) The role of mass spectrometry in structure elucidation of dynamic protein complexes. Annu Rev Biochem 76:167-193.
    • (2007) Annu Rev Biochem , vol.76 , pp. 167-193
    • Sharon, M.1    Robinson, C.V.2
  • 19
    • 29244481662 scopus 로고    scopus 로고
    • L55P transthyretin accelerates subunit exchange and leads to rapid formation of hybrid tetramers
    • Keetch CA, et al. (2005) L55P transthyretin accelerates subunit exchange and leads to rapid formation of hybrid tetramers. J Biol Chem 280:41667-41674.
    • (2005) J Biol Chem , vol.280 , pp. 41667-41674
    • Keetch, C.A.1
  • 20
    • 20444487795 scopus 로고    scopus 로고
    • Determination of affinity constants and response factors of the noncovalent dimer of gramicidin by electrospray ionization mass spectrometry and mathematical modeling
    • Chitta RK, Rempel DL, Gross ML (2005) Determination of affinity constants and response factors of the noncovalent dimer of gramicidin by electrospray ionization mass spectrometry and mathematical modeling. J Am Soc Mass Spectrom 16:1031-1038.
    • (2005) J Am Soc Mass Spectrom , vol.16 , pp. 1031-1038
    • Chitta, R.K.1    Rempel, D.L.2    Gross, M.L.3
  • 21
    • 0037064096 scopus 로고    scopus 로고
    • Subunit exchange of multimeric protein complexes: Real-time monitoring of subunit exchange between small heat shock proteins by using electrospray mass spectrometry
    • DOI 10.1074/jbc.M206060200
    • Sobott F, Benesch JL, Vierling E, Robinson CV (2002) Subunit exchange of multimeric protein complexes. Real-time monitoring of subunit exchange between small heat shock proteins by using electrospray mass spectrometry. J Biol Chem 277:38921-38929. (Pubitemid 35154757)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.41 , pp. 38921-38929
    • Sobott, F.1    Benesch, J.L.P.2    Vierling, E.3    Robinson, C.V.4
  • 23
    • 0347723910 scopus 로고    scopus 로고
    • Crystal structure of a superstable mutant of human p53 core domain. Insights into the mechanism of rescuing oncogenic mutations
    • Joerger AC, Allen MD, Fersht AR (2004) Crystal structure of a superstable mutant of human p53 core domain. Insights into the mechanism of rescuing oncogenic mutations. J Biol Chem 279:1291-1296.
    • (2004) J Biol Chem , vol.279 , pp. 1291-1296
    • Joerger, A.C.1    Allen, M.D.2    Fersht, A.R.3
  • 25
    • 18144387188 scopus 로고    scopus 로고
    • Structures of p53 cancer mutants and mechanism of rescue by second-site suppressor mutations
    • Joerger AC, Ang HC, Veprintsev DB, Blair CM, Fersht AR (2005) Structures of p53 cancer mutants and mechanism of rescue by second-site suppressor mutations. J Biol Chem 280:16030-16037.
    • (2005) J Biol Chem , vol.280 , pp. 16030-16037
    • Joerger, A.C.1    Ang, H.C.2    Veprintsev, D.B.3    Blair, C.M.4    Fersht, A.R.5
  • 26
    • 0034594995 scopus 로고    scopus 로고
    • Quantitative analysis of residual folding and DNA binding in mutant p53 core domain: Definition of mutant states for rescue in cancer therapy
    • Bullock AN, Henckel J, Fersht AR (2000) Quantitative analysis of residual folding and DNA binding in mutant p53 core domain: Definition of mutant states for rescue in cancer therapy. Oncogene 19:1245-1256. (Pubitemid 30160617)
    • (2000) Oncogene , vol.19 , Issue.10 , pp. 1245-1256
    • Bullock, A.N.1    Henckel, J.2    Fersht, A.R.3
  • 28
    • 0037591875 scopus 로고    scopus 로고
    • Kinetic instability of p53 core domain mutants. Implications for rescue by small molecules
    • DOI 10.1074/jbc.M302458200
    • Friedler A, Veprintsev DB, Hansson LO, Fersht AR (2003) Kinetic instability of p53 core domain mutants: Implications for rescue by small molecules. J Biol Chem 278:24108-24112. (Pubitemid 36830245)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.26 , pp. 24108-24112
    • Friedler, A.1    Veprintsev, D.B.2    Hansson, L.O.3    Fersht, A.R.4
  • 29
    • 41149090794 scopus 로고    scopus 로고
    • Algorithm for prediction of tumour suppressor p53 affinity for binding sites in DNA
    • Veprintsev DB, Fersht AR (2008) Algorithm for prediction of tumour suppressor p53 affinity for binding sites in DNA. Nucleic Acids Res 36:1589-1598.
    • (2008) Nucleic Acids Res , vol.36 , pp. 1589-1598
    • Veprintsev, D.B.1    Fersht, A.R.2
  • 31
    • 33750036093 scopus 로고    scopus 로고
    • Structural basis for understanding oncogenic p53 mutations and designing rescue drugs
    • Joerger AC, Ang HC, Fersht AR (2006) Structural basis for understanding oncogenic p53 mutations and designing rescue drugs. Proc Natl Acad Sci USA 103:15056-15061.
    • (2006) Proc Natl Acad Sci USA , vol.103 , pp. 15056-15061
    • Joerger, A.C.1    Ang, H.C.2    Fersht, A.R.3
  • 32
    • 33845959658 scopus 로고    scopus 로고
    • Effects of oncogenic mutations and DNA response elements on the binding of p53 to p53-binding protein 2 (53BP2)
    • DOI 10.1074/jbc.M604725200
    • Tidow H, Veprintsev DB, Freund SM, Fersht AR (2006) Effects of oncogenic mutations and DNA response elements on the binding of p53 to p53-binding protein 2 (53BP2). J Biol Chem 281:32526-32533. (Pubitemid 46036807)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.43 , pp. 32526-32533
    • Tidow, H.1    Veprintsev, D.B.2    Freund, S.M.V.3    Fersht, A.R.4
  • 33
  • 35
    • 0037086063 scopus 로고    scopus 로고
    • A tandem mass spectrometer for improved transmission and analysis of large macromolecular assemblies
    • DOI 10.1021/ac0110552
    • Sobott F, Hernandez H, McCammon MG, Tito MA, Robinson CV (2002) A tandem mass spectrometer for improved transmission and analysis of large macromolecular assemblies. Anal Chem 74:1402-1407. (Pubitemid 34233333)
    • (2002) Analytical Chemistry , vol.74 , Issue.6 , pp. 1402-1407
    • Sobott, F.1    Hernandez, H.2    McCammon, M.G.3    Tito, M.A.4    Robinson, C.V.5
  • 36
    • 0032555738 scopus 로고    scopus 로고
    • Protein subunit interactions and structural integrity of amyloidogenic transthyretins: Evidence from electrospray mass spectrometry
    • Nettleton EJ, et al. (1998) Protein subunit interactions and structural integrity of amyloidogenic transthyretins: Evidence from electrospray mass spectrometry. J Mol Biol 281:553-564.
    • (1998) J Mol Biol , vol.281 , pp. 553-564
    • Nettleton, E.J.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.