The evolution of MDM2 family genes

Gene

Volumn 486, Issue 1-2, 2011, Pages 23-30

  Momand, Jamil ^a   Villegas, Alberto ^a   Belyi, Vladimir A ^b,c  

^a CALIFORNIA STATE UNIVERSITY   (United States)

^b INSTITUTE FOR ADVANCED STUDY   (United States)

^c RUTGERS CANCER INSTITUTE OF NEW JERSEY   (United States)

Author keywords

Cancer; MDM; MDM2; MDM4; MDMX; P53

Indexed keywords

MDM PROTEIN; ONCOPROTEIN; PROTEIN MDM2; PROTEIN MDMX; PROTEIN P53; PROTEIN P63; PROTEIN P73; RING FINGER PROTEIN; UNCLASSIFIED DRUG;

ANIMAL EXPERIMENT; ARTICLE; COMPARATIVE GENE MAPPING; CONTROLLED STUDY; DIMERIZATION; FISH; GENE DUPLICATION; GENE EXPRESSION; GENE SEQUENCE; GENETIC CONSERVATION; HETERODIMERIZATION; INVERTEBRATE; NONHUMAN; NUCLEOTIDE SEQUENCE; OLIGOMERIZATION; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN DOMAIN; PROTEIN FUNCTION; UBIQUITINATION; VERTEBRATE;

ANIMALS; CONSERVED SEQUENCE; EVOLUTION, MOLECULAR; GENE DUPLICATION; GENES, P53; GENETIC VARIATION; HUMANS; INVERTEBRATES; MULTIGENE FAMILY; NUCLEAR PROTEINS; PROTEIN STRUCTURE, TERTIARY; PROTO-ONCOGENE PROTEINS; PROTO-ONCOGENE PROTEINS C-MDM2; PROTO-ONCOGENES; TIME FACTORS; VERTEBRATES;

CHONDRICHTHYES; EUTELEOSTOMI; GNATHOSTOMATA (VERTEBRATE); INVERTEBRATA; MAMMALIA;

EID: 84860390380     PISSN: 03781119     EISSN: 18790038     Source Type: Journal    
DOI: 10.1016/j.gene.2011.06.030     Document Type: Article

References (70)

1. Altschul S.F., et al. Gapped BLAST and PSI-BLAST: a new generation of protein database search programs. Nucleic Acids Res. 1997, 25:3389-3402.
2. Araki S., et al. TGF-beta1-induced expression of human MDM2 correlates with late-stage metastatic breast cancer. J. Clin. Invest. 2010, 120:290-302.
3. Balint E., Reisman D. Increased rate of transcription contributes to elevated expression of the mutant p53 gene in Burkitt's lymphoma cells. Cancer Res. 1996, 56:1648-1653.
4. Belyi V.A., et al. The origins and evolution of the p53 family of genes. Cold Spring Harb. Perspect. Biol. 2010, 2:a001198.
5. Bergamaschi D., et al. iASPP oncoprotein is a key inhibitor of p53 conserved from worm to human. Nat. Genet. 2003, 33:162-167.
6. Bond G.L., et al. MDM2 SNP309 accelerates tumor formation in a gender-specific and hormone-dependent manner. Cancer Res. 2006, 66:5104-5110.
7. Brandt T., Petrovich M., Joerger A.C., Veprintsev D.B. Conservation of DNA-binding specificity and oligomerisation properties within the p53 family. BMC Genomics 2009, 10:628.
8. Cahilly-Snyder L., Yang-Feng T., Francke U., George D.L. Molecular analysis and chromosomal mapping of amplified genes isolated from a transformed mouse 3T3 cell line. Somat. Cell Mol. Genet. 1987, 13:235-244.
9. Calabro V., et al. The human MDM2 oncoprotein increases the transcriptional activity and the protein level of the p53 homolog p63. J. Biol. Chem. 2002, 277:2674-2681.
10. Dawkins R. The Ancestor's Tale: A Pilgrimage to the Dawn of Evolution 2004, Houghton Mifflin, New York.
11. Derry W.B., Putzke A.P., Rothman J.H. Caenorhabditis elegans p53: role in apoptosis, meiosis, and stress resistance. Science 2001, 294:591-595.
12. Eitel M., Guidi L., Hadrys H., Balsamo M., Schierwater B. New insights into placozoan sexual reproduction and development. PLoS One 2011, 6:e19639.
13. el-Deiry W.S., et al. WAF1, a potential mediator of p53 tumor suppression. Cell 1993, 75:817-825.
14. Fakharzadeh S.S., Trusko S.P., George D.L. Tumorigenic potential associated with enhanced expression of a gene that is amplified in a mouse tumor cell line. EMBO J. 1991, 10:1565-1569.
15. 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. 2000, 275:8945-8951.
16. Flicek P., et al. Ensembl 2011. Nucleic Acids Res. 2011, 39:D800-D806.
17. Glazko G.V., Nei M. Estimation of divergence times for major lineages of primate species. Mol. Biol. Evol. 2003, 20:424-434.
18. Haupt Y., Maya R., Kazaz A., Oren M. MDM2 promotes the rapid degradation of p53. Nature 1997, 387:296-299.
19. Hock A., Vousden K.H. Regulation of the p53 pathway by ubiquitin and related proteins. Int. J. Biochem. Cell Biol. 2010, 42:1618-1621.
20. Honda R., Tanaka H., Yasuda H. Oncoprotein MDM2 is a ubiquitin ligase E3 for tumor suppressor p53. FEBS Lett. 1997, 420:25-27.
21. Hubbard T.J., et al. Ensembl 2009. Nucleic Acids Res. 2009, 37:D690-D697.
22. Hunter S., et al. InterPro: the integrative protein signature database. Nucleic Acids Res. 2009, 37:D211-D215.
23. Jackson M.W., Lindstrom M.S., Berberich S.J. MdmX binding to ARF affects MDM2 protein stability and p53 transactivation. J. Biol. Chem. 2001, 276:25336-25341.
24. Jin S., et al. Identification and characterization of a p53 homologue in Drosophila melanogaster. Proc. Natl. Acad. Sci. U.S.A. 2000, 97:7301-7306.
25. Kadakia M., Slader C., Berberich S.J. Regulation of p63 function by MDM2 and MdmX. DNA Cell Biol. 2001, 20:321-330.
26. Kallen J., et al. Crystal structures of human MdmX (HdmX) in complex with p53 peptide analogues reveal surprising conformational changes. J. Biol. Chem. 2009, 284:8812-8821.
27. King N., et al. The genome of the choanoflagellate Monosiga brevicollis and the origin of metazoans. Nature 2008, 451:783-788.
28. Kojima T., Ikawa Y., Katoh I. Analysis of molecular interactions of the p53-family p51(p63) gene products in a yeast two-hybrid system: homotypic and heterotypic interactions and association with p53-regulatory factors. Biochem. Biophys. Res. Commun. 2001, 281:1170-1175.
29. Kostic M., Matt T., Martinez-Yamout M.A., Dyson H.J., Wright P.E. Solution structure of the Hdm2 C2H2C4 RING, a domain critical for ubiquitination of p53. J. Mol. Biol. 2006, 363:433-450.
30. Kubbutat M.H., Jones S.N., Vousden K.H. Regulation of p53 stability by MDM2. Nature 1997, 387:299-303.
31. Kussie P.H., et al. Structure of the MDM2 oncoprotein bound to the p53 tumor suppressor transactivation domain. Science 1996, 274:948-953.
32. Lane D.P., et al. MDM2 and p53 are highly conserved from placozoans to man. Cell Cycle 2010, 9:540-547.
33. Lane D.P., et al. The MDM2 and p53 genes are conserved in the Arachnids. Cell Cycle 2010, 9:748-754.
34. Larkin M.A., et al. Clustal W and Clustal X version 2.0. Bioinformatics 2007, 23:2947-2948.
35. Laurie N.A., et al. Inactivation of the p53 pathway in retinoblastoma. Nature 2006, 444:61-66.
36. Li M., et al. Mono- versus polyubiquitination: differential control of p53 fate by MDM2. Science 2003, 302:1972-1975.
37. Liang M., et al. HDM4 is overexpressed in mantle cell lymphoma and its inhibition induces p21 expression and apoptosis. Mod. Pathol. 2010, 23:381-391.
38. Linares L.K., Hengstermann A., Ciechanover A., Muller S., Scheffner M. HdmX stimulates Hdm2-mediated ubiquitination and degradation of p53. Proc. Natl. Acad. Sci. U.S.A. 2003, 100:12009-12014.
39. Linke K., et al. Structure of the MDM2/MDMX RING domain heterodimer reveals dimerization is required for their ubiquitylation in trans. Cell Death Differ. 2008, 15:841-848.
40. Little N.A., Jochemsen A.G. Hdmx and MDM2 can repress transcription activation by p53 but not by p63. Oncogene 2001, 20:4576-4580.
41. Margoliash E. Primary structure and evolution of Cytochrome C. Proc. Natl. Acad. Sci. U.S.A. 1963, 50:672-679.
42. Mavinahalli J.N., Madhumalar A., Beuerman R.W., Lane D.P., Verma C. Differences in the transactivation domains of p53 family members: a computational study. BMC Genomics 2010, 11(Suppl 1):S5.
43. Miller D.J., Ball E.E. Animal evolution: the enigmatic phylum placozoa revisited. Curr. Biol. 2005, 15:R26-R28.
44. Miller W., et al. 28-way vertebrate alignment and conservation track in the UCSC Genome Browser. Genome Res. 2007, 17:1797-1808.
45. Momand J., Zambetti G.P., Olson D.C., George D., Levine A.J. The MDM-2 oncogene product forms a complex with the p53 protein and inhibits p53-mediated transactivation. Cell 1992, 69:1237-1245.
46. Momand J., Jung D., Wilczynski S., Niland J. The MDM2 gene amplification database. Nucleic Acids Res. 1998, 26:3453-3459.
47. Murphy W.J., Pringle T.H., Crider T.A., Springer M.S., Miller W. Using genomic data to unravel the root of the placental mammal phylogeny. Genome Res. 2007, 17:413-421.
48. Muttray A.F., O'Toole T.F., Morrill W., Van Beneden R.J., Baldwin S.A. An invertebrate mdm homolog interacts with p53 and is differentially expressed together with p53 and ras in neoplastic Mytilus trossulus haemocytes. Comp. Biochem. Physiol. B Biochem. Mol. Biol. 2010, 156:298-308.
49. Nedelcu A.M., Tan C. Early diversification and complex evolutionary history of the p53 tumor suppressor gene family. Dev. Genes Evol. 2007, 217:801-806.
50. Needleman S.B., Wunsch C.D. A general method applicable to the search for similarities in amino acid sequence of two proteins. J. Mol. Biol. 1970, 48:443-453.
51. Oliner J.D., Kinzler K.W., Meltzer P.S., George D.L., Vogelstein B. Amplification of a gene encoding a p53-associated protein in human sarcomas. Nature 1992, 358:80-83.
52. Pazos F., Valencia A. Protein co-evolution, co-adaptation and interactions. EMBO J. 2008, 27:2648-2655.
53. Popowicz G.M., et al. Molecular basis for the inhibition of p53 by Mdmx. Cell Cycle 2007, 6:2386-2392.
54. Prasad A.B., Allard M.W., Green E.D. Confirming the phylogeny of mammals by use of large comparative sequence data sets. Mol. Biol. Evol. 2008, 25:1795-1808.
55. Putnam N.H., et al. The amphioxus genome and the evolution of the chordate karyotype. Nature 2008, 453:1064-1071.
56. Rice P., Longden I., Bleasby A. EMBOSS: the European Molecular Biology Open Software Suite. Trends Genet. 2000, 16:276-277.
57. Rutkowski R., Hofmann K., Gartner A. Phylogeny and function of the invertebrate p53 superfamily. Cold Spring Harb. Perspect. Biol. 2010, 2:a001131.
58. Shvarts A., et al. MDMX: a novel p53-binding protein with some functional properties of MDM2. EMBO J. 1996, 15:5349-5357.
59. Singh R.K., Iyappan S., Scheffner M. Hetero-oligomerization with MdmX rescues the ubiquitin/Nedd8 ligase activity of RING finger mutants of MDM2. J. Biol. Chem. 2007, 282:10901-10907.
60. Srivastava M., et al. The Trichoplax genome and the nature of placozoans. Nature 2008, 454:955-960.
61. Tanimura S., et al. MDM2 interacts with MDMX through their RING finger domains. FEBS Lett. 1999, 447:5-9.
62. Toledo F., Wahl G.M. Regulating the p53 pathway: in vitro hypotheses, in vivo veritas. Nat. Rev. Cancer 2006, 6:909-923.
63. Uldrijan S., Pannekoek W.J., Vousden K.H. An essential function of the extreme C-terminus of MDM2 can be provided by MDMX. EMBO J. 2007, 26:102-112.
64. Wade M., Wang Y.V., Wahl G.M. The p53 orchestra: MDM2 and Mdmx set the tone. Trends Cell Biol. 2010, 20:299-309.
65. Wang X., et al. MDM2 and MDMX can interact differently with ARF and members of the p53 family. FEBS Lett. 2001, 490:202-208.
66. Weber J.D., Taylor L.J., Roussel M.F., Sherr C.J., Bar-Sagi D. Nucleolar Arf sequesters MDM2 and activates p53. Nat. Cell Biol. 1999, 1:20-26.
67. Yu G.W., Allen M.D., Andreeva A., Fersht A.R., Bycroft M. Solution structure of the C4 zinc finger domain of HDM2. Protein Sci. 2006, 15:384-389.
68. Zdzalik M., et al. Interaction of regulators MDM2 and Mdmx with transcription factors p53, p63 and p73. Cell Cycle 2010, 9:4584-4591.
69. Zeng X., et al. MDM2 suppresses p73 function without promoting p73 degradation. Mol. Cell. Biol. 1999, 19:3257-3266.
70. Zuckerkandl E., Pauling L.B. Molecular disease, evolution, and genetic heterogeneity. Horizons in Biochemistry 1962, 189-225. Academic Press, New York. M. Kasha, B. Pullman (Eds.).