E3 ubiquitin ligase RNF2 interacts with the S6′ proteasomal ATPase subunit and increases the ATP hydrolysis activity of S6′

We reported previously that the human RNF2 (RING finger protein 2) protein is an E3 ubiquitin ligase that interacts with the human ubiquitin-conjugating enzyme Hip-2/hE2-25K. In the present study, we show that RNF2 interacts with S6′ ATPase, a subunit of the proteasomal 19 S regulatory complex. S6′ interacts with RNF2 through its N-terminal RING domain, and RNF2 interacts with S6′ through its C-terminal region. Interestingly, the RNF2-S6′ interaction increases the ATP hydrolysis activity of the S6′ protein. Moreover, S6′ ATPase activity is highly increased in the presence of ubiquitinated proteins. The present study suggests that the E3 ubiquitin ligase RNF2 might have a dual function: facilitating the ubiquitination of its target substrates and recruiting the substrates to the proteasome. Furthermore, ATP hydrolysis in the E3/proteasome complex might act as an important signal for the protein degradation pathway.

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An E3 Ubiquitin Ligase RNF139 Serves as a Tumor-Suppressor in Glioma

Journal of Molecular Neuroscience ◽

10.1007/s12031-021-01860-4 ◽

2021 ◽

Author(s):

Xiaofeng Chen ◽

Weiping Kuang ◽

Yong Zhu ◽

Bin Zhou ◽

Xiaosong Li ◽

...

Keyword(s):

Tumor Suppressor ◽

Cell Lines ◽

Ubiquitin Ligase ◽

Glioma Cell ◽

Protein Modification ◽

E3 Ubiquitin Ligase ◽

Ring Finger ◽

Glioma Cells ◽

Migration And Invasion ◽

Tissue Samples

AbstractGlioma is highly lethal because of its high malignancy. Ubiquitination, a type of ubiquitin-dependent protein modification, has been reported to play an oncogenic or tumor-suppressive role in glioma development, depending on the targets. Ring finger protein 139 (RNF139) is a membrane-bound E3 ubiquitin ligase serving as a tumor suppressor by ubiquitylation-dependently suppressing cell growth. Herein, we firstly confirmed the abnormal downregulation of RNF139 in glioma tissues and cell lines. In glioma cells, ectopic RNF139 overexpression could inhibit, whereas RNF139 knockdown could aggravate the aggressive behaviors of glioma cells, including hyperproliferation, migration, and invasion. Moreover, in two glioma cell lines, RNF139 overexpression inhibited, whereas RNF139 knockdown enhanced the phosphorylation of phosphatidylinositol 3-kinase (PI3K) and AKT serine/threonine kinase 1 (AKT). In a word, we demonstrate the aberration in RNF139 expression in glioma tissue samples and cell lines. RNF139 serves as a tumor-suppressor in glioma by inhibiting glioma cell proliferation, migration, and invasion and promoting glioma cell apoptosis through regulating PI3K/AKT signaling.

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DNA Damage-Induced Foci of E2 Ubiquitin-Conjugating Enzyme are Detectable upon Co-transfection with an Interacting E3 Ubiquitin Ligase

Biochemical Genetics ◽

10.1007/s10528-015-9707-8 ◽

2015 ◽

Vol 54 (2) ◽

pp. 147-157 ◽

Cited By ~ 1

Author(s):

Degui Wang ◽

Yingxia Tian ◽

Dong Wei ◽

Yuhong Jing ◽

Haitao Niu ◽

...

Keyword(s):

Dna Damage ◽

Ubiquitin Ligase ◽

E3 Ubiquitin Ligase ◽

Ubiquitin Conjugating Enzyme ◽

Conjugating Enzyme

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p53 down-regulates SARS coronavirus replication and is targeted by the SARS-unique domain and PLprovia E3 ubiquitin ligase RCHY1

Proceedings of the National Academy of Sciences ◽

10.1073/pnas.1603435113 ◽

2016 ◽

Vol 113 (35) ◽

pp. E5192-E5201 ◽

Cited By ~ 55

Author(s):

Yue Ma-Lauer ◽

Javier Carbajo-Lozoya ◽

Marco Y. Hein ◽

Marcel A. Müller ◽

Wen Deng ◽

...

Keyword(s):

Ubiquitin Ligase ◽

Nonstructural Protein ◽

E3 Ubiquitin Ligase ◽

Ring Finger ◽

Immune Recognition ◽

Major Player ◽

Nonstructural Protein 3 ◽

Human Coronaviruses ◽

Unique Domain

Highly pathogenic severe acute respiratory syndrome coronavirus (SARS-CoV) has developed strategies to inhibit host immune recognition. We identify cellular E3 ubiquitin ligase ring-finger and CHY zinc-finger domain-containing 1 (RCHY1) as an interacting partner of the viral SARS-unique domain (SUD) and papain-like protease (PLpro), and, as a consequence, the involvement of cellular p53 as antagonist of coronaviral replication. Residues 95–144 of RCHY1 and 389–652 of SUD (SUD-NM) subdomains are crucial for interaction. Association with SUD increases the stability of RCHY1 and augments RCHY1-mediated ubiquitination as well as degradation of p53. The calcium/calmodulin-dependent protein kinase II delta (CAMK2D), which normally influences RCHY1 stability by phosphorylation, also binds to SUD. In vivo phosphorylation shows that SUD does not regulate phosphorylation of RCHY1 via CAMK2D. Similarly to SUD, the PLpros from SARS-CoV, MERS-CoV, and HCoV-NL63 physically interact with and stabilize RCHY1, and thus trigger degradation of endogenous p53. The SARS-CoV papain-like protease is encoded next to SUD within nonstructural protein 3. A SUD–PLprofusion interacts with RCHY1 more intensively and causes stronger p53 degradation than SARS-CoV PLproalone. We show that p53 inhibits replication of infectious SARS-CoV as well as of replicons and human coronavirus NL63. Hence, human coronaviruses antagonize the viral inhibitor p53 via stabilizing RCHY1 and promoting RCHY1-mediated p53 degradation. SUD functions as an enhancer to strengthen interaction between RCHY1 and nonstructural protein 3, leading to a further increase in in p53 degradation. The significance of these findings is that down-regulation of p53 as a major player in antiviral innate immunity provides a long-sought explanation for delayed activities of respective genes.

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The RING Finger Protein MSL2 in the MOF Complex Is an E3 Ubiquitin Ligase for H2B K34 and Is Involved in Crosstalk with H3 K4 and K79 Methylation

Molecular Cell ◽

10.1016/j.molcel.2011.05.015 ◽

2011 ◽

Vol 43 (1) ◽

pp. 132-144 ◽

Cited By ~ 92

Author(s):

Lipeng Wu ◽

Barry M. Zee ◽

Yanming Wang ◽

Benjamin A. Garcia ◽

Yali Dou

Keyword(s):

Ubiquitin Ligase ◽

E3 Ubiquitin Ligase ◽

Ring Finger ◽

Ring Finger Protein ◽

Finger Protein

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Apple RING finger E3 ubiquitin ligase MdMIEL1 negatively regulates salt and oxidative stresses tolerance

Journal of Plant Biology ◽

10.1007/s12374-016-0457-x ◽

2017 ◽

Vol 60 (2) ◽

pp. 137-145 ◽

Cited By ~ 5

Author(s):

Jian-Ping An ◽

Xin Liu ◽

Lai-Qing Song ◽

Chun-Xiang You ◽

Xiao-Fei Wang ◽

...

Keyword(s):

Ubiquitin Ligase ◽

E3 Ubiquitin Ligase ◽

Ring Finger ◽

Oxidative Stresses ◽

Salt And Oxidative Stresses

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Stella protein facilitates DNA demethylation by disrupting the chromatin association of the RING finger–type E3 ubiquitin ligase UHRF1

Journal of Biological Chemistry ◽

10.1074/jbc.ra119.008008 ◽

2019 ◽

Vol 294 (22) ◽

pp. 8907-8917 ◽

Cited By ~ 5

Author(s):

Wenlong Du ◽

Qiang Dong ◽

Zhuqiang Zhang ◽

Baodong Liu ◽

Ting Zhou ◽

...

Keyword(s):

Ubiquitin Ligase ◽

E3 Ubiquitin Ligase ◽

Ring Finger ◽

Dna Demethylation

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AtPPRT1, an E3 Ubiquitin Ligase, Enhances the Thermotolerance in Arabidopsis

Plants ◽

10.3390/plants9091074 ◽

2020 ◽

Vol 9 (9) ◽

pp. 1074

Author(s):

Yu Liu ◽

Shuya Xiao ◽

Haoran Sun ◽

Linsen Pei ◽

Yingying Liu ◽

...

Keyword(s):

Heat Stress ◽

Ubiquitin Ligase ◽

E3 Ubiquitin Ligase ◽

Degradation Pathway ◽

Vital Role ◽

Loss Of Function ◽

Positive Role ◽

Heat Stress Response ◽

Acquired Thermotolerance ◽

Ubiquitin E3 Ligase

E3 ubiquitin ligase plays a vital role in the ubiquitin-mediated heat-related protein degradation pathway. Herein, we report that the expression of AtPPRT1, a C3HC4 zinc-finger ubiquitin E3 ligase gene, was induced by heat stress, and the β-glucuronidase (GUS) gene driven by the AtPPRT1 promoter has shown increased activity after basal and acquired thermotolerance. To further explore the function of AtPPRT1 in heat stress response (HSR), we used the atpprt1 mutant and AtPPRT1-overexpressing lines (OE2 and OE10) to expose in heat shock. In this study, the atpprt1 mutant had a lower germination and survival rate than those of Col-0 when suffered from the heat stress, whereas OEs enhanced basal and acquired thermotolerance in Arabidopsis seedlings. When compared to Col-0 and OEs, loss-of-function in AtPPRT1 resulted in lower chlorophyll retention and higher content of reactive oxygen species (ROS) after heat treatment. Moreover, the transcript levels of AtPPRT1 and several heat-related genes (AtZAT12, AtHSP21 and AtHSFA7a) were upregulated to greater extents in OEs and lower extents in atpprt1 compared to Col-0 after heat treated. Hence, we suggest that AtPPRT1 may act as a positive role in regulating the high temperature by mediating the degradation of unknown target proteins.

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