Log in

Relevant bibliographies by topics / Sumo E3 Ligase / Journal articles

To see the other types of publications on this topic, follow the link: Sumo E3 Ligase.

Journal articles on the topic 'Sumo E3 Ligase'

Author: Grafiati

Published: 4 June 2021

Last updated: 7 September 2023

Create a spot-on reference in APA, MLA, Chicago, Harvard, and other styles

Select a source type:

Consult the top 50 journal articles for your research on the topic 'Sumo E3 Ligase.'

Next to every source in the list of references, there is an 'Add to bibliography' button. Press on it, and we will generate automatically the bibliographic reference to the chosen work in the citation style you need: APA, MLA, Harvard, Chicago, Vancouver, etc.

You can also download the full text of the academic publication as pdf and read online its abstract whenever available in the metadata.

Browse journal articles on a wide variety of disciplines and organise your bibliography correctly.

1

Huang, Wei, Yaling Liang, Jianhua Dong та ін. "SUMO E3 Ligase PIASy Mediates High Glucose-Induced Activation of NF-κB Inflammatory Signaling in Rat Mesangial Cells". Mediators of Inflammation 2017 (2017): 1–9. http://dx.doi.org/10.1155/2017/1685194.

Full text

Abstract:

Background. Sumoylation is extensively involved in the regulation of NF-κB signaling. PIASy, as a SUMO E3 ligase, has been proved to mediate sumoylation of IκB kinase γ (IKKγ) and contribute to the activation of NF-κB under genotoxic agent stimulation. However, the association of PIASy and NF-κB signaling in the pathogenesis of diabetic nephropathy (DN) has not been defined. Methods. Rat glomerular mesangial cells (GMCs) were stimulated by high glucose; siRNA was constructed to silence the expression of PIASy; the expression of PIASy, SUMO isoforms (SUMO1, SUMO2/3), and NF-κB signaling compone

APA, Harvard, Vancouver, ISO, and other styles

2

Li, Min, Xiaohua Xu, Chou-Wei Chang, and Yilun Liu. "TRIM28 functions as the SUMO E3 ligase for PCNA in prevention of transcription induced DNA breaks." Proceedings of the National Academy of Sciences 117, no. 38 (2020): 23588–96. http://dx.doi.org/10.1073/pnas.2004122117.

Full text

Abstract:

In human cells, the DNA replication factor proliferating cell nuclear antigen (PCNA) can be conjugated to either the small ubiquitinlike modifier SUMO1 or SUMO2, but only SUMO2-conjugated PCNA is induced by transcription to facilitate resolution of transcription–replication conflict (TRC). To date, the SUMO E3 ligase that provides substrate specificity for SUMO2-PCNA conjugation in response to TRC remains unknown. Using a proteomic approach, we identified TRIM28 as the E3 ligase that catalyzes SUMO2-PCNA conjugation. In vitro, TRIM28, together with the RNA polymerase II (RNAPII)-interacting pr

APA, Harvard, Vancouver, ISO, and other styles

3

Wang, Weibin, Yifan Chen, Shuya Wang та ін. "PIASxα Ligase Enhances SUMO1 Modification of PTEN Protein as a SUMO E3 Ligase". Journal of Biological Chemistry 289, № 6 (2013): 3217–30. http://dx.doi.org/10.1074/jbc.m113.508515.

Full text

APA, Harvard, Vancouver, ISO, and other styles

4

Chu, Y., and X. Yang. "SUMO E3 ligase activity of TRIM proteins." Oncogene 30, no. 9 (2010): 1108–16. http://dx.doi.org/10.1038/onc.2010.462.

Full text

APA, Harvard, Vancouver, ISO, and other styles

5

Lear, Travis, Alison C. McKelvey, Shristi Rajbhandari, et al. "Ubiquitin E3 ligase FIEL1 regulates fibrotic lung injury through SUMO-E3 ligase PIAS4." Journal of Experimental Medicine 213, no. 6 (2016): 1029–46. http://dx.doi.org/10.1084/jem.20151229.

Full text

Abstract:

The E3 small ubiquitin-like modifier (SUMO) protein ligase protein inhibitor of activated STAT 4 (PIAS4) is a pivotal protein in regulating the TGFβ pathway. In this study, we discovered a new protein isoform encoded by KIAA0317, termed fibrosis-inducing E3 ligase 1 (FIEL1), which potently stimulates the TGFβ signaling pathway through the site-specific ubiquitination of PIAS4. FIEL1 targets PIAS4 using a double locking mechanism that is facilitated by the kinases PKCζ and GSK3β. Specifically, PKCζ phosphorylation of PIAS4 and GSK3β phosphorylation of FIEL1 are both essential for the degradatio

APA, Harvard, Vancouver, ISO, and other styles

6

Lear, Travis, Alison McKelvey, Shristi Rajbhandari, et al. "Ubiquitin E3 ligase FIEL1 regulates fibrotic lung injury through SUMO-E3 ligase PIAS4." Journal of Cell Biology 213, no. 4 (2016): 2134OIA108. http://dx.doi.org/10.1083/jcb.2134oia108.

Full text

APA, Harvard, Vancouver, ISO, and other styles

7

Gao, Sujuan, Xueqin Zeng, Jianhao Wang, et al. "Arabidopsis SUMO E3 Ligase SIZ1 Interacts with HDA6 and Negatively Regulates HDA6 Function during Flowering." Cells 10, no. 11 (2021): 3001. http://dx.doi.org/10.3390/cells10113001.

Full text

Abstract:

The changes in histone acetylation mediated by histone deacetylases (HDAC) play a crucial role in plant development and response to environmental changes. Mammalian HDACs are regulated by post-translational modifications (PTM), such as phosphorylation, acetylation, ubiquitination and small ubiquitin-like modifier (SUMO) modification (SUMOylation), which affect enzymatic activity and transcriptional repression. Whether PTMs of plant HDACs alter their functions are largely unknown. In this study, we demonstrated that the Arabidopsis SUMO E3 ligase SAP AND MIZ1 DOMAIN-CONTAINING LIGASE1 (SIZ1) in

APA, Harvard, Vancouver, ISO, and other styles

8

Sohn, Sook-Young, та Patrick Hearing. "The adenovirus E4-ORF3 protein functions as a SUMO E3 ligase for TIF-1γ sumoylation and poly-SUMO chain elongation". Proceedings of the National Academy of Sciences 113, № 24 (2016): 6725–30. http://dx.doi.org/10.1073/pnas.1603872113.

Full text

Abstract:

The adenovirus (Ad) early region 4 (E4)-ORF3 protein regulates diverse cellular processes to optimize the host environment for the establishment of Ad replication. E4-ORF3 self-assembles into multimers to form a nuclear scaffold in infected cells and creates distinct binding interfaces for different cellular target proteins. Previous studies have shown that the Ad5 E4-ORF3 protein induces sumoylation of multiple cellular proteins and subsequent proteasomal degradation of some of them, but the detailed mechanism of E4-ORF3 function remained unknown. Here, we investigate the role of E4-ORF3 in t

APA, Harvard, Vancouver, ISO, and other styles

9

Yang, Shen-hsi, and Andrew D. Sharrocks. "The SUMO E3 Ligase Activity of Pc2 Is Coordinated through a SUMO Interaction Motif." Molecular and Cellular Biology 30, no. 9 (2010): 2193–205. http://dx.doi.org/10.1128/mcb.01510-09.

Full text

Abstract:

ABSTRACT Protein modification by SUMO conjugation has emerged to be an important regulatory event. Recently, the mechanisms through which SUMO elicits its effects on target proteins have been elucidated. One of these is the noncovalent association between SUMO and coregulatory proteins via SUMO interaction motifs (SIMs). We therefore searched for additional binding proteins to elucidate how SUMO acts as a signal to potentiate novel noncovalent interactions with SUMO-binding proteins. We identified an E3 ligase, Pc2, as a SUMO-binding protein with two functionally distinct SIMs. Here, we focus

APA, Harvard, Vancouver, ISO, and other styles

10

Geerts, Cornelia J., Linda Jacobsen, Rhea van de Bospoort, Matthijs Verhage та Alexander J. A. Groffen. "Tomosyn Interacts with the SUMO E3 Ligase PIASγ". PLoS ONE 9, № 3 (2014): e91697. http://dx.doi.org/10.1371/journal.pone.0091697.

Full text

APA, Harvard, Vancouver, ISO, and other styles

11

Werner, Andreas, Annette Flotho, and Frauke Melchior. "The RanBP2/RanGAP1∗SUMO1/Ubc9 Complex Is a Multisubunit SUMO E3 Ligase." Molecular Cell 46, no. 3 (2012): 287–98. http://dx.doi.org/10.1016/j.molcel.2012.02.017.

Full text

APA, Harvard, Vancouver, ISO, and other styles

12

Liu, Yang, Ya-Dong Zhang, Liang Guo та ін. "Protein Inhibitor of Activated STAT 1 (PIAS1) Is Identified as the SUMO E3 Ligase of CCAAT/Enhancer-Binding Protein β (C/EBPβ) during Adipogenesis". Molecular and Cellular Biology 33, № 22 (2013): 4606–17. http://dx.doi.org/10.1128/mcb.00723-13.

Full text

Abstract:

It is well recognized that PIAS1, a SUMO (small ubiquitin-like modifier) E3 ligase, modulates such cellular processes as cell proliferation, DNA damage responses, and inflammation responses. Recent studies have shown that PIAS1 also plays a part in cell differentiation. However, the role of PIAS1 in adipocyte differentiation remains unknown. CCAAT/enhancer-binding protein β (C/EBPβ), a major regulator of adipogenesis, is a target of SUMOylation, but the E3 ligase responsible for the SUMOylation of C/EBPβ has not been identified. The present study showed that PIAS1 functions as a SUMO E3 ligase

APA, Harvard, Vancouver, ISO, and other styles

13

Westerbeck, Jason W., Nagesh Pasupala, Mark Guillotte, et al. "A SUMO-targeted ubiquitin ligase is involved in the degradation of the nuclear pool of the SUMO E3 ligase Siz1." Molecular Biology of the Cell 25, no. 1 (2014): 1–16. http://dx.doi.org/10.1091/mbc.e13-05-0291.

Full text

Abstract:

The Slx5/Slx8 heterodimer constitutes a SUMO-targeted ubiquitin ligase (STUbL) with an important role in SUMO-targeted degradation and SUMO-dependent signaling. This STUbL relies on SUMO-interacting motifs in Slx5 to aid in substrate targeting and carboxy-terminal RING domains in both Slx5 and Slx8 for substrate ubiquitylation. In budding yeast cells, Slx5 resides in the nucleus, forms distinct foci, and can associate with double-stranded DNA breaks. However, it remains unclear how STUbLs interact with other proteins and their substrates. To examine the targeting and functions of the Slx5/Slx8

APA, Harvard, Vancouver, ISO, and other styles

14

Castillo-Villanueva, Elizabeth, Grisel Ballesteros, Melanie Schmid, et al. "The Mre11 Cellular Protein Is Modified by Conjugation of Both SUMO-1 and SUMO-2/3 during Adenovirus Infection." ISRN Virology 2014 (April 7, 2014): 1–14. http://dx.doi.org/10.1155/2014/989160.

Full text

Abstract:

The adenovirus type 5 (Ad5) E1B 55 kDa and E4 Orf6 proteins assemble a Cullin 5-E3 ubiquitin (Ub) ligase that targets, among other cellular proteins, p53 and the Mre11-Rad50-Nbs1 (MRN) complex for degradation. The latter is also inhibited by the E4 Orf3 protein, which promotes the recruitment of Mre11 into specific nuclear sites to promote viral DNA replication. The activities associated with the E1B 55 kDa and E4 Orf6 viral proteins depend mostly on the assembly of this E3-Ub ligase. However, E1B 55 kDa can also function as an E3-SUMO ligase, suggesting not only that regulation of cellular pr

APA, Harvard, Vancouver, ISO, and other styles

15

Jin, Jing Bo, and Paul M. Hasegawa. "Flowering time regulation by the SUMO E3 Ligase SIZ1." Plant Signaling & Behavior 3, no. 10 (2008): 891–92. http://dx.doi.org/10.4161/psb.3.10.6513.

Full text

APA, Harvard, Vancouver, ISO, and other styles

16

Zhang, Shengchun, Yanli Qi, and Chengwei Yang. "Arabidopsis SUMO E3 ligase AtMMS21 regulates root meristem development." Plant Signaling & Behavior 5, no. 1 (2010): 53–55. http://dx.doi.org/10.4161/psb.5.1.10158.

Full text

APA, Harvard, Vancouver, ISO, and other styles

17

Lee, Jiyoung, Kenji Miura, Ray A. Bressan, Paul M. Hasegawa, and Dae-Jin Yun. "Regulation of Plant Innate Immunity by SUMO E3 Ligase." Plant Signaling & Behavior 2, no. 4 (2007): 253–54. http://dx.doi.org/10.4161/psb.2.4.3867.

Full text

APA, Harvard, Vancouver, ISO, and other styles

18

Zhang, Song, Shiju Wang, Jinlian Lv, et al. "SUMO E3 Ligase SlSIZ1 Facilitates Heat Tolerance in Tomato." Plant and Cell Physiology 59, no. 1 (2017): 58–71. http://dx.doi.org/10.1093/pcp/pcx160.

Full text

APA, Harvard, Vancouver, ISO, and other styles

19

Coleman, Duncan, Ayako Kawamura, Momoko Ikeuchi, et al. "The SUMO E3 Ligase SIZ1 Negatively Regulates Shoot Regeneration." Plant Physiology 184, no. 1 (2020): 330–44. http://dx.doi.org/10.1104/pp.20.00626.

Full text

APA, Harvard, Vancouver, ISO, and other styles

20

Duan, Xinyuan, William B. Holmes, and Hong Ye. "Interaction Mapping betweenSaccharomyces cerevisiaeSmc5 and SUMO E3 Ligase Mms21." Biochemistry 50, no. 46 (2011): 10182–88. http://dx.doi.org/10.1021/bi201376e.

Full text

APA, Harvard, Vancouver, ISO, and other styles

21

Spoden, Gilles A., Dieter Morandell, Daniela Ehehalt, et al. "The SUMO-E3 ligase PIAS3 targets pyruvate kinase M2." Journal of Cellular Biochemistry 107, no. 2 (2009): 293–302. http://dx.doi.org/10.1002/jcb.22125.

Full text

APA, Harvard, Vancouver, ISO, and other styles

22

Geoffroy, Marie-Claude, Ellis G. Jaffray, Katherine J. Walker, and Ronald T. Hay. "Arsenic-Induced SUMO-Dependent Recruitment of RNF4 into PML Nuclear Bodies." Molecular Biology of the Cell 21, no. 23 (2010): 4227–39. http://dx.doi.org/10.1091/mbc.e10-05-0449.

Full text

Abstract:

In acute promyelocytic leukemia (APL), the promyelocytic leukemia (PML) protein is fused to the retinoic acid receptor alpha (RAR). Arsenic is an effective treatment for this disease as it induces SUMO-dependent ubiquitin-mediated proteasomal degradation of the PML-RAR fusion protein. Here we analyze the nuclear trafficking dynamics of PML and its SUMO-dependent ubiquitin E3 ligase, RNF4 in response to arsenic. After administration of arsenic, PML immediately transits into nuclear bodies where it undergoes SUMO modification. This initial recruitment of PML into nuclear bodies is not dependent

APA, Harvard, Vancouver, ISO, and other styles

23

van Waardenburg, Robert C. A. M., David M. Duda, Cynthia S. Lancaster, Brenda A. Schulman, and Mary-Ann Bjornsti. "Distinct Functional Domains of Ubc9 Dictate Cell Survival and Resistance to Genotoxic Stress." Molecular and Cellular Biology 26, no. 13 (2006): 4958–69. http://dx.doi.org/10.1128/mcb.00160-06.

Full text

Abstract:

ABSTRACT Covalent modification with SUMO alters protein function, intracellular localization, or protein-protein interactions. Target recognition is determined, in part, by the SUMO E2 enzyme, Ubc9, while Siz/Pias E3 ligases may facilitate select interactions by acting as substrate adaptors. A yeast conditional Ubc9P123L mutant was viable at 36°C yet exhibited enhanced sensitivity to DNA damage. To define functional domains in Ubc9 that dictate cellular responses to genotoxic stress versus those necessary for cell viability, a 1.75-Å structure of yeast Ubc9 that demonstrated considerable cons

APA, Harvard, Vancouver, ISO, and other styles

24

Wan, Jun, Min Zhou, Xiean Ling, Guanggui Ding та Jian Wang. "HSP70 Promotes Heat Tolerance Effect of Lung Cancer Cells Through Mediating SUMOylation of HIF-1α". Journal of Biomaterials and Tissue Engineering 10, № 8 (2020): 1077–84. http://dx.doi.org/10.1166/jbt.2020.2378.

Full text

Abstract:

Radiofrequency ablation produces a heat-tolerance effect and increases HIF-1αp, and HSP70 expression is distributed in the lesion, but whether HSP70 mediates HIF-1α SUMOylation in lung cancer cells remains unclear. Mouse lung cancer LLC cells were cultured under hypoxia and randomly assigned into control group, heat tolerance group and HSP70 siRNA group followed by analysis of HSP70 and HIF-1α level by real time PCR and Western blot, association of HIF-1α with SUMO-1 and SUMO-2/3 by immunoprecipitation, SENP-1, Ubc9 and E3 ligase expression. CD4 + T cells were isolated and divided into control

APA, Harvard, Vancouver, ISO, and other styles

25

Neo, Shu Hui, Yoko Itahana, Jennifer Alagu, et al. "TRIM28 Is an E3 Ligase for ARF-Mediated NPM1/B23 SUMOylation That Represses Centrosome Amplification." Molecular and Cellular Biology 35, no. 16 (2015): 2851–63. http://dx.doi.org/10.1128/mcb.01064-14.

Full text

Abstract:

The tumor suppressor ARF enhances the SUMOylation of target proteins; however, the physiological function of ARF-mediated SUMOylation has been unclear due to the lack of a known, associated E3 SUMO ligase. Here we uncover TRIM28/KAP1 as a novel ARF-binding protein and SUMO E3 ligase for NPM1/B23. ARF and TRIM28 cooperate to SUMOylate NPM1, a nucleolar protein that regulates centrosome duplication and genomic stability. ARF-mediated SUMOylation of NPM1 was attenuated by TRIM28 depletion and enhanced by TRIM28 overexpression. Coexpression of ARF and TRIM28 promoted NPM1 centrosomal localization

APA, Harvard, Vancouver, ISO, and other styles

26

Hay, Ronald T. "Decoding the SUMO signal." Biochemical Society Transactions 41, no. 2 (2013): 463–73. http://dx.doi.org/10.1042/bst20130015.

Full text

Abstract:

SUMO (small ubiquitin-like modifier) emerged from the shadow of the well-established ubiquitin some 15 years ago when it was shown that a distinct conjugation pathway was responsible for SUMO modification. Since then it has been established that SUMO modifies over a thousand substrates and plays diverse roles in many important biological processes. Recognition of SUMO is mediated by short peptide sequences known as SIMs (SUMO-interaction motifs) that allow effector proteins to engage SUMO-modified substrates. Like ubiquitin, SUMO can form polymeric chains, and these chains can be recognized by

APA, Harvard, Vancouver, ISO, and other styles

27

Gur, Ibrahim, Kazushiro Fujiwara, Koichi Hasegawa, and Kazuaki Yoshikawa. "Necdin Promotes Ubiquitin-Dependent Degradation of PIAS1 SUMO E3 Ligase." PLoS ONE 9, no. 6 (2014): e99503. http://dx.doi.org/10.1371/journal.pone.0099503.

Full text

APA, Harvard, Vancouver, ISO, and other styles

28

Miura, K., A. Rus, A. Sharkhuu, et al. "The Arabidopsis SUMO E3 ligase SIZ1 controls phosphate deficiency responses." Proceedings of the National Academy of Sciences 102, no. 21 (2005): 7760–65. http://dx.doi.org/10.1073/pnas.0500778102.

Full text

APA, Harvard, Vancouver, ISO, and other styles

29

Fuhs, Stephen R., and Paul A. Insel. "Caveolin-3 Undergoes SUMOylation by the SUMO E3 Ligase PIASy." Journal of Biological Chemistry 286, no. 17 (2011): 14830–41. http://dx.doi.org/10.1074/jbc.m110.214270.

Full text

APA, Harvard, Vancouver, ISO, and other styles

30

Natalie Winteringham, Louise, Raelene Endersby, Jennifer Beaumont, Jean-Philippe Lalonde, Merlin Crossley, and Svend Peter Klinken. "Hls5, a Novel Ubiquitin E3 Ligase, Modulates Levels of Sumoylated GATA-1." Blood 114, no. 22 (2009): 253. http://dx.doi.org/10.1182/blood.v114.22.253.253.

Full text

Abstract:

Abstract Abstract 253 Hemopoietic lineage commitment is controlled, in part, by transcription factors that regulate specific genes required for the formation of mature blood cells. Differentiation along particular hemopoietic lineages is dependant not only on the presence of particular transcription factors, but also on appropriate concentrations - altering transcription factor levels can force cells into different hemopoietic pathways. Transcription factors undergo numerous post-translational modifications and are controlled spatially via sub-cellular localisation. De-regulation of transcript

APA, Harvard, Vancouver, ISO, and other styles

31

Takahashi, Yoshimitsu, and Yoshiko Kikuchi. "Yeast PIAS-type Ull1/Siz1 Is Composed of SUMO Ligase and Regulatory Domains." Journal of Biological Chemistry 280, no. 43 (2005): 35822–28. http://dx.doi.org/10.1074/jbc.m506794200.

Full text

Abstract:

SUMO (small ubiquitin-like modifier)/Smt3 (suppressor of mif two) is a member of the ubiquitin-related protein family and is known to conjugate with many proteins. In the sumoylation pathway, SUMO/Smt3 is transferred to substrate lysine residues through the thioester cascade of E1 (activating enzyme) and E2 (conjugating enzyme), and E3 (SUMO ligase) functions as an adaptor between E2 and each substrate. Yeast Ull1 (ubiquitin-like protein ligase 1)/Siz1, a PIAS (protein inhibitor of activated STAT)-type SUMO ligase, modifies both cytoplasmic and nuclear proteins. In this paper, we performed a d

APA, Harvard, Vancouver, ISO, and other styles

32

Zhang, Shengchun, Yanli Qi, Ming Liu, and Chengwei Yang. "SUMO E3 Ligase AtMMS21 Regulates Drought Tolerance in Arabidopsis thaliana F." Journal of Integrative Plant Biology 55, no. 1 (2013): 83–95. http://dx.doi.org/10.1111/jipb.12024.

Full text

APA, Harvard, Vancouver, ISO, and other styles

33

Pichler, Andrea, Puck Knipscheer, Hisato Saitoh, Titia K. Sixma, and Frauke Melchior. "The RanBP2 SUMO E3 ligase is neither HECT- nor RING-type." Nature Structural & Molecular Biology 11, no. 10 (2004): 984–91. http://dx.doi.org/10.1038/nsmb834.

Full text

APA, Harvard, Vancouver, ISO, and other styles

34

Chen, Chyi-Chuann, Yong-Yi Chen, I.-Chien Tang, et al. "Arabidopsis SUMO E3 Ligase SIZ1 Is Involved in Excess Copper Tolerance." Plant Physiology 156, no. 4 (2011): 2225–34. http://dx.doi.org/10.1104/pp.111.178996.

Full text

APA, Harvard, Vancouver, ISO, and other styles

35

Liang, Jason, Bin-zhong Li, Alexander P. Tan, Richard D. Kolodner, Christopher D. Putnam, and Huilin Zhou. "SUMO E3 ligase Mms21 prevents spontaneous DNA damage induced genome rearrangements." PLOS Genetics 14, no. 3 (2018): e1007250. http://dx.doi.org/10.1371/journal.pgen.1007250.

Full text

APA, Harvard, Vancouver, ISO, and other styles

36

Kirsh, O. "The SUMO E3 ligase RanBP2 promotes modification of the HDAC4 deacetylase." EMBO Journal 21, no. 11 (2002): 2682–91. http://dx.doi.org/10.1093/emboj/21.11.2682.

Full text

APA, Harvard, Vancouver, ISO, and other styles

37

Lin, Hsiao-Yun, Yu-Shu Liu, Ching-Ya Huang, et al. "SUMO E3 ligase PIAS1 is a potential biomarker indicating stress susceptibility." Psychoneuroendocrinology 120 (October 2020): 104800. http://dx.doi.org/10.1016/j.psyneuen.2020.104800.

Full text

APA, Harvard, Vancouver, ISO, and other styles

38

Zhang, Rui-Fen, Ying Guo, Yuan-Yuan Li, Li-Jie Zhou, Yu-Jin Hao, and Chun-Xiang You. "Functional identification of MdSIZ1 as a SUMO E3 ligase in apple." Journal of Plant Physiology 198 (July 2016): 69–80. http://dx.doi.org/10.1016/j.jplph.2016.04.007.

Full text

APA, Harvard, Vancouver, ISO, and other styles

39

Yamashita, Daisuke, Takanobu Moriuchi, Takashi Osumi та Fumiko Hirose. "Transcription Factor hDREF Is a Novel SUMO E3 Ligase of Mi2α". Journal of Biological Chemistry 291, № 22 (2016): 11619–34. http://dx.doi.org/10.1074/jbc.m115.713370.

Full text

APA, Harvard, Vancouver, ISO, and other styles

40

Kim, Sung‐Il, Jun Soo Kwak, Jong Tae Song, and Hak Soo Seo. "The E3 SUMO ligase AtSIZ1 functions in seed germination in Arabidopsis." Physiologia Plantarum 158, no. 3 (2016): 256–71. http://dx.doi.org/10.1111/ppl.12462.

Full text

APA, Harvard, Vancouver, ISO, and other styles

41

Kwak, Jun Soo, Sung-Il Kim, Sang Woo Park, Jong Tae Song, and Hak Soo Seo. "E3 SUMO ligase AtSIZ1 regulates the cruciferin content of Arabidopsis seeds." Biochemical and Biophysical Research Communications 519, no. 4 (2019): 761–66. http://dx.doi.org/10.1016/j.bbrc.2019.09.064.

Full text

APA, Harvard, Vancouver, ISO, and other styles

42

Journal, Baghdad Science. "Determination of Advanced Oxidation Protein Products, E3 SUMO-Protein Ligase NSE2[NSMCE2], as a Marker to Predict Child Acute Lymphoblastic Leukemia." Baghdad Science Journal 11, no. 1 (2014): 128–38. http://dx.doi.org/10.21123/bsj.11.1.128-138.

Full text

Abstract:

Acute lymphoblastic leukemia (ALL) is a cancer of the blood and bone marrow (spongy tissue in the center of bone). In ALL, too many bone marrow stem cells develop into a type of white blood cell called lymphocytes. These abnormal lymphocytes are not able to fight infection very well. The aim of this study was to investigate possible links between E3 SUMO-Protein Ligase NSE2 [NSMCE2] and increase DNA damage in the childhood patients with Acute lymphoblastic leukemia (ALL). Laboratory investigations including hemoglobin(Hb) ,white blood cell (WBC) , serum total protein , albumin ,globulin , in a

APA, Harvard, Vancouver, ISO, and other styles

43

Suhandynata, Raymond T., Yong-Qi Gao, Ann L. Zhou, Yusheng Yang, Pang-Che Wang, and Huilin Zhou. "Shared and distinct roles of Esc2 and Mms21 in suppressing genome rearrangements and regulating intracellular sumoylation." PLOS ONE 16, no. 2 (2021): e0247132. http://dx.doi.org/10.1371/journal.pone.0247132.

Full text

Abstract:

Protein sumoylation, especially when catalyzed by the Mms21 SUMO E3 ligase, plays a major role in suppressing duplication-mediated gross chromosomal rearrangements (dGCRs). How Mms21 targets its substrates in the cell is insufficiently understood. Here, we demonstrate that Esc2, a protein with SUMO-like domains (SLDs), recruits the Ubc9 SUMO conjugating enzyme to specifically facilitate Mms21-dependent sumoylation and suppress dGCRs. The D430R mutation in Esc2 impairs its binding to Ubc9 and causes a synergistic growth defect and accumulation of dGCRs with mutations that delete the Siz1 and Si

APA, Harvard, Vancouver, ISO, and other styles

44

Malloy, Melanie Theodore, Deneshia J. McIntosh, Treniqka S. Walters, Andrea Flores, J. Shawn Goodwin, and Ifeanyi J. Arinze. "Trafficking of the Transcription Factor Nrf2 to Promyelocytic Leukemia-Nuclear Bodies." Journal of Biological Chemistry 288, no. 20 (2013): 14569–83. http://dx.doi.org/10.1074/jbc.m112.437392.

Full text

Abstract:

Ubiquitylation of Nrf2 by the Keap1-Cullin3/RING box1 (Cul3-Rbx1) E3 ubiquitin ligase complex targets Nrf2 for proteasomal degradation in the cytoplasm and is an extensively studied mechanism for regulating the cellular level of Nrf2. Although mechanistic details are lacking, reports abound that Nrf2 can also be degraded in the nucleus. Here, we demonstrate that Nrf2 is a target for sumoylation by both SUMO-1 and SUMO-2. HepG2 cells treated with As2O3, which enhances attachment of SUMO-2/3 to target proteins, increased SUMO-2/3-modification (polysumoylation) of Nrf2. We show that Nrf2 traffics

APA, Harvard, Vancouver, ISO, and other styles

45

Sáez, Julián Esteban, Cristian Arredondo, Carlos Rivera та María Estela Andrés. "PIASγ controls stability and facilitates SUMO-2 conjugation to CoREST family of transcriptional co-repressors". Biochemical Journal 475, № 8 (2018): 1441–54. http://dx.doi.org/10.1042/bcj20170983.

Full text

Abstract:

CoREST family of transcriptional co-repressors regulates gene expression and cell fate determination during development. CoREST co-repressors recruit with different affinity the histone demethylase LSD1 (KDM1A) and the deacetylases HDAC1/2 to repress with variable strength the expression of target genes. CoREST protein levels are differentially regulated during cell fate determination and in mature tissues. However, regulatory mechanisms of CoREST co-repressors at the protein level have not been studied. Here, we report that CoREST (CoREST1, RCOR1) and its homologs CoREST2 (RCOR2) and CoREST3

APA, Harvard, Vancouver, ISO, and other styles

46

Lee, Martin B., Lioudmila A. Lebedeva, Miyuki Suzawa, Subhagya A. Wadekar, Marion Desclozeaux, and Holly A. Ingraham. "The DEAD-Box Protein DP103 (Ddx20 or Gemin-3) Represses Orphan Nuclear Receptor Activity via SUMO Modification." Molecular and Cellular Biology 25, no. 5 (2005): 1879–90. http://dx.doi.org/10.1128/mcb.25.5.1879-1890.2005.

Full text

Abstract:

ABSTRACT Structural analysis of nuclear receptor subfamily V orphan nuclear receptors suggests that ligand-independent mechanisms must regulate this subclass of receptors. Here, we report that steroidogenic factor 1 (SF-1) and liver receptor homolog 1 are repressed via posttranslational SUMO modification at conserved lysines within the hinge domain. Indeed, mutating these lysines or adding the SUMO isopeptidase SENP1 dramatically increased both native and Gal4-chimera receptor activities. The mechanism by which SUMO conjugation attenuates SF-1 activity was found to be largely histone deacetyla

APA, Harvard, Vancouver, ISO, and other styles

47

Higginbotham, Jennifer M., and Clodagh C. O'Shea. "Adenovirus E4-ORF3 Targets PIAS3 and Together with E1B-55K Remodels SUMO Interactions in the Nucleus and at Virus Genome Replication Domains." Journal of Virology 89, no. 20 (2015): 10260–72. http://dx.doi.org/10.1128/jvi.01091-15.

Full text

Abstract:

ABSTRACTAdenovirus E4-ORF3 and E1B-55K converge in subverting critical overlapping cellular pathways to facilitate virus replication. Here, we show that E1B-55K and E4-ORF3 induce sumoylation and the assembly of SUMO2/3 viral genome replication domains. Using a conjugation-deficient SUMO2 construct, we demonstrate that SUMO2/3 is recruited to E2A viral genome replication domains through noncovalent interactions. E1B-55K and E4-ORF3 have critical functions in inactivating MRN and ATM to facilitate viral genome replication. We show that ATM kinase inhibitors rescue ΔE1B-55K/ΔE4-ORF3 viral genome

APA, Harvard, Vancouver, ISO, and other styles

48

Delegkou, Georgia N., Maria Birkou, Nefeli Fragkaki, et al. "E2 Partner Tunes the Ubiquitylation Specificity of Arkadia E3 Ubiquitin Ligase." Cancers 15, no. 4 (2023): 1040. http://dx.doi.org/10.3390/cancers15041040.

Full text

Abstract:

Arkadia (RNF111) is a positive regulator of the TGF-β signaling that mediates the proteasome-dependent degradation of negative factors of the pathway. It is classified as an E3 ubiquitin ligase and a SUMO-targeted ubiquitin ligase (STUBL), implicated in various pathological conditions including cancer and fibrosis. The enzymatic (ligase) activity of Arkadia is located at its C-terminus and involves the RING domain. Notably, E3 ligases require E2 enzymes to perform ubiquitylation. However, little is known about the cooperation of Arkadia with various E2 enzymes and the type of ubiquitylation th

APA, Harvard, Vancouver, ISO, and other styles

49

Hickey, Christopher M., та Mark Hochstrasser. "STUbL-mediated degradation of the transcription factor MATα2 requires degradation elements that coincide with corepressor binding sites". Molecular Biology of the Cell 26, № 19 (2015): 3401–12. http://dx.doi.org/10.1091/mbc.e15-06-0436.

Full text

Abstract:

The yeast transcription factor MATα2 (α2) is a short-lived protein known to be ubiquitylated by two distinct pathways, one involving the ubiquitin-conjugating enzymes (E2s) Ubc6 and Ubc7 and the ubiquitin ligase (E3) Doa10 and the other operating with the E2 Ubc4 and the heterodimeric E3 Slx5/Slx8. Although Slx5/Slx8 is a small ubiquitin-like modifier (SUMO)-targeted ubiquitin ligase (STUbL), it does not require SUMO to target α2 but instead directly recognizes α2. Little is known about the α2 determinants required for its Ubc4- and STUbL-mediated degradation or how these determinants substitu

APA, Harvard, Vancouver, ISO, and other styles

50

Danielsen, Jannie Rendtlew, Lou Klitgaard Povlsen, Bine Hare Villumsen, et al. "DNA damage–inducible SUMOylation of HERC2 promotes RNF8 binding via a novel SUMO-binding Zinc finger." Journal of Cell Biology 197, no. 2 (2012): 179–87. http://dx.doi.org/10.1083/jcb.201106152.

Full text

Abstract:

Nonproteolytic ubiquitylation of chromatin surrounding deoxyribonucleic acid (DNA) double-strand breaks (DSBs) by the RNF8/RNF168/HERC2 ubiquitin ligases facilitates restoration of genome integrity by licensing chromatin to concentrate genome caretaker proteins near the lesions. In parallel, SUMOylation of so-far elusive upstream DSB regulators is also required for execution of this ubiquitin-dependent chromatin response. We show that HERC2 and RNF168 are novel DNA damage–dependent SUMOylation targets in human cells. In response to DSBs, both HERC2 and RNF168 were specifically modified with SU

APA, Harvard, Vancouver, ISO, and other styles

We offer discounts on all premium plans for authors whose works are included in thematic literature selections. Contact us to get a unique promo code!