UHRF2, a ubiquitin E3 ligase, acts as a small ubiquitin-like modifier E3 ligase for zinc finger protein 131

Journal of Biological Chemistry

Volumn 288, Issue 13, 2013, Pages 9102-9111

  Oh, Yohan ^a   Chung, Kwang Chul ^a  

^a Yonsei University   (South Korea)

Author keywords

[No Author keywords available]

Indexed keywords

ENZYMATIC ACTIVITIES; FUNCTIONAL PROPERTIES; NUCLEAR LOCALIZATION; REGULATORY MECHANISM; SMALL UBIQUITIN-LIKE MODIFIER E3 LIGASE; SMALL UBIQUITIN-LIKE MODIFIERS; UBIQUITIN-CONJUGATING ENZYMES; ZINC FINGER PROTEIN;

AMINO ACIDS; MAMMALS; PROTEINS; TRANSIENTS; ZINC;

ENZYMES;

NP95 ICBP90 LIKE RING FINGER PROTEIN; PROTEIN UBC9; UBIQUITIN PROTEIN LIGASE E3; UNCLASSIFIED DRUG; ZINC FINGER PROTEIN; ZINC FINGER PROTEIN 131;

ARTICLE; CONTROLLED STUDY; ENZYME ACTIVITY; NUCLEOTIDE SEQUENCE; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN FUNCTION; PROTEIN PROTEIN INTERACTION; STRUCTURE ACTIVITY RELATION; SUMOYLATION; UBIQUITINATION;

ANIMALS; CELL NUCLEUS; CERCOPITHECUS AETHIOPS; COS CELLS; DIMERIZATION; DNA; DNA-BINDING PROTEINS; HEK293 CELLS; HUMANS; LEUPEPTINS; MODELS, BIOLOGICAL; PROTEASOME ENDOPEPTIDASE COMPLEX; PROTEIN BINDING; PROTEIN PROCESSING, POST-TRANSLATIONAL; PROTEIN STRUCTURE, TERTIARY; RNA INTERFERENCE; TRANSCRIPTION FACTORS; UBIQUITIN; UBIQUITIN-PROTEIN LIGASES;

MAMMALIA;

EID: 84875986771     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M112.438234     Document Type: Article

References (45)

1. Wilkinson, K. A., and Henley, J. M. (2010) Mechanisms, regulation and consequences of protein SUMOylation. Biochem. J. 428, 133-145
2. Johnson, E. S., Schwienhorst, I., Dohmen, R. J., and Blobel, G. (1997) The ubiquitin-like protein Smt3p is activated for conjugation to other proteins by an Aos1p/Uba2p heterodimer. EMBO J. 16, 5509-5519
3. Desterro, J. M., Rodriguez, M. S., Kemp, G. D., and Hay, R. T. (1999) Identification of the enzyme required for activation of the small ubiquitinlike protein SUMO-1. J. Biol. Chem. 274, 10618-10624
4. Okuma, T., Honda, R., Ichikawa, G., Tsumagari, N., and Yasuda, H. (1999) In vitro SUMO-1 modification requires two enzymatic steps, E1 and E2. Biochem. Biophys. Res. Commun. 254, 693-698
5. Johnson, E. S., and Blobel, G. (1997) Ubc9p is the conjugating enzyme for the ubiquitin-like protein Smt3p. J. Biol. Chem. 272, 26799-26802
6. Desterro, J. M., Thomson, J., and Hay, R. T. (1997) Ubch9 conjugates SUMO but not ubiquitin. FEBS Lett. 417, 297-300
7. Gong, L., Kamitani, T., Fujise, K., Caskey, L. S., and Yeh, E. T. (1997) Preferential interaction of sentrin with a ubiquitin-conjugating enzyme, Ubc9. J. Biol. Chem. 272, 28198-28201
8. Rodriguez, M. S., Dargemont, C., and Hay, R. T. (2001) SUMO-1 conjugation in vivo requires both a consensus modification motif and nuclear targeting. J. Biol. Chem. 276, 12654-12659
9. Sampson, D. A., Wang, M., and Matunis, M. J. (2001) The small ubiquitin-like modifier-1 (SUMO-1) consensus sequence mediates Ubc9 binding and is essential for SUMO-1 modification. J. Biol. Chem. 276, 21664-21669
10. Sachdev, S., Bruhn, L., Sieber, H., Pichler, A., Melchior, F., and Grosschedl, R. (2001) PIASy, a nuclear matrix-associated SUMO E3 ligase, represses LEF1 activity by sequestration into nuclear bodies. Genes Dev. 15, 3088-3103
11. Kahyo, T., Nishida, T., and Yasuda, H. (2001) Involvement of PIAS1 in the sumoylation of tumor suppressor p53. Mol. Cell 8, 713-718
12. Schmidt, D., and Müller, S. (2002) Members of the PIAS family act as SUMOligases for c-Jun and p53 and repress p53 activity. Proc. Natl. Acad. Sci. U.S.A. 99, 2872-2877
13. Hochstrasser, M. (2001) SP-RING for SUMO: new functions bloom for a ubiquitin-like protein. Cell 107, 5-8
14. Pichler, A., Gast, A., Seeler, J. S., Dejean, A., and Melchior, F. (2002) The nucleoporin RanBP2 has SUMO1 E3 ligase activity. Cell 108, 109-120
15. Kirsh, O., Seeler, J. S., Pichler, A., Gast, A., Müller, S., Miska, E., Mathieu, M., Harel-Bellan, A., Kouzarides, T., Melchior, F., and Dejean, A. (2002) The SUMO E3 ligase RanBP2 promotes modification of the HDAC4 deacetylase. EMBO J. 21, 2682-2691
16. Kagey, M. H., Melhuish, T. A., and Wotton, D. (2003) The polycomb protein Pc2 is a SUMO E3. Cell 113, 127-137
17. Wotton, D., and Merrill, J. C. (2007) Pc2 and SUMOylation. Biochem. Soc. Trans. 35, 1401-1404
18. Merrill, J. C., Melhuish, T. A., Kagey, M. H., Yang, S. H., Sharrocks, A. D., and Wotton, D. (2010) A role for non-covalent SUMO interaction motifs in Pc2/CBX4 E3 activity. PLoS ONE 5, e8794
19. Zhao, X., Sternsdorf, T., Bolger, T. A., Evans, R. M., and Yao, T. P. (2005) Regulation of MEF2 by histone deacetylase 4- and SIRT1 deacetylase-mediated lysine modifications. Mol. Cell Biol. 25, 8456-8464
20. Weger, S., Hammer, E., and Heilbronn, R. (2005) Topors acts as a SUMO-1 E3 ligase for p53 in vitro and in vivo. FEBS Lett. 579, 5007-5012
21. Morita, Y., Kanei-Ishii, C., Nomura, T., and Ishii, S. (2005) TRAF7 sequesters c-Myb to the cytoplasm by stimulating its sumoylation. Mol. Biol. Cell 16, 5433-5444
22. Chu, Y., and Yang, X. (2011) SUMO E3 ligase activity of TRIM proteins. Oncogene 30, 1108-1116
23. Ulrich, H. D. (2005) Mutual interactions between the SUMO and ubiquitin systems: a plea of no contest. Trends Cell Biol. 15, 525-532
24. Mori, T., Li, Y., Hata, H., Ono, K., and Kochi, H. (2002) NIRF, a novel RING finger protein, is involved in cell-cycle regulation. Biochem. Biophys. Res. Commun. 296, 530-536
25. Iwata, A., Nagashima, Y., Matsumoto, L., Suzuki, T., Yamanaka, T., Date, H., Deoka, K., Nukina, N., and Tsuji, S. (2009) Intranuclear degradation of polyglutamine aggregates by the ubiquitin-proteasome system. J. Biol. Chem. 284, 9796-9803
26. Li, Y., Mori, T., Hata, H., Homma, Y., and Kochi, H. (2004) NIRF induces G1 arrest and associates with Cdk2. Biochem. Biophys. Res. Commun. 319, 464-468
27. Mori, T., Ikeda, D. D., Fukushima, T., Takenoshita, S., and Kochi, H. (2011) NIRF constitutes a nodal point in the cell cycle network and is a candidate tumor suppressor. Cell Cycle 10, 3284-3299
28. Mori, T., Li, Y., Hata, H., and Kochi, H. (2004) NIRF is a ubiquitin ligase that is capable of ubiquitinating PCNP, a PEST-containing nuclear protein. FEBS Lett. 557, 209-214
29. Bai, L., Wang, X., Jin, F., Yang, Y., Qian, G., and Duan, C. (2012) UHRF2, another E3 ubiquitin ligase for p53. Biochem. Biophys. Res. Commun. 425, 908-911
30. Oh, Y., and Chung, K. C. (2012) Small ubiquitin-like modifier (SUMO) modification of zinc finger protein 131 potentiates its negative effect on estrogen signaling. J. Biol. Chem. 287, 17517-17529
31. Donaldson, N. S., Daniel, Y., Kelly, K. F., Graham, M., and Daniel, J. M. (2007) Nuclear trafficking of the POZ-ZF protein Znf131. Biochim. Biophys. Acta 1773, 546-555
32. Gareau, J. R., and Lima, C. D. (2010) The SUMO pathway: emerging mechanisms that shape specificity, conjugation and recognition. Nat. Rev. Mol. Cell Biol. 11, 861-871
33. Rajendra, R., Malegaonkar, D., Pungaliya, P., Marshall, H., Rasheed, Z., Brownell, J., Liu, L. F., Lutzker, S., Saleem, A., and Rubin, E. H. (2004) Topors functions as an E3 ubiquitin ligase with specific E2 enzymes and ubiquitinates p53. J. Biol. Chem. 279, 36440-36444
34. Bouwmeester, T., Bauch, A., Ruffner, H., Angrand, P. O., Bergamini, G., Croughton, K., Cruciat, C., Eberhard, D., Gagneur, J., Ghidelli, S., Hopf, C., Huhse, B., Mangano, R., Michon, A. M., Schirle, M., Schlegl, J., Schwab, M., Stein, M. A., Bauer, A., Casari, G., Drewes, G., Gavin, A. C., Jackson, D. B., Joberty, G., Neubauer, G., Rick, J., Kuster, B., and Superti-Furga, G. (2004) A physical and functional map of the human TNF-α/NF-κB signal transduction pathway. Nat. Cell Biol. 6, 97-105
35. Ihara, M., Yamamoto, H., and Kikuchi, A. (2005) SUMO-1 modification of PIASy, an E3 ligase, is necessary for PIASy-dependent activation of Tcf-4. Mol. Cell Biol. 25, 3506-3518
36. Ivanov, A. V., Peng, H., Yurchenko, V., Yap, K. L., Negorev, D. G., Schultz, D. C., Psulkowski, E., Fredericks, W. J., White, D. E., Maul, G. G., Sadofsky, M. J., Zhou, M. M., and Rauscher, F. J., 3rd. (2007) PHD domain-mediated E3 ligase activity directs intramolecular sumoylation of an adjacent bromodomain required for gene silencing. Mol. Cell 28, 823-837
37. Bronner, C., Achour, M., Arima, Y., Chataigneau, T., Saya, H., and Schini- Kerth, V. B. (2007) The UHRF family: oncogenes that are drugable targets for cancer therapy in the near future? Pharmacol. Ther. 115, 419-434
38. Zhang, J., Gao, Q., Li, P., Liu, X., Jia, Y., Wu, W., Li, J., Dong, S., Koseki, H., and Wong, J. (2011) S phase-dependent interaction with DNMT1 dictates the role of UHRF1 but not UHRF2 inDNAmethylation maintenance. Cell Res. 21, 1723-1739
39. Mori, T., Ikeda, D. D., Yamaguchi, Y., and Unoki, M. (2012) NIRF/UHRF2 occupies a central position in the cell cycle network and allows coupling with the epigenetic landscape. FEBS Lett. 586, 1570-1583
40. Gao, C., Ho, C. C., Reineke, E., Lam, M., Cheng, X., Stanya, K. J., Liu, Y., Chakraborty, S., Shih, H. M., and Kao, H. Y. (2008) Histone deacetylase 7 promotes PML sumoylation and is essential for PML nuclear body formation. Mol. Cell Biol. 28, 5658-5667
41. Tommerup, N., and Vissing, H. (1995) Isolation and fine mapping of 16 novel human zinc finger-encoding cDNAs identify putative candidate genes for developmental and malignant disorders. Genomics 27, 259-264
42. Han, X., Guo, J., Deng, W., Zhang, C., Du, P., Shi, T., and Ma, D. (2008) High-throughput cell-based screening reveals a role for ZNF131 as a repressor of ERα signaling. BMC Genomics 9, 476
43. Oh, Y., and Chung, K. C. (2013) Zinc finger protein 131 inhibits estrogen signaling by suppressing estrogen receptor α homo-dimerization. Biochem. Biophys. Res. Commun. 430, 400-405
44. Wu, J., Liu, S., Liu, G., Dombkowski, A., Abrams, J., Martin-Trevino, R., Wicha, M. S., Ethier, S. P., and Yang, Z. Q. (2012) Identification and functional analysis of 9p24 amplified genes in human breast cancer. Oncogene 31, 333-341
45. Donaldson, N. S., Nordgaard, C. L., Pierre, C. C., Kelly, K. F., Robinson, S. C., Swystun, L., Henriquez, R., Graham, M., and Daniel, J. M. (2010) Kaiso regulates Znf131-mediated transcriptional activation. Exp. Cell Res. 316, 1692-1705