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Author: Grafiati

Published: 10 December 2022

Last updated: 28 January 2023

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1

Sivakumar, Dakshinamurthy, Vikash Kumar, Michael Naumann, and Matthias Stein. "Activation and selectivity of OTUB-1 and OTUB-2 deubiquitinylases." Journal of Biological Chemistry 295, no. 20 (April 7, 2020): 6972–82. http://dx.doi.org/10.1074/jbc.ra120.013073.

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The ovarian tumor domain (OTU) deubiquitinylating cysteine proteases OTUB1 and OTUB2 (OTU ubiquitin aldehyde binding 1 and 2) are representative members of the OTU subfamily of deubiquitinylases. Deubiquitinylation critically regulates a multitude of important cellular processes, such as apoptosis, cell signaling, and growth. Moreover, elevated OTUB expression has been observed in various cancers, including glioma, endometrial cancer, ovarian cancer, and breast cancer. Here, using molecular dynamics simulation approaches, we found that both OTUB1 and OTUB2 display a catalytic triad characteristic of proteases but differ in their configuration and protonation states. The OTUB1 protein had a prearranged catalytic site, with strong electrostatic interactions between the active-site residues His265 and Asp267. In OTUB2, however, the arrangement of the catalytic triad was different. In the absence of ubiquitin, the neutral states of the catalytic-site residues in OTUB2 were more stable, resulting in larger distances between these residues. Only upon ubiquitin binding did the catalytic triad in OTUB2 rearrange and bring the active site into a catalytically feasible state. An analysis of water access channels revealed only a few diffusion trajectories for the catalytically active form of OTUB1, whereas in OTUB2 the catalytic site was solvent-accessible, and a larger number of water molecules reached and left the binding pocket. Interestingly, in OTUB2, the catalytic residues His224 and Asn226 formed a stable hydrogen bond. We propose that the observed differences in activation kinetics, protonation states, water channels, and active-site accessibility between OTUB1 and OTUB2 may be relevant for the selective design of OTU inhibitors.

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2

Edelmann, Mariola J., Alexander Iphöfer, Masato Akutsu, Mikael Altun, Katalin di Gleria, Holger B. Kramer, Edda Fiebiger, Sirano Dhe-Paganon, and Benedikt M. Kessler. "Structural basis and specificity of human otubain 1-mediated deubiquitination." Biochemical Journal 418, no. 2 (February 11, 2009): 379–90. http://dx.doi.org/10.1042/bj20081318.

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OTUB (otubain) 1 is a human deubiquitinating enzyme that is implicated in mediating lymphocyte antigen responsiveness, but whose molecular function is generally not well defined. A structural analysis of OTUB1 shows differences in accessibility to the active site and in surface properties of the substrate-binding regions when compared with its close homologue, OTUB2, suggesting variations in regulatory mechanisms and substrate specificity. Biochemical analysis reveals that OTUB1 has a preference for cleaving Lys48-linked polyubiquitin chains over Lys63-linked polyubiquitin chains, and it is capable of cleaving NEDD8 (neural-precursor-cell-expressed developmentally down-regulated 8), but not SUMO (small ubiquitin-related modifier) 1/2/3 and ISG15 (interferon-stimulated gene 15) conjugates. A functional comparison of OTUB1 and OTUB2 indicated a differential reactivity towards ubiquitin-based active-site probes carrying a vinyl methyl ester, a 2-chloroethyl or a 2-bromoethyl group at the C-terminus. Mutational analysis suggested that a narrow P1′ site, as observed in OTUB1, correlates with its ability to preferentially cleave Lys48-linked ubiquitin chains. Analysis of cellular interaction partners of OTUB1 by co-immunoprecipitation and MS/MS (tandem mass spectrometry) experiments demonstrated that FUS [fusion involved in t(12;6) in malignant liposarcoma; also known as TLS (translocation in liposarcoma) or CHOP (CCAAT/enhancer-binding protein homologous protein)] and RACK1 [receptor for activated kinase 1; also known as GNB2L1 (guanine-nucleotide-binding protein β polypeptide 2-like 1)] are part of OTUB1-containing complexes, pointing towards a molecular function of this deubiquitinating enzyme in RNA processing and cell adhesion/morphology.

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3

Thanh Huyen, Nguyen, Nguyen Hoang Giang, and Nguyen Thi Xuan. "Expression of deubiquitinase genes and inflammatory response in myeloid leukemia." Vietnam Journal of Biotechnology 20, no. 3 (September 30, 2022): 401–8. http://dx.doi.org/10.15625/1811-4989/16428.

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Myeloid leukemia (ML) is a cancer of the blood that begins when cells of the myeloid lineage uncontrollably change and grow. Acute myeloid leukemia (AML) is a disorder of rapid, uncontrolled growth of immature myeloid cells in the blood and bone marrow. Chronic myeloid leukemia (CML) is characterized by the aberrant proliferation of myeloid cells and driven by the translocation of regions of the BCR and ABL genes to form the Philadelphia (Ph) chromosome. The deubiquitinase enzymes (DUBs) including A20, OTUB1, OTUB2, and Cezanne play important roles in inhibiting NF-κB activation in response to various stimuli. Cytokines including tumor necrosis factor-alpha (TNF-α), IL-6, and IL-1β are released from immune cell activation triggered by antigenic stimulation. To this end, blood samples of 20 AML and 62 CML patients and the control group consisting of 37 healthy individuals were used to examine the mRNA expression of A20, OTUB1, OTUB2 and Cezanne genes by using quantitative RT-PCR and determine IL-6, TNF-α and IL-1β concentrations by using ELISA. As a result, the mRNA level of OTUB1 was significantly decreased in both AML and CML patients compared to that in healthy individuals, however, no difference in the transcriptional expression of OTUB2 among AML and CML patients and control group was detected. Unlike the levels of OTUB1 and OTUB2, the expressions of A20 and Cezanne in CML, but not in AML patients were significantly lower than healthy individuals. For serum cytokine analysis of the study groups, in AML and CML samples, IL-6 and TNF-α concentrations significantly increased in comparison with the control group, however, IL-1β level was similar among CML, AML patients and healthy individuals. In conclusion, this study revealed the different DUB involvement in the pathogenesis of ML, suggesting further investigations on gene polymorphisms and their functions linked to biological properties of leukemia cells.

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4

Pasupala, Nagesh, Marie E. Morrow, Lauren T. Que, Barbara A. Malynn, Averil Ma, and Cynthia Wolberger. "OTUB1 non-catalytically stabilizes the E2 ubiquitin-conjugating enzyme UBE2E1 by preventing its autoubiquitination." Journal of Biological Chemistry 293, no. 47 (October 3, 2018): 18285–95. http://dx.doi.org/10.1074/jbc.ra118.004677.

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OTUB1 is a deubiquitinating enzyme that cleaves Lys-48–linked polyubiquitin chains and also regulates ubiquitin signaling through a unique, noncatalytic mechanism. OTUB1 binds to a subset of E2 ubiquitin-conjugating enzymes and inhibits their activity by trapping the E2∼ubiquitin thioester and preventing ubiquitin transfer. The same set of E2s stimulate the deubiquitinating activity of OTUB1 when the E2 is not charged with ubiquitin. Previous studies have shown that, in cells, OTUB1 binds to E2-conjugating enzymes of the UBE2D (UBCH5) and UBE2E families, as well as to UBE2N (UBC13). Cellular roles have been identified for the interaction of OTUB1 with UBE2N and members of the UBE2D family, but not for interactions with UBE2E E2 enzymes. We report here a novel role for OTUB1–E2 interactions in modulating E2 protein ubiquitination. We observe that Otub1−/− knockout mice exhibit late-stage embryonic lethality. We find that OTUB1 depletion dramatically destabilizes the E2-conjugating enzyme UBE2E1 (UBCH6) in both mouse and human OTUB1 knockout cell lines. Of note, this effect is independent of the catalytic activity of OTUB1, but depends on its ability to bind to UBE2E1. We show that OTUB1 suppresses UBE2E1 autoubiquitination in vitro and in cells, thereby preventing UBE2E1 from being targeted to the proteasome for degradation. Taken together, we provide evidence that OTUB1 rescues UBE2E1 from degradation in vivo.

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5

Baek, Suk-Hwan, and Han Zhong Pei. "Ovarian tumor domain-containing ubiquitin aldehyde binding protein 1 inhibits IL-6 production by regulating Nur77 stability." Journal of Immunology 202, no. 1_Supplement (May 1, 2019): 52.6. http://dx.doi.org/10.4049/jimmunol.202.supp.52.6.

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Abstract Nur77 (NR4A1) plays an important role in various cellular responses such as apoptosis and inflammation. Nur77 is rapidly degraded in cells and its protein level is critically controlled. Although few ubiquitin E3 ligases regulating the Nur77 protein have been defined, the deubiquitinase (DUB) responsible for Nur77 stability has not been reported to date. We identified ovarian tumor domain-containing ubiquitin aldehyde binding protein 1 (OTUB1) as a DUB that stabilizes Nur77 by preventing its proteasomal degradation. We found that OTUB1 interacted with Nur77 to deubiquitinate it, thereby stabilizing Nur77 in an Asp88-dependent manner. This suggests that OTUB1 targets Nur77 for deubiquitination via a non-canonical mechanism. Moreover, we confirmed that OTUB1 reverses ubiquitination of the K48-linked chains in Nur77. Functionally, OTUB1 inhibited TNFα-induced IL-6 production by promoting Nur77 protein stability. OTUB1 modulated the stability of Nur77 as a counterpart of tripartite motif 13 (Trim13). That is, OTUB1 reduced the ubiquitination and degradation of Nur77 potentiated by Trim13. In addition, this DUB also inhibited IL-6 production, which was further amplified by Trim13 in TNFα-induced IL-6 production. These findings suggest that OTUB1 is an important regulator of Nur77 stability and plays a role in controlling the inflammatory response.

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Ruiz-Serrano, Amalia, Christina Boyle, Josep Monné Rodríguez, Julia Günter, Agnieszka Jucht, Svende Pfundstein, Andreas Bapst, Thomas Lutz, Roland Wenger, and Carsten Scholz. "The Deubiquitinase OTUB1 Is a Key Regulator of Energy Metabolism." International Journal of Molecular Sciences 23, no. 3 (January 28, 2022): 1536. http://dx.doi.org/10.3390/ijms23031536.

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Dysregulated energy metabolism is a major contributor to a multitude of pathologies, including obesity and diabetes. Understanding the regulation of metabolic homeostasis is of utmost importance for the identification of therapeutic targets for the treatment of metabolically driven diseases. We previously identified the deubiquitinase OTUB1 as substrate for the cellular oxygen sensor factor-inhibiting HIF (FIH) with regulatory effects on cellular energy metabolism, but the physiological relevance of OTUB1 is unclear. Here, we report that the induced global deletion of OTUB1 in adult mice (Otub1 iKO) elevated energy expenditure, reduced age-dependent body weight gain, facilitated blood glucose clearance and lowered basal plasma insulin levels. The respiratory exchange ratio was maintained, indicating an unaltered nutrient oxidation. In addition, Otub1 deletion in cells enhanced AKT activity, leading to a larger cell size, higher ATP levels and reduced AMPK phosphorylation. AKT is an integral part of insulin-mediated signaling and Otub1 iKO mice presented with increased AKT phosphorylation following acute insulin administration combined with insulin hypersensitivity. We conclude that OTUB1 is an important regulator of metabolic homeostasis.

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7

Koschel, Josephin, Gopala Nishanth, Sissy Just, Kunjan Harit, Andrea Kröger, Martina Deckert, Michael Naumann, and Dirk Schlüter. "OTUB1 prevents lethal hepatocyte necroptosis through stabilization of c-IAP1 during murine liver inflammation." Cell Death & Differentiation 28, no. 7 (March 12, 2021): 2257–75. http://dx.doi.org/10.1038/s41418-021-00752-9.

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AbstractIn bacterial and sterile inflammation of the liver, hepatocyte apoptosis is, in contrast to necroptosis, a common feature. The molecular mechanisms preventing hepatocyte necroptosis and the potential consequences of hepatocyte necroptosis are largely unknown. Apoptosis and necroptosis are critically regulated by the ubiquitination of signaling molecules but especially the regulatory function of deubiquitinating enzymes (DUBs) is imperfectly defined. Here, we addressed the role of the DUB OTU domain aldehyde binding-1 (OTUB1) in hepatocyte cell death upon both infection with the hepatocyte-infecting bacterium Listeria monocytogenes (Lm) and D-Galactosamine (DGal)/Tumor necrosis factor (TNF)-induced sterile inflammation. Combined in vivo and in vitro experiments comprising mice lacking OTUB1 specifically in liver parenchymal cells (OTUB1LPC-KO) and human OTUB1-deficient HepG2 cells revealed that OTUB1 prevented hepatocyte necroptosis but not apoptosis upon infection with Lm and DGal/TNF challenge. Lm-induced necroptosis in OTUB1LPC-KO mice resulted in increased alanine aminotransferase (ALT) and lactate dehydrogenase (LDH) release and rapid lethality. Treatment with the receptor-interacting serine/threonine-protein kinase (RIPK) 1 inhibitor necrostatin-1s and deletion of the pseudokinase mixed lineage kinase domain-like protein (MLKL) prevented liver damage and death of infected OTUB1LPC-KO mice. Mechanistically, OTUB1 reduced K48-linked polyubiquitination of the cellular inhibitor of apoptosis 1 (c-IAP1), thereby diminishing its degradation. In the absence of OTUB1, c-IAP1 degradation resulted in reduced K63-linked polyubiquitination and increased phosphorylation of RIPK1, RIPK1/RIPK3 necrosome formation, MLKL-phosphorylation and hepatocyte death. Additionally, OTUB1-deficiency induced RIPK1-dependent extracellular-signal-regulated kinase (ERK) activation and TNF production in Lm-infected hepatocytes. Collectively, these findings identify OTUB1 as a novel regulator of hepatocyte-intrinsic necroptosis and a critical factor for survival of bacterial hepatitis and TNF challenge.

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8

Kumari, Raniki, Roshan Kumar, Sanjay Kumar, Abhishek Kumar Singh, Pranita Hanpude, Deepak Jangir, and Tushar Kanti Maiti. "Amyloid aggregates of the deubiquitinase OTUB1 are neurotoxic, suggesting that they contribute to the development of Parkinson's disease." Journal of Biological Chemistry 295, no. 11 (January 31, 2020): 3466–84. http://dx.doi.org/10.1074/jbc.ra119.009546.

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Parkinson's disease (PD) is a multifactorial malady and the second most common neurodegenerative disorder, characterized by loss of dopaminergic neurons in the midbrain. A hallmark of PD pathology is the formation of intracellular protein inclusions, termed Lewy bodies (LBs). Recent MS studies have shown that OTU deubiquitinase ubiquitin aldehyde-binding 1 (OTUB1), a deubiquitinating enzyme of the OTU family, is enriched together with α-synuclein in LBs from individuals with PD and is also present in amyloid plaques associated with Alzheimer's disease. In the present study, using mammalian cell cultures and a PD mouse model, along with CD spectroscopy, atomic force microscopy, immunofluorescence-based imaging, and various biochemical assays, we demonstrate that after heat-induced protein aggregation, OTUB1 reacts strongly with both anti-A11 and anti-osteocalcin antibodies, detecting oligomeric, prefibrillar structures or fibrillar species of amyloidogenic proteins, respectively. Further, recombinant OTUB1 exhibited high thioflavin-T and Congo red binding and increased β-sheet formation upon heat induction. The oligomeric OTUB1 aggregates were highly cytotoxic, characteristic of many amyloid proteins. OTUB1 formed inclusions in neuronal cells and co-localized with thioflavin S and with α-synuclein during rotenone-induced stress. It also co-localized with the disease-associated variant pS129-α-synuclein in rotenone-exposed mouse brains. Interestingly, OTUB1 aggregates were also associated with severe cytoskeleton damage, rapid internalization inside the neuronal cells, and mitochondrial damage, all of which contribute to neurotoxicity. In conclusion, the results of our study indicate that OTUB1 may contribute to LB pathology through its amyloidogenic properties.

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9

Kim, Soomi, Kibeom Park, Jung-Min Oh, and Hongtae Kim. "RNF126 is a positive regulator of TRAF3 ubiquitination." Bioscience, Biotechnology, and Biochemistry 85, no. 12 (October 13, 2021): 2420–28. http://dx.doi.org/10.1093/bbb/zbab177.

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ABSTRACT Ubiquitination and deubiquitination of signaling molecules are critical regulatory mechanisms in various biological contexts such as inflammatory signaling and the DNA damage response. Thus, finely tuned regulation of protein ubiquitination is essential for maintaining cellular homeostasis. Here, we showed that the RING finger protein RNF126 interacts with TRAF3 and promotes its K63-linked polyubiquitination, which is a crucial step in the TRAF3-dependent antiviral response. We found that RNF126 also interacts with OTUB1, a deubiquitinating enzyme that negatively regulates K63-linked ubiquitination of TRAF3. RNF126 promotes ubiquitination of OTUB1, leading to reduced deubiquitinating activity toward TRAF3. Moreover, RNF126 promotes ubiquitination of OTUB1 on cysteine 91, which is reportedly required for its catalytic activity. Taken together, our results suggest that RNF126 positively regulates the antiviral response by directly promoting K63-linked polyubiquitination of TRAF3 and by reducing OTUB1 activity.

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10

Saldana, Matthew, Kacey VanderVorst, Anastasia L. Berg, Hyun Lee, and Kermit L. Carraway. "Otubain 1: a non-canonical deubiquitinase with an emerging role in cancer." Endocrine-Related Cancer 26, no. 1 (January 2019): R1—R14. http://dx.doi.org/10.1530/erc-18-0264.

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The ubiquitin system regulates diverse biological processes, many involved in cancer pathogenesis, by altering the ubiquitination state of protein substrates. This is accomplished by ubiquitin ligases and deubiquitinases (DUBs), which respectively add or remove ubiquitin from substrates to alter their stability, activity, localization and interactions. While lack of catalytic activity makes therapeutic targeting of ubiquitin ligases difficult, DUB inhibitors represent an active area of research and the identification of cancer-associated DUBs may lead to the development of novel therapeutics. A growing body of literature demonstrates that the DUB Otubain 1 (OTUB1) regulates many cancer-associated signaling pathways including MAPK, ERa, epithelial-mesenchymal transition (EMT), RHOa, mTORC1, FOXM1 and P53 to promote tumor cell survival, proliferation, invasiveness and therapeutic resistance. In addition, clinical studies have associated elevated OTUB1 expression with high grade, invasiveness and metastasis in several tumor types including lung, breast, ovarian, glioma, colon and gastric. Interestingly, in addition to catalytic DUB activity, OTUB1 displays a catalytic-independent, non-canonical activity where it inhibits the transfer of ubiquitin onto protein substrates by sequestration of E2 ubiquitin-conjugating enzymes. The aim of this review is to describe the canonical and non-canonical activities of OTUB1, summarize roles for OTUB1 in cancer-associated pathways and discuss its potential therapeutic targeting.

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11

Moree, Shannon E., Laure Maneix, Polina Iakova, Fabio Stossi, Ergun Sahin, and Andre Catic. "Imaging-Based Screening of Deubiquitinating Proteases Identifies Otubain-1 as a Stabilizer of c-MYC." Cancers 14, no. 3 (February 4, 2022): 806. http://dx.doi.org/10.3390/cancers14030806.

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The ubiquitin–proteasome pathway precisely controls the turnover of transcription factors in the nucleus, playing an important role in maintaining appropriate quantities of these regulatory proteins. The transcription factor c-MYC is essential for normal development and is a critical cancer driver. Despite being highly expressed in several tissues and malignancies, the c-MYC protein is also continuously targeted by the ubiquitin–proteasome pathway, which can either facilitate or inhibit c-MYC degradation. Deubiquitinating proteases can remove ubiquitin chains from target proteins and rescue them from proteasomal digestion. This study sought to determine novel elements of the ubiquitin–proteasome pathway that regulate c-MYC levels. We performed an overexpression screen with 41 human proteases to identify which deubiquitinases stabilize c-MYC. We discovered that the highly expressed Otubain-1 (OTUB1) protease increases c-MYC protein levels. Confirming its role in enhancing c-MYC activity, we found that elevated OTUB1 correlates with inferior clinical outcomes in the c-MYC-dependent cancer multiple myeloma, and overexpression of OTUB1 accelerates the growth of myeloma cells. In summary, our study identifies OTUB1 as a novel amplifier of the proto-oncogene c-MYC.

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12

Hu, Zhenzhen, Dan Xiao, Tingting Qiu, Jun Li, and Zhentian Liu. "MicroRNA-103a Curtails the Stemness of Non-Small Cell Lung Cancer Cells by Binding OTUB1 via the Hippo Signaling Pathway." Technology in Cancer Research & Treatment 19 (January 1, 2020): 153303382097164. http://dx.doi.org/10.1177/1533033820971643.

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Objective: Although microRNA-103a (miR-103a) dysfunction has been implicated in various cancers, its relevance to non-small cell lung cancer (NSCLC) has not been clarified. This study was conducted to examine the molecular mechanism underlying the regulatory role of miR-103a in NSCLC. Methods: Kaplan–Meier analysis was carried out to assess the relationship between overall survival of NSCLC patients and miR-103a expression. Reverse-transcription quantitative polymerase chain reaction and western blot analyses were applied to evaluate the expression of relevant genes in tissues and cells. Sphere formation, MTS, flow cytometry, and Transwell assays were performed to characterize stemness. Dual luciferase reporter gene assays were used to clarify the binding relationship between miR-103a and ovarian tumor domain-containing ubiquitin aldehyde binding protein 1 (OTUB1). Finally, western blot analysis was used to assess the involvement of the Hippo pathway in NSCLC. Results: In NSCLC tissues and cells, miR-103a was expressed at low levels, whereas OTUB1 was expressed at high levels. Higher miR-103 expression levels were associated with a better prognosis for patients with NSCLC. When miR-103a was overexpressed, cell viability and stemness decreased, whereas apoptosis and cell cycle arrest were facilitated. The expression of phosphorylated YAP also decreased significantly. Opposite trends were observed after miR-103a silencing. OTUB1 expression and YAP phosphorylation decreased in the presence of miR-103a, and OTUB1 overexpression blocked the inhibitory effects of miR-103a on NSCLC cells. Conclusion: The miR-103a/OTUB1/Hippo axis may play a role in modulating the malignant behavior and stemness of cancer stem cells and thus could be a potential therapeutic target for the management of NSCLC.

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Seo, Seung Un, Seon Min Woo, Shin Kim, Jong-Wook Park, Hyun-Shik Lee, Young-Seuk Bae, Sang Hyun Kim, et al. "Inhibition of cathepsin K sensitizes oxaliplatin-induced apoptotic cell death by Bax upregulation through OTUB1-mediated p53 stabilization in vitro and in vivo." Oncogene 41, no. 4 (November 16, 2021): 550–59. http://dx.doi.org/10.1038/s41388-021-02088-7.

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AbstractCathepsin K is highly expressed in various types of cancers. However, the effect of cathepsin K inhibition in cancer cells is not well characterized. Here, cathepsin K inhibitor (odanacatib; ODN) and knockdown of cathepsin K (siRNA) enhanced oxaliplatin-induced apoptosis in multiple cancer cells through Bax upregulation. Bax knockdown significantly inhibited the combined ODN and oxaliplatin treatment-induced apoptotic cell death. Stabilization of p53 by ODN played a critical role in upregulating Bax expression at the transcriptional level. Casein kinase 2 (CK2)-dependent phosphorylation of OTUB1 at Ser16 played a critical role in ODN- and cathepsin K siRNA-mediated p53 stabilization. Interestingly, ODN-induced p53 and Bax upregulation were modulated by the production of mitochondrial reactive oxygen species (ROS). Mitochondrial ROS scavengers prevented OTUB1-mediated p53 stabilization and Bax upregulation by ODN. These in vitro results were confirmed by in mouse xenograft model, combined treatment with ODN and oxaliplatin significantly reduced tumor size and induced Bax upregulation. Furthermore, human renal clear carcinoma (RCC) tissues revealed a strong correlation between phosphorylation of OTUB1(Ser16) and p53/Bax expression. Our results demonstrate that cathepsin K inhibition enhances oxaliplatin-induced apoptosis by increasing OTUB1 phosphorylation via CK2 activation, thereby promoting p53 stabilization, and hence upregulating Bax.

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Stanišić, Vladimir, Anna Malovannaya, Jun Qin, David M. Lonard, and Bert W. O'Malley. "OTU Domain-containing Ubiquitin Aldehyde-binding Protein 1 (OTUB1) Deubiquitinates Estrogen Receptor (ER) α and Affects ERα Transcriptional Activity." Journal of Biological Chemistry 284, no. 24 (April 21, 2009): 16135–45. http://dx.doi.org/10.1074/jbc.m109.007484.

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Estrogen receptor (ER) α is an essential component in human physiology and is a key factor involved in the development of breast and endometrial cancers. ERα protein levels and transcriptional activity are tightly controlled by the ubiquitin proteasome system. Deubiquitinating enzymes, a class of proteases capable of removing ubiquitin from proteins, are increasingly being seen as key modulators of the ubiquitin proteasome system, regulating protein stability and other functions by countering the actions of ubiquitin ligases. Using mass spectrometry analysis of an ERα protein complex, we identified OTU domain-containing ubiquitin aldehyde-binding protein 1 (OTUB1) as a novel ERα-interacting protein capable of deubiquitinating ERα in cells and in vitro. We show that OTUB1 negatively regulates transcription mediated by ERα in transient reporter gene assays and transcription mediated by endogenous ERα in Ishikawa endometrial cancer cells. We also show that OTUB1 regulates the availability and functional activity of ERα in Ishikawa cells by affecting the transcription of the ERα gene and by stabilizing the ERα protein in the chromatin.

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Li, Jinling, Hongyuan Yu, Jinlong Yao, Zhenming Jiang, Zhenhua Li, and Xiaolu Cui. "Integrative Analysis and Experimental Validation Indicated That SNHG17 Is a Prognostic Marker in Prostate Cancer and a Modulator of the Tumor Microenvironment via a Competitive Endogenous RNA Regulatory Network." Oxidative Medicine and Cellular Longevity 2022 (July 12, 2022): 1–24. http://dx.doi.org/10.1155/2022/1747604.

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The incidence of prostate cancer (PC) is growing rapidly worldwide, and studies uncovering the molecular mechanisms driving the progression and modulating the immune infiltration and antitumor immunity of PC are urgently needed. The long noncoding RNA SNHG family has been recognized as a prognostic marker in cancers and contributes to the progression of multiple cancers, including PC. In this study, we aimed to clarify the prognostic values and underlying mechanisms of SNHGs in promoting the progression and modulating the tumor microenvironment of PC through data mining based on The Cancer Genome Atlas (TCGA) database. We identified that within the SNHG family, SNHG17 was most correlated with the overall survival of PC patients and could act as an independent predictor. Moreover, we constructed a competitive endogenous RNA (ceRNA) network by which SNHG17 promotes progression and potentially inhibits the immune infiltration and immune response of prostate cancer. By interacting with miR-23a-3p/23b-3p/23c, SNHG17 upregulates the expression of UBE2M and OTUB1, which have been demonstrated to play critical roles in the tumorigenesis of human cancers, more importantly promoting cancer cell immunosuppression and resistance to cytotoxic stimulation. Finally, we examined the correlation between SNHG17 expression and the clinical progression of PC patients based on our cohort of 52 PC patients. We also verified the SNHG17/miR-23a/OTUB1 axis in RV-1 and PC-3 cells by dual luciferase and RIP assays, and we further identified that SNHG17 promoted cellular invasive capacity by modulating OTUB1. In summary, the current study conducted a ceRNA-based SNHG17-UBE2M/OTUB1 axis and indicated that SNHG17 might be a novel prognostic factor associated with the progression, immunosuppression, and cytotoxic resistance of PC.

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Li, Shu, Hao Zheng, Ai-Ping Mao, Bo Zhong, Ying Li, Yu Liu, Yan Gao, Yong Ran, Po Tien, and Hong-Bing Shu. "Regulation of Virus-triggered Signaling by OTUB1- and OTUB2-mediated Deubiquitination of TRAF3 and TRAF6." Journal of Biological Chemistry 285, no. 7 (December 7, 2009): 4291–97. http://dx.doi.org/10.1074/jbc.m109.074971.

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Liu, Xin, Wei-Na Jiang, Ji-Gang Wang, and Hua Chen. "Colon cancer bears overexpression of OTUB1." Pathology - Research and Practice 210, no. 11 (November 2014): 770–73. http://dx.doi.org/10.1016/j.prp.2014.05.008.

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18

Sivakumar, Dakshinamurthy, and Matthias Stein. "Binding of SARS-CoV Covalent Non-Covalent Inhibitors to the SARS-CoV-2 Papain-Like Protease and Ovarian Tumor Domain Deubiquitinases." Biomolecules 11, no. 6 (May 28, 2021): 802. http://dx.doi.org/10.3390/biom11060802.

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The urgent need for novel and effective drugs against the SARS-CoV-2 coronavirus pandemic has stimulated research worldwide. The Papain-like protease (PLpro), which is essential for viral replication, shares a similar active site structural architecture to other cysteine proteases. Here, we have used representatives of the Ovarian Tumor Domain deubiquitinase family OTUB1 and OTUB2 along with the PLpro of SARS-CoV-2 to validate and rationalize the binding of inhibitors from previous SARS-CoV candidate compounds. By forming a new chemical bond with the cysteine residue of the catalytic triad, covalent inhibitors irreversibly suppress the protein’s activity. Modeling covalent inhibitor binding requires detailed knowledge about the compounds’ reactivities and binding. Molecular Dynamics refinement simulations of top poses reveal detailed ligand-protein interactions and show their stability over time. The recently discovered selective OTUB2 covalent inhibitors were used to establish and validate the computational protocol. Structural parameters and ligand dynamics are in excellent agreement with the ligand-bound OTUB2 crystal structures. For SARS-CoV-2 PLpro, recent covalent peptidomimetic inhibitors were simulated and reveal that the ligand-protein interaction is very dynamic. The covalent and non-covalent docking plus subsequent MD refinement of known SARS-CoV inhibitors into DUBs and the SARS-CoV-2 PLpro point out a possible approach to target the PLpro cysteine protease from SARS-CoV-2. The results show that such an approach gives insight into ligand-protein interactions, their dynamic character, and indicates a path for selective ligand design.

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Xie, Lili, Aihong Li, Jiabing Shen, Maohong Cao, Xiaojin Ning, Debin Yuan, Yuteng Ji, Hongmei Wang, and Kaifu Ke. "OTUB1 attenuates neuronal apoptosis after intracerebral hemorrhage." Molecular and Cellular Biochemistry 422, no. 1-2 (September 15, 2016): 171–80. http://dx.doi.org/10.1007/s11010-016-2817-8.

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20

Chen C, Hua. "Immunohistochemical Study of OTUB1 Expression in Colon Cancer." International Journal of Sciences 2, no. 02 (2016): 22–26. http://dx.doi.org/10.18483/ijsci.906.

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21

Wiener, Reuven, Xiangbin Zhang, Tao Wang, and Cynthia Wolberger. "The mechanism of OTUB1-mediated inhibition of ubiquitination." Nature 483, no. 7391 (February 22, 2012): 618–22. http://dx.doi.org/10.1038/nature10911.

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22

Wu, Qiong, Yaping Huang, Liya Gu, Zhijie Chang, and Guo-Min Li. "OTUB1 stabilizes mismatch repair protein MSH2 by blocking ubiquitination." Journal of Biological Chemistry 296 (January 2021): 100466. http://dx.doi.org/10.1016/j.jbc.2021.100466.

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RIHAM M. ABU ZEID, M.D., NEDAL A. HEGAZY, M. D., and EMAN A. IBRAHIM, M. D. DIANA Z. SAAD, M.Sc. "Immunohistochemical Expression of Debiquitinating Enzyme OTUB1 in Colorectal Carcinoma." Medical Journal of Cairo University 86, March (March 1, 2018): 695–702. http://dx.doi.org/10.21608/mjcu.2018.55385.

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Liu, Tong, Le Jiang, Omid Tavana, and Wei Gu. "The Deubiquitylase OTUB1 Mediates Ferroptosis via Stabilization of SLC7A11." Cancer Research 79, no. 8 (February 1, 2019): 1913–24. http://dx.doi.org/10.1158/0008-5472.can-18-3037.

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Goncharov, Tatiana, Kyle Niessen, Maria Cristina de Almagro, Anita Izrael-Tomasevic, Anna V. Fedorova, Eugene Varfolomeev, David Arnott, Kurt Deshayes, Donald S. Kirkpatrick, and Domagoj Vucic. "OTUB1 modulates c-IAP1 stability to regulate signalling pathways." EMBO Journal 32, no. 8 (March 22, 2013): 1103–14. http://dx.doi.org/10.1038/emboj.2013.62.

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Que, Lauren T., Marie E. Morrow, and Cynthia Wolberger. "Comparison of Cross-Regulation by Different OTUB1:E2 Complexes." Biochemistry 59, no. 8 (February 12, 2020): 921–32. http://dx.doi.org/10.1021/acs.biochem.9b00993.

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Zhou, Yi, Qingzhu Jia, Xiaoqing Meng, Diangang Chen, and Bo Zhu. "ERRα Regulates OTUB1 Expression to Promote Colorectal Cancer Cell Migration." Journal of Cancer 10, no. 23 (2019): 5812–19. http://dx.doi.org/10.7150/jca.30720.

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Wiener, Reuven, Anthony T. DiBello, Patrick M. Lombardi, Catherine M. Guzzo, Xiangbin Zhang, Michael J. Matunis, and Cynthia Wolberger. "E2 ubiquitin-conjugating enzymes regulate the deubiquitinating activity of OTUB1." Nature Structural & Molecular Biology 20, no. 9 (August 18, 2013): 1033–39. http://dx.doi.org/10.1038/nsmb.2655.

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Nakada, Shinichiro, Ikue Tai, Stephanie Panier, Abdallah Al-Hakim, Shun-ichiro Iemura, Yu-Chi Juang, Lara O’Donnell, et al. "Non-canonical inhibition of DNA damage-dependent ubiquitination by OTUB1." Nature 466, no. 7309 (August 2010): 941–46. http://dx.doi.org/10.1038/nature09297.

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Scholz, Carsten C., Javier Rodriguez, Christina Pickel, Stephen Burr, Jacqueline-alba Fabrizio, Karen A. Nolan, Patrick Spielmann, et al. "FIH Regulates Cellular Metabolism through Hydroxylation of the Deubiquitinase OTUB1." PLOS Biology 14, no. 1 (January 11, 2016): e1002347. http://dx.doi.org/10.1371/journal.pbio.1002347.

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Chen, Yingxiao, Yue-Gang Wang, Yuhuang Li, Xiao-Xin Sun, and Mu-Shui Dai. "Otub1 stabilizes MDMX and promotes its proapoptotic function at the mitochondria." Oncotarget 8, no. 7 (December 27, 2016): 11053–62. http://dx.doi.org/10.18632/oncotarget.14278.

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Xie, Peiyi, Qing Chao, Jiuang Mao, Yue Liu, Jiayu Fang, Jing Xie, Jing Zhen, et al. "The deubiquitinase OTUB1 fosters papillary thyroid carcinoma growth through EYA1 stabilization." Journal of Cellular and Molecular Medicine 25, no. 23 (November 12, 2021): 10980–89. http://dx.doi.org/10.1111/jcmm.17020.

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33

Lee, Bok-Soon, Sung Un Kang, Mei Huang, Yeon Soo Kim, Young-Sun Lee, Jae-Yong Park, and Chul-Ho Kim. "OTUB1 knockdown promotes apoptosis in melanoma cells by upregulating TRAIL expression." BMB Reports 54, no. 12 (December 31, 2021): 608–13. http://dx.doi.org/10.5483/bmbrep.2021.54.12.033.

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Zhou, Honghong, Yongshuo Liu, Rui Zhu, Fang Ding, Xiufeng Cao, Dongxin Lin, and Zhihua Liu. "OTUB1 promotes esophageal squamous cell carcinoma metastasis through modulating Snail stability." Oncogene 37, no. 25 (March 21, 2018): 3356–68. http://dx.doi.org/10.1038/s41388-018-0224-1.

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Xu, Li, Jinquan Li, Zhen Bao, Peng Xu, Hao Chang, Jingjing Wu, Yuanqi Bei, et al. "Silencing of OTUB1 inhibits migration of human glioma cells in vitro." Neuropathology 37, no. 3 (January 31, 2017): 217–26. http://dx.doi.org/10.1111/neup.12366.

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Sorada, Tomoki, Daichi Morimoto, Erik Walinda, and Kenji Sugase. "Molecular recognition and deubiquitination of cyclic K48-linked ubiquitin chains by OTUB1." Biochemical and Biophysical Research Communications 562 (July 2021): 94–99. http://dx.doi.org/10.1016/j.bbrc.2021.05.031.

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Liao, Yihao, Mengyue Yang, Keke Wang, Youzhi Wang, Boqiang Zhong, and Ning Jiang. "Deubiquitinating enzyme OTUB1 in immunity and cancer: Good player or bad actor?" Cancer Letters 526 (February 2022): 248–58. http://dx.doi.org/10.1016/j.canlet.2021.12.002.

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Iskandar, Athirah, Nur Wahida Zulkifli, Muhammad Khairi Ahmad, Kumitaa Theva Das, and Nurulisa Zulkifle. "OTUB1 expression and interaction network analyses in MCF-7 breast cancer cells." Gene Reports 24 (September 2021): 101273. http://dx.doi.org/10.1016/j.genrep.2021.101273.

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Li, Yanchuan, Jin-Young Yang, Xiaoping Xie, Zuliang Jie, Lingyun Zhang, Jianhong Shi, Daniel Lin, et al. "Preventing abnormal NF-κB activation and autoimmunity by Otub1-mediated p100 stabilization." Cell Research 29, no. 6 (May 13, 2019): 474–85. http://dx.doi.org/10.1038/s41422-019-0174-3.

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Bialas, Johanna, Annika N. Boehm, Nicola Catone, Annette Aichem, and Marcus Groettrup. "The ubiquitin-like modifier FAT10 stimulates the activity of deubiquitylating enzyme OTUB1." Journal of Biological Chemistry 294, no. 12 (February 4, 2019): 4315–30. http://dx.doi.org/10.1074/jbc.ra118.005406.

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Juang, Yu-Chi, Marie-Claude Landry, Mario Sanches, Vinayak Vittal, Charles C. Y. Leung, Derek F. Ceccarelli, Abigail-Rachele F. Mateo, et al. "OTUB1 Co-opts Lys48-Linked Ubiquitin Recognition to Suppress E2 Enzyme Function." Molecular Cell 45, no. 3 (February 2012): 384–97. http://dx.doi.org/10.1016/j.molcel.2012.01.011.

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Juang, Yu-Chi, Marie-Claude Landry, Mario Sanches, Vinayak Vittal, Charles Leung, Derek F. Ceccarelli, Abigail-Rachele F. Mateo, et al. "OTUB1 Co-opts Lys48-Linked Ubiquitin Recognition to Suppress E2 Enzyme Function." Molecular Cell 46, no. 4 (May 2012): 549. http://dx.doi.org/10.1016/j.molcel.2012.05.013.

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Zhang, Hui‐Hui, Chao Li, Jian‐Wei Ren, Lian Liu, Xue‐Hua Du, Jie Gao, Tao Liu, and Shang‐Ze Li. "OTUB1 facilitates bladder cancer progression by stabilizing ATF6 in response to endoplasmic reticulum stress." Cancer Science 112, no. 6 (May 2, 2021): 2199–209. http://dx.doi.org/10.1111/cas.14876.

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Karunarathna, U., M. Kongsema, S. Zona, C. Gong, E. Cabrera, A. R. Gomes, E. P. S. Man, et al. "OTUB1 inhibits the ubiquitination and degradation of FOXM1 in breast cancer and epirubicin resistance." Oncogene 35, no. 11 (July 6, 2015): 1433–44. http://dx.doi.org/10.1038/onc.2015.208.

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Huggins, Matthew A., and Sara E. Hamilton. "Deubiquitinase Otub1 negatively regulates IL-15 signaling in CD8 T cells and NK cells." Cellular & Molecular Immunology 16, no. 11 (September 11, 2019): 846–47. http://dx.doi.org/10.1038/s41423-019-0283-4.

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Herhaus, Lina, Ana B. Perez-Oliva, Giorgio Cozza, Robert Gourlay, Simone Weidlich, David G. Campbell, Lorenzo A. Pinna, and Gopal P. Sapkota. "Casein kinase 2 (CK2) phosphorylates the deubiquitylase OTUB1 at Ser16to trigger its nuclear localization." Science Signaling 8, no. 372 (April 14, 2015): ra35. http://dx.doi.org/10.1126/scisignal.aaa0441.

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Pickel, Christina, Julia Günter, Amalia Ruiz-Serrano, Patrick Spielmann, Jacqueline-Alba Fabrizio, Witold Wolski, Daniel J. Peet, Roland H. Wenger, and Carsten C. Scholz. "Oxygen-dependent bond formation with FIH regulates the activity of the client protein OTUB1." Redox Biology 26 (September 2019): 101265. http://dx.doi.org/10.1016/j.redox.2019.101265.

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Wang, Shunni, Yan Ning, Ping Wei, Dongliag Cai, Linghui Lu, Jing Li, and Yiqin Wang. "The non-coding RNA OTUB1-isoform2 promotes ovarian tumour progression and predicts poor prognosis." Journal of Cellular and Molecular Medicine 22, no. 10 (July 25, 2018): 4794–806. http://dx.doi.org/10.1111/jcmm.13733.

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Zhou, Yi, Jiangxue Wu, Xiang Fu, Wuying Du, Ling Zhou, Xiangqi Meng, Hongyan Yu, et al. "OTUB1 promotes metastasis and serves as a marker of poor prognosis in colorectal cancer." Molecular Cancer 13, no. 1 (2014): 258. http://dx.doi.org/10.1186/1476-4598-13-258.

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Zhao, Linlin, Xinbo Wang, Yue Yu, Lu Deng, Lei Chen, Xiaoping Peng, Chenchen Jiao, et al. "OTUB1 protein suppresses mTOR complex 1 (mTORC1) activity by deubiquitinating the mTORC1 inhibitor DEPTOR." Journal of Biological Chemistry 293, no. 13 (January 30, 2018): 4883–92. http://dx.doi.org/10.1074/jbc.m117.809533.

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