| Structural highlights
Function
[RNF4_RAT] E3 ubiquitin-protein ligase which binds polysumoylated chains covalently attached to proteins and mediates 'Lys-6'-, 'Lys-11'-, 'Lys-48'- and 'Lys-63'-linked polyubiquitination of those substrates and their subsequent targeting to the proteasome for degradation. Regulates the degradation of several proteins including PML and the transcriptional activator PEA3. Involved in chromosome alignment and spindle assembly, it regulates the kinetochore CENPH-CENPI-CENPK complex by targeting polysumoylated CENPI to proteasomal degradation. Regulates the cellular responses to hypoxia and heat shock through degradation of respectively EPAS1 and PARP1. Alternatively, it may also bind DNA/nucleosomes and have a more direct role in the regulation of transcription for instance enhancing basal transcription and steroid receptor-mediated transcriptional activation.[1] [2] [3] [4] [5] [6]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
RNF4 [RING (really interesting new gene) finger protein 4] family ubiquitin ligases are RING E3 ligases that regulate the homoeostasis of SUMOylated proteins by promoting their ubiquitylation. In the present paper we report that the RING domain of RNF4 forms a stable dimer, and that dimerization is required for ubiquitin transfer. Our results suggest that the stability of the E2~ubiquitin thioester bond is regulated by RING domain dimerization.
RING domain dimerization is essential for RNF4 function.,Liew CW, Sun H, Hunter T, Day CL Biochem J. 2010 Oct 1;431(1):23-9. PMID:20681948[7]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Moilanen AM, Poukka H, Karvonen U, Hakli M, Janne OA, Palvimo JJ. Identification of a novel RING finger protein as a coregulator in steroid receptor-mediated gene transcription. Mol Cell Biol. 1998 Sep;18(9):5128-39. PMID:9710597
- ↑ Hakli M, Karvonen U, Janne OA, Palvimo JJ. The RING finger protein SNURF is a bifunctional protein possessing DNA binding activity. J Biol Chem. 2001 Jun 29;276(26):23653-60. Epub 2001 Apr 23. PMID:11319220 doi:10.1074/jbc.M009891200
- ↑ Hakli M, Lorick KL, Weissman AM, Janne OA, Palvimo JJ. Transcriptional coregulator SNURF (RNF4) possesses ubiquitin E3 ligase activity. FEBS Lett. 2004 Feb 27;560(1-3):56-62. PMID:14987998 doi:10.1016/S0014-5793(04)00070-5
- ↑ Hakli M, Karvonen U, Janne OA, Palvimo JJ. SUMO-1 promotes association of SNURF (RNF4) with PML nuclear bodies. Exp Cell Res. 2005 Mar 10;304(1):224-33. Epub 2004 Nov 23. PMID:15707587 doi:10.1016/j.yexcr.2004.10.029
- ↑ Tatham MH, Geoffroy MC, Shen L, Plechanovova A, Hattersley N, Jaffray EG, Palvimo JJ, Hay RT. RNF4 is a poly-SUMO-specific E3 ubiquitin ligase required for arsenic-induced PML degradation. Nat Cell Biol. 2008 May;10(5):538-46. doi: 10.1038/ncb1716. Epub 2008 Apr 13. PMID:18408734 doi:10.1038/ncb1716
- ↑ Geoffroy MC, Jaffray EG, Walker KJ, Hay RT. Arsenic-induced SUMO-dependent recruitment of RNF4 into PML nuclear bodies. Mol Biol Cell. 2010 Dec;21(23):4227-39. doi: 10.1091/mbc.E10-05-0449. Epub 2010, Oct 13. PMID:20943951 doi:10.1091/mbc.E10-05-0449
- ↑ Liew CW, Sun H, Hunter T, Day CL. RING domain dimerization is essential for RNF4 function. Biochem J. 2010 Oct 1;431(1):23-9. PMID:20681948 doi:10.1042/BJ20100957
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