| Structural highlights
Function
SIZ1_ARATH E3 SUMO protein ligase involved in regulation processes. Mediates SUMO/ attachment to PHR1, a MYB transcriptional activator controlling the phosphate deficiency responses. Functions as an upstream negative regulator of salicylic acid (SA) accumulation and subsequent SA-mediated systemic acquired resistance (SAR) signaling. Probably not involved in jasmonic acid (JA)-mediated defense response. Participates in abiotic stress-induced sumoylation. Controls heat shock-induced SUMO1 and SUMO2 conjugation and facilitates basal thermotolerance. Involved in freezing tolerance by mediating sumoylation of ICE1, a transcription activator of the cold signaling regulator CBF3/DREB1A. Acts as positive regulator of drought stress tolerance. Acts as floral repressor that promotes FLC expression by repressing FLD activity through sumoylation. Acts as negative regulator of abscisic acid (ABA) signaling through ABI5 sumoylation. Mediates sumoylation of SCE1, GTE3 and GTE5.[1] [2] [3] [4] [5] [6] [7] [8] [9]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
References
- ↑ Miura K, Rus A, Sharkhuu A, Yokoi S, Karthikeyan AS, Raghothama KG, Baek D, Koo YD, Jin JB, Bressan RA, Yun DJ, Hasegawa PM. The Arabidopsis SUMO E3 ligase SIZ1 controls phosphate deficiency responses. Proc Natl Acad Sci U S A. 2005 May 24;102(21):7760-5. Epub 2005 May 13. PMID:15894620 doi:http://dx.doi.org/0500778102
- ↑ Yoo CY, Miura K, Jin JB, Lee J, Park HC, Salt DE, Yun DJ, Bressan RA, Hasegawa PM. SIZ1 small ubiquitin-like modifier E3 ligase facilitates basal thermotolerance in Arabidopsis independent of salicylic acid. Plant Physiol. 2006 Dec;142(4):1548-58. Epub 2006 Oct 13. PMID:17041025 doi:http://dx.doi.org/10.1104/pp.106.088831
- ↑ Miura K, Jin JB, Lee J, Yoo CY, Stirm V, Miura T, Ashworth EN, Bressan RA, Yun DJ, Hasegawa PM. SIZ1-mediated sumoylation of ICE1 controls CBF3/DREB1A expression and freezing tolerance in Arabidopsis. Plant Cell. 2007 Apr;19(4):1403-14. Epub 2007 Apr 6. PMID:17416732 doi:http://dx.doi.org/10.1105/tpc.106.048397
- ↑ Catala R, Ouyang J, Abreu IA, Hu Y, Seo H, Zhang X, Chua NH. The Arabidopsis E3 SUMO ligase SIZ1 regulates plant growth and drought responses. Plant Cell. 2007 Sep;19(9):2952-66. Epub 2007 Sep 28. PMID:17905899 doi:http://dx.doi.org/10.1105/tpc.106.049981
- ↑ Lee J, Nam J, Park HC, Na G, Miura K, Jin JB, Yoo CY, Baek D, Kim DH, Jeong JC, Kim D, Lee SY, Salt DE, Mengiste T, Gong Q, Ma S, Bohnert HJ, Kwak SS, Bressan RA, Hasegawa PM, Yun DJ. Salicylic acid-mediated innate immunity in Arabidopsis is regulated by SIZ1 SUMO E3 ligase. Plant J. 2007 Jan;49(1):79-90. Epub 2006 Dec 6. PMID:17163880 doi:http://dx.doi.org/10.1111/j.1365-313X.2006.02947.x
- ↑ Saracco SA, Miller MJ, Kurepa J, Vierstra RD. Genetic analysis of SUMOylation in Arabidopsis: conjugation of SUMO1 and SUMO2 to nuclear proteins is essential. Plant Physiol. 2007 Sep;145(1):119-34. Epub 2007 Jul 20. PMID:17644626 doi:http://dx.doi.org/10.1104/pp.107.102285
- ↑ Garcia-Dominguez M, March-Diaz R, Reyes JC. The PHD domain of plant PIAS proteins mediates sumoylation of bromodomain GTE proteins. J Biol Chem. 2008 Aug 1;283(31):21469-77. doi: 10.1074/jbc.M708176200. Epub 2008 , May 23. PMID:18502747 doi:http://dx.doi.org/10.1074/jbc.M708176200
- ↑ Jin JB, Jin YH, Lee J, Miura K, Yoo CY, Kim WY, Van Oosten M, Hyun Y, Somers DE, Lee I, Yun DJ, Bressan RA, Hasegawa PM. The SUMO E3 ligase, AtSIZ1, regulates flowering by controlling a salicylic acid-mediated floral promotion pathway and through affects on FLC chromatin structure. Plant J. 2008 Feb;53(3):530-40. Epub 2007 Dec 6. PMID:18069938 doi:http://dx.doi.org/10.1111/j.1365-313X.2007.03359.x
- ↑ Miura K, Lee J, Jin JB, Yoo CY, Miura T, Hasegawa PM. Sumoylation of ABI5 by the Arabidopsis SUMO E3 ligase SIZ1 negatively regulates abscisic acid signaling. Proc Natl Acad Sci U S A. 2009 Mar 31;106(13):5418-23. doi:, 10.1073/pnas.0811088106. Epub 2009 Mar 10. PMID:19276109 doi:http://dx.doi.org/10.1073/pnas.0811088106
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