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Volumn 423, Issue 4, 2012, Pages 515-527

Structural basis for ASPP2 recognition by the tumor suppressor p73

Author keywords

53BP2; DNA damage; mutant p53; TP73; transactivation

Indexed keywords

ANKYRIN; ASPP2 PROTEIN; PROTEIN P53; PROTEIN P73; PROTEIN SH3; PROTEIN VARIANT; UNCLASSIFIED DRUG;

EID: 84867263844     PISSN: 00222836     EISSN: 10898638     Source Type: Journal    
DOI: 10.1016/j.jmb.2012.08.005     Document Type: Article
Times cited : (19)

References (61)
  • 1
    • 33646798450 scopus 로고    scopus 로고
    • P53/p63/p73 isoforms: An orchestra of isoforms to harmonise cell differentiation and response to stress
    • F. Murray-Zmijewski, D.P. Lane, and J.C. Bourdon p53/p63/p73 isoforms: an orchestra of isoforms to harmonise cell differentiation and response to stress Cell Death Differ. 13 2006 962 972
    • (2006) Cell Death Differ. , vol.13 , pp. 962-972
    • Murray-Zmijewski, F.1    Lane, D.P.2    Bourdon, J.C.3
  • 2
    • 33847230852 scopus 로고    scopus 로고
    • The p53 family in differentiation and tumorigenesis
    • T. Stiewe The p53 family in differentiation and tumorigenesis Nat. Rev. Cancer 7 2007 165 168
    • (2007) Nat. Rev. Cancer , vol.7 , pp. 165-168
    • Stiewe, T.1
  • 3
    • 0037041392 scopus 로고    scopus 로고
    • P63 and p73 are required for p53-dependent apoptosis in response to DNA damage
    • E.R. Flores, K.Y. Tsai, D. Crowley, S. Sengupta, A. Yang, F. McKeon, and T. Jacks p63 and p73 are required for p53-dependent apoptosis in response to DNA damage Nature 416 2002 560 564
    • (2002) Nature , vol.416 , pp. 560-564
    • Flores, E.R.1    Tsai, K.Y.2    Crowley, D.3    Sengupta, S.4    Yang, A.5    McKeon, F.6    Jacks, T.7
  • 4
    • 34547753615 scopus 로고    scopus 로고
    • P63 and p73 in human cancer: Defining the network
    • M.P. DeYoung, and L.W. Ellisen p63 and p73 in human cancer: defining the network Oncogene 26 2007 5169 5183
    • (2007) Oncogene , vol.26 , pp. 5169-5183
    • Deyoung, M.P.1    Ellisen, L.W.2
  • 6
    • 0037222381 scopus 로고    scopus 로고
    • Germline TP53 mutations and Li-Fraumeni syndrome
    • J.M. Varley Germline TP53 mutations and Li-Fraumeni syndrome Hum. Mutat. 21 2003 313 320
    • (2003) Hum. Mutat. , vol.21 , pp. 313-320
    • Varley, J.M.1
  • 7
    • 0033594485 scopus 로고    scopus 로고
    • P63 is essential for regenerative proliferation in limb, craniofacial and epithelial development
    • A. Yang, R. Schweitzer, D.Q. Sun, M. Kaghad, N. Walker, and R.T. Bronson p63 is essential for regenerative proliferation in limb, craniofacial and epithelial development Nature 398 1999 714 718
    • (1999) Nature , vol.398 , pp. 714-718
    • Yang, A.1    Schweitzer, R.2    Sun, D.Q.3    Kaghad, M.4    Walker, N.5    Bronson, R.T.6
  • 8
    • 17544363909 scopus 로고    scopus 로고
    • P73-deficient mice have neurological, pheromonal and inflammatory defects but lack spontaneous tumours
    • A. Yang, N. Walker, R. Bronson, M. Kaghad, M. Oosterwegel, and J. Bonnin p73-deficient mice have neurological, pheromonal and inflammatory defects but lack spontaneous tumours Nature 404 2000 99 103
    • (2000) Nature , vol.404 , pp. 99-103
    • Yang, A.1    Walker, N.2    Bronson, R.3    Kaghad, M.4    Oosterwegel, M.5    Bonnin, J.6
  • 9
    • 0033387525 scopus 로고    scopus 로고
    • Structure and function in the p53 family
    • C.H. Arrowsmith Structure and function in the p53 family Cell Death Differ. 6 1999 1169 1173
    • (1999) Cell Death Differ. , vol.6 , pp. 1169-1173
    • Arrowsmith, C.H.1
  • 12
    • 77949362925 scopus 로고    scopus 로고
    • Isoform-specific p73 knockout mice reveal a novel role for Delta Np73 in the DNA damage response pathway
    • M.T. Wilhelm, A. Rufini, M.K. Wetzel, K. Tsuchihara, S. Inoue, and R. Tomasini Isoform-specific p73 knockout mice reveal a novel role for Delta Np73 in the DNA damage response pathway Genes Dev. 24 2010 549 560
    • (2010) Genes Dev. , vol.24 , pp. 549-560
    • Wilhelm, M.T.1    Rufini, A.2    Wetzel, M.K.3    Tsuchihara, K.4    Inoue, S.5    Tomasini, R.6
  • 13
    • 53549134949 scopus 로고    scopus 로고
    • TAp73 knockout shows genomic instability with infertility and tumor suppressor functions
    • R. Tomasini, K. Tsuchihara, M. Wilhelm, M. Fujitani, A. Rufini, and C.C. Cheung TAp73 knockout shows genomic instability with infertility and tumor suppressor functions Genes Dev. 22 2008 2677 2691
    • (2008) Genes Dev. , vol.22 , pp. 2677-2691
    • Tomasini, R.1    Tsuchihara, K.2    Wilhelm, M.3    Fujitani, M.4    Rufini, A.5    Cheung, C.C.6
  • 14
    • 0031564954 scopus 로고    scopus 로고
    • P73 is a simian [correction of human] p53-related protein that can induce apoptosis
    • C.A. Jost, M.C. Marin, and W.G. Kaelin Jr p73 is a simian [correction of human] p53-related protein that can induce apoptosis Nature 389 1997 191 194
    • (1997) Nature , vol.389 , pp. 191-194
    • Jost, C.A.1    Marin, M.C.2    Kaelin, Jr.W.G.3
  • 15
    • 77953170345 scopus 로고    scopus 로고
    • P73 tumor suppressor protein A close relative of p53 not only in structure but also in anti-cancer approach?
    • J. Zawacka-Pankau, A. Kostecka, A. Sznarkowska, E. Hedstrom, and A. Kawiak p73 tumor suppressor protein A close relative of p53 not only in structure but also in anti-cancer approach? Cell Cycle 9 2010 720 728
    • (2010) Cell Cycle , vol.9 , pp. 720-728
    • Zawacka-Pankau, J.1    Kostecka, A.2    Sznarkowska, A.3    Hedstrom, E.4    Kawiak, A.5
  • 16
    • 33746615125 scopus 로고    scopus 로고
    • Small-molecule modulators of p53 family signaling and antitumor effects in p53-deficient human colon tumor xenografts
    • W. Wang, S.H. Kim, and W.S. El-Deiry Small-molecule modulators of p53 family signaling and antitumor effects in p53-deficient human colon tumor xenografts Proc. Natl Acad. Sci. USA 103 2006 11003 11008
    • (2006) Proc. Natl Acad. Sci. USA , vol.103 , pp. 11003-11008
    • Wang, W.1    Kim, S.H.2    El-Deiry, W.S.3
  • 18
    • 34147190124 scopus 로고    scopus 로고
    • A p53-derived apoptotic peptide derepresses p73 to cause tumor regression in vivo
    • H.S. Bell, C. Dufes, J. O'Prey, D. Crighton, D. Bergamaschi, and X. Lu A p53-derived apoptotic peptide derepresses p73 to cause tumor regression in vivo J. Clin. Invest. 117 2007 1008 1018
    • (2007) J. Clin. Invest. , vol.117 , pp. 1008-1018
    • Bell, H.S.1    Dufes, C.2    O'Prey, J.3    Crighton, D.4    Bergamaschi, D.5    Lu, X.6
  • 19
    • 38949199337 scopus 로고    scopus 로고
    • HDM2 antagonist Nutlin-3 disrupts p73-HDM2 binding and enhances p73 function
    • L.M. Lau, J.K. Nugent, X. Zhao, and M.S. Irwin HDM2 antagonist Nutlin-3 disrupts p73-HDM2 binding and enhances p73 function Oncogene 27 2008 997 1003
    • (2008) Oncogene , vol.27 , pp. 997-1003
    • Lau, L.M.1    Nugent, J.K.2    Zhao, X.3    Irwin, M.S.4
  • 20
    • 84863046504 scopus 로고    scopus 로고
    • Aurora kinase-A inactivates DNA damage-induced apoptosis and spindle assembly checkpoint response functions of p73
    • H. Katayama, J. Wang, W. Treekitkarnmongkol, H. Kawai, K. Sasai, and H. Zhang Aurora kinase-A inactivates DNA damage-induced apoptosis and spindle assembly checkpoint response functions of p73 Cancer Cell 21 2012 196 211
    • (2012) Cancer Cell , vol.21 , pp. 196-211
    • Katayama, H.1    Wang, J.2    Treekitkarnmongkol, W.3    Kawai, H.4    Sasai, K.5    Zhang, H.6
  • 21
    • 55349124289 scopus 로고    scopus 로고
    • Aurora kinase A inhibition leads to p73-dependent apoptosis in p53-deficient cancer cells
    • A.A. Dar, A. Belkhiri, J. Ecsedy, A. Zaika, and W. El-Rifai Aurora kinase A inhibition leads to p73-dependent apoptosis in p53-deficient cancer cells Cancer Res. 68 2008 8998 9004
    • (2008) Cancer Res. , vol.68 , pp. 8998-9004
    • Dar, A.A.1    Belkhiri, A.2    Ecsedy, J.3    Zaika, A.4    El-Rifai, W.5
  • 22
    • 77955709042 scopus 로고    scopus 로고
    • Combination of nutlin-3 and VX-680 selectively targets p53 mutant cells with reversible effects on cells expressing wild-type p53
    • C.F. Cheok, N. Kua, P. Kaldis, and D.P. Lane Combination of nutlin-3 and VX-680 selectively targets p53 mutant cells with reversible effects on cells expressing wild-type p53 Cell Death Differ. 17 2010 1486 1500
    • (2010) Cell Death Differ. , vol.17 , pp. 1486-1500
    • Cheok, C.F.1    Kua, N.2    Kaldis, P.3    Lane, D.P.4
  • 25
    • 0030575866 scopus 로고    scopus 로고
    • Structure of the p53 tumor suppressor bound to the ankyrin and SH3 domains of 53BP2
    • S. Gorina, and N.P. Pavletich Structure of the p53 tumor suppressor bound to the ankyrin and SH3 domains of 53BP2 Science 274 1996 1001 1005
    • (1996) Science , vol.274 , pp. 1001-1005
    • Gorina, S.1    Pavletich, N.P.2
  • 27
    • 0027983669 scopus 로고
    • Crystal structure of a P53 tumor-suppressor DNA complex - Understanding tumorigenic mutations
    • Y.J. Cho, S. Gorina, P.D. Jeffrey, and N.P. Pavletich Crystal structure of a P53 tumor-suppressor DNA complex - understanding tumorigenic mutations Science 265 1994 346 355
    • (1994) Science , vol.265 , pp. 346-355
    • Cho, Y.J.1    Gorina, S.2    Jeffrey, P.D.3    Pavletich, N.P.4
  • 29
    • 79953315362 scopus 로고    scopus 로고
    • Redox modulation of p53: Mechanisms and functional significance
    • D.H. Kim, J.K. Kundu, and Y.J. Surh Redox modulation of p53: mechanisms and functional significance Mol. Carcinog. 50 2011 222 234
    • (2011) Mol. Carcinog. , vol.50 , pp. 222-234
    • Kim, D.H.1    Kundu, J.K.2    Surh, Y.J.3
  • 30
    • 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
    • A.N. Bullock, J. Henckel, and A.R. Fersht Quantitative analysis of residual folding and DNA binding in mutant p53 core domain: definition of mutant states for rescue in cancer therapy Oncogene 19 2000 1245 1256
    • (2000) Oncogene , vol.19 , pp. 1245-1256
    • Bullock, A.N.1    Henckel, J.2    Fersht, A.R.3
  • 33
    • 84855823856 scopus 로고    scopus 로고
    • Structure and kinetic stability of the p63 tetramerization domain
    • E. Natan, and A.C. Joerger Structure and kinetic stability of the p63 tetramerization domain J. Mol. Biol. 415 2012 503 513
    • (2012) J. Mol. Biol. , vol.415 , pp. 503-513
    • Natan, E.1    Joerger, A.C.2
  • 35
    • 70449713323 scopus 로고    scopus 로고
    • Conformational stability and activity of p73 require a second helix in the tetramerization domain
    • D. Coutandin, F. Lohr, F.H. Niesen, T. Ikeya, T.A. Weber, and B. Schafer Conformational stability and activity of p73 require a second helix in the tetramerization domain Cell Death Differ. 16 2009 1582 1589
    • (2009) Cell Death Differ. , vol.16 , pp. 1582-1589
    • Coutandin, D.1    Lohr, F.2    Niesen, F.H.3    Ikeya, T.4    Weber, T.A.5    Schafer, B.6
  • 36
    • 33846704798 scopus 로고    scopus 로고
    • P53 and p73 display common and distinct requirements for sequence specific binding to DNA
    • M. Lokshin, Y. Li, C. Gaiddon, and C. Prives p53 and p73 display common and distinct requirements for sequence specific binding to DNA Nucleic Acids Res. 35 2007 340 352
    • (2007) Nucleic Acids Res. , vol.35 , pp. 340-352
    • Lokshin, M.1    Li, Y.2    Gaiddon, C.3    Prives, C.4
  • 37
    • 74549130412 scopus 로고    scopus 로고
    • Conservation of DNA-binding specificity and oligomerisation properties within the p53 family
    • T. Brandt, M. Petrovich, A.C. Joerger, and D.B. Veprintsev Conservation of DNA-binding specificity and oligomerisation properties within the p53 family BMC Genomics 10 2009 628
    • (2009) BMC Genomics , vol.10 , pp. 628
    • Brandt, T.1    Petrovich, M.2    Joerger, A.C.3    Veprintsev, D.B.4
  • 38
    • 79955609976 scopus 로고    scopus 로고
    • Structures of p63 DNA binding domain in complexes with half-site and with spacer-containing full response elements
    • C. Chen, N. Gorlatova, Z. Kelman, and O. Herzberg Structures of p63 DNA binding domain in complexes with half-site and with spacer-containing full response elements Proc. Natl Acad. Sci. USA 108 2011 6456 6461
    • (2011) Proc. Natl Acad. Sci. USA , vol.108 , pp. 6456-6461
    • Chen, C.1    Gorlatova, N.2    Kelman, Z.3    Herzberg, O.4
  • 39
    • 40549119464 scopus 로고    scopus 로고
    • The p73 DNA binding domain displays enhanced stability relative to its homologue, the tumor suppressor p53, and exhibits cooperative DNA binding
    • S. Patel, T.T. Bui, A.F. Drake, F. Fraternali, and P.V. Nikolova The p73 DNA binding domain displays enhanced stability relative to its homologue, the tumor suppressor p53, and exhibits cooperative DNA binding Biochemistry 47 2008 3235 3244
    • (2008) Biochemistry , vol.47 , pp. 3235-3244
    • Patel, S.1    Bui, T.T.2    Drake, A.F.3    Fraternali, F.4    Nikolova, P.V.5
  • 40
    • 38949123716 scopus 로고    scopus 로고
    • Biochemical and structural studies of ASPP proteins reveal differential binding to p53, p63, and p73
    • R.A. Robinson, X. Lu, E.Y. Jones, and C. Siebold Biochemical and structural studies of ASPP proteins reveal differential binding to p53, p63, and p73 Structure 16 2008 259 268
    • (2008) Structure , vol.16 , pp. 259-268
    • Robinson, R.A.1    Lu, X.2    Jones, E.Y.3    Siebold, C.4
  • 41
    • 33845959658 scopus 로고    scopus 로고
    • Effects of oncogenic mutations and DNA response elements on the binding of p53 to p53-binding protein 2 (53BP2)
    • H. Tidow, D.B. Veprintsev, S.M. Freund, and A.R. Fersht Effects of oncogenic mutations and DNA response elements on the binding of p53 to p53-binding protein 2 (53BP2) J. Biol. Chem. 281 2006 32526 32533
    • (2006) J. Biol. Chem. , vol.281 , pp. 32526-32533
    • Tidow, H.1    Veprintsev, D.B.2    Freund, S.M.3    Fersht, A.R.4
  • 42
    • 52649151797 scopus 로고    scopus 로고
    • Molecular interactions of ASPP1 and ASPP2 with the p53 protein family and the apoptotic promoters PUMA and Bax
    • S. Patel, R. George, F. Autore, F. Fraternali, J.E. Ladbury, and P.V. Nikolova Molecular interactions of ASPP1 and ASPP2 with the p53 protein family and the apoptotic promoters PUMA and Bax Nucleic Acids Res. 36 2008 5139 5151
    • (2008) Nucleic Acids Res. , vol.36 , pp. 5139-5151
    • Patel, S.1    George, R.2    Autore, F.3    Fraternali, F.4    Ladbury, J.E.5    Nikolova, P.V.6
  • 43
    • 67649405072 scopus 로고    scopus 로고
    • Insight into the structural basis of pro- and antiapoptotic p53 modulation by ASPP proteins
    • J. Ahn, I.J. Byeon, C.H. Byeon, and A.M. Gronenborn Insight into the structural basis of pro- and antiapoptotic p53 modulation by ASPP proteins J. Biol. Chem. 284 2009 13812 13822
    • (2009) J. Biol. Chem. , vol.284 , pp. 13812-13822
    • Ahn, J.1    Byeon, I.J.2    Byeon, C.H.3    Gronenborn, A.M.4
  • 44
    • 34548232365 scopus 로고    scopus 로고
    • Inference of macromolecular assemblies from crystalline state
    • E. Krissinel, and K. Henrick Inference of macromolecular assemblies from crystalline state J. Mol. Biol. 372 2007 774 797
    • (2007) J. Mol. Biol. , vol.372 , pp. 774-797
    • Krissinel, E.1    Henrick, K.2
  • 46
    • 33748250439 scopus 로고    scopus 로고
    • Crystal structure of SV40 large T-antigen bound to p53: Interplay between a viral oncoprotein and a cellular tumor suppressor
    • W. Lilyestrom, M.G. Klein, R. Zhang, A. Joachimiak, and X.S. Chen Crystal structure of SV40 large T-antigen bound to p53: interplay between a viral oncoprotein and a cellular tumor suppressor Genes Dev. 20 2006 2373 2382
    • (2006) Genes Dev. , vol.20 , pp. 2373-2382
    • Lilyestrom, W.1    Klein, M.G.2    Zhang, R.3    Joachimiak, A.4    Chen, X.S.5
  • 47
    • 0028103275 scopus 로고
    • The CCP4 suite: Programs for protein crystallography
    • Collaborative Computational Project Number 4
    • Collaborative Computational Project Number 4 The CCP4 suite: programs for protein crystallography Acta Crystallogr., Sect. D: Biol. Crystallogr. 50 1994 760 763
    • (1994) Acta Crystallogr., Sect. D: Biol. Crystallogr. , vol.50 , pp. 760-763
  • 48
    • 71649092785 scopus 로고    scopus 로고
    • Processing diffraction data with Mosflm
    • R.J. Read, J.L. Sussman, Springer-Verlag New York, NY
    • A.G.W. Leslie, and H.R. Powell Processing diffraction data with Mosflm R.J. Read, J.L. Sussman, Evolving Methods for Macromolecular Crystallography 2007 Springer-Verlag New York, NY 41 51
    • (2007) Evolving Methods for Macromolecular Crystallography , pp. 41-51
    • Leslie, A.G.W.1    Powell, H.R.2
  • 54
    • 33646260450 scopus 로고    scopus 로고
    • Optimal description of a protein structure in terms of multiple groups undergoing TLS motion
    • J. Painter, and E.A. Merritt Optimal description of a protein structure in terms of multiple groups undergoing TLS motion Acta Crystallogr., Sect. D: Biol. Crystallogr. 62 2006 439 450
    • (2006) Acta Crystallogr., Sect. D: Biol. Crystallogr. , vol.62 , pp. 439-450
    • Painter, J.1    Merritt, E.A.2
  • 56
    • 0030817618 scopus 로고    scopus 로고
    • Combining constraints for electron-density modification
    • K.Y. Zhang, K. Cowtan, and P. Main Combining constraints for electron-density modification Methods Enzymol. 277 1997 53 64
    • (1997) Methods Enzymol. , vol.277 , pp. 53-64
    • Zhang, K.Y.1    Cowtan, K.2    Main, P.3
  • 58
    • 33748337934 scopus 로고    scopus 로고
    • The Buccaneer software for automated model building. 1. Tracing protein chains
    • K. Cowtan The Buccaneer software for automated model building. 1. Tracing protein chains Acta Crystallogr., Sect. D: Biol. Crystallogr. 62 2006 1002 1011
    • (2006) Acta Crystallogr., Sect. D: Biol. Crystallogr. , vol.62 , pp. 1002-1011
    • Cowtan, K.1


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