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Article ; Online: Role of c-Jun NH

Niu, Xiao-Jing / Wang, Li-Jun / Meng, Hui / Wang, Hong-Fang / Xu, Bao-Hua / Wang, Chen

2022 Volume 30, Issue 1, Page(s) 47–64

Abstract: ... stress responses. The function of the c-Jun NH ...

Abstract	The mitogen-activated protein kinase (MAPK) cascade pathway plays an important role in regulating stress responses. The function of the c-Jun NH
MeSH term(s)	Bees ; Animals ; Antioxidants/metabolism ; Transcription Factor AP-1 ; Mitogen-Activated Protein Kinases ; Pesticides ; Insect Proteins/genetics
Chemical Substances	Antioxidants ; Transcription Factor AP-1 ; Mitogen-Activated Protein Kinases (EC 2.7.11.24) ; Pesticides ; Insect Proteins
Language	English
Publishing date	2022-06-01
Publishing country	Australia
Document type	Journal Article
ZDB-ID	2179775-4
ISSN	1744-7917 ; 1672-9609
ISSN (online)	1744-7917
ISSN	1672-9609
DOI	10.1111/1744-7917.13053
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Article ; Online: c-Jun NH

Chen, Yiping / Liu, Kaihua / Zhang, Jingwen / Hai, Yan / Wang, Peng / Wang, Hongyan / Liu, Qiuyan / Wong, Catherine C L / Yao, Jun / Gao, Yang / Liao, Yijiao / Tang, Xiuwen / Wang, Xiu Jun

Hepatology (Baltimore, Md.)

2020 Volume 71, Issue 5, Page(s) 1787–1801

Abstract: ... While the activation of c-Jun NH: Approach and results: In this study, we demonstrated that the activation of JNK ...

Abstract	Background and aims: Acetaminophen (APAP) overdose induces severe liver injury and hepatic failure. While the activation of c-Jun NH Approach and results: In this study, we demonstrated that the activation of JNK in mouse liver following exposure to APAP was correlated with the phosphorylation of Nrf2 and down-regulation of the antioxidant response element (ARE)-driven genes, NAD(P)H:quinone dehydrogenase 1, glutathione S-transferase α3, glutathione S-transferase M1, glutathione S-transferase M5, and aldo-keto reductase 1C. The JNK inhibitor, SP600125, or knockdown of JNK by infection of adenovirus expressing JNK small interfering RNA, ameliorated the APAP induced liver toxicity, and inhibited the phosphorylation of Nrf2 and down-regulation of detoxifying enzymes by stabilizing the transcription factor. Mechanistically, JNK antagonized Nrf2- and ARE-driven gene expression in a Kelch-like ECH-associated protein 1-independent manner. Biochemical analysis revealed that phosphorylated JNK (P-JNK) directly interacted with the Nrf2-ECH homology (Neh) 1 domain of Nrf2 and phosphorylated the serine-aspartate-serine motif 1 (SDS1) region in the Neh6 domain of Nrf2. Conclusions: Mass spectrometric analysis identified serine 335 in the SDS1 region of mNrf2 as the major phosphorylation site for modulation of Nrf2 ubiquitylation by P-JNK. This study demonstrates that Nrf2 is a target of P-JNK in AILI. Our finding may provide a strategy for the treatment of AILI.
MeSH term(s)	Acetaminophen/toxicity ; Analgesics, Non-Narcotic/toxicity ; Animals ; Anthracenes/pharmacology ; Chemical and Drug Induced Liver Injury/genetics ; Chemical and Drug Induced Liver Injury/metabolism ; Chemical and Drug Induced Liver Injury/pathology ; Cytoprotection/drug effects ; Cytoprotection/genetics ; Disease Models, Animal ; Down-Regulation ; Enzyme Inhibitors/pharmacology ; Liver/drug effects ; Liver/metabolism ; Liver/pathology ; Male ; Mice ; Mice, Inbred C57BL ; Mitogen-Activated Protein Kinase 8/metabolism ; NF-E2-Related Factor 2 ; Phosphorylation/drug effects ; Protein Domains ; Ubiquitination
Chemical Substances	Analgesics, Non-Narcotic ; Anthracenes ; Enzyme Inhibitors ; NF-E2-Related Factor 2 ; Nfe2l2 protein, mouse ; pyrazolanthrone (1TW30Y2766) ; Acetaminophen (362O9ITL9D) ; Mitogen-Activated Protein Kinase 8 (EC 2.7.11.24)
Language	English
Publishing date	2020-02-05
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	604603-4
ISSN	1527-3350 ; 0270-9139
ISSN (online)	1527-3350
ISSN	0270-9139
DOI	10.1002/hep.31116
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Article ; Online: The chromatin remodeling factor Arid1a cooperates with Jun/Fos to promote osteoclastogenesis by epigenetically upregulating Siglec15 expression.

Zhang, Yongxing / Sun, Hangxiang / Huang, Fei / Chen, Yang / Ding, Xiying / Zhou, Chenhe / Wu, Yan / Zhang, Qing / Ma, Xiao / Wang, Jun / Yue, Rui / Shen, Li / Sun, Xuxu / Ye, Zhaoming

Journal of bone and mineral research : the official journal of the American Society for Bone and Mineral Research

2024

Abstract: ... Siglec15) by transcription factor Jun/Fos, which results in the upregulation of Siglec15 and promotion ...

Abstract	Osteoporosis is characterized by an imbalance between osteoclast-mediated bone resorption and osteoblast-related bone formation, particularly increased osteoclastogenesis. However, the mechanisms by which epigenetic factors regulate osteoclast precursor differentiation during osteoclastogenesis remain poorly understood. Here, we show that the specific knockout of the chromatin remodeling factor Arid1a in bone marrow-derived macrophages (BMDMs) results in increased bone mass. The loss of Arid1a in BMDM inhibits cell-cell fusion and maturation of osteoclast precursors, thereby suppressing osteoclast differentiation. Mechanistically, Arid1a increases the chromatin access in the gene promoter region of sialic acid-binding Ig-like lectin 15 (Siglec15) by transcription factor Jun/Fos, which results in the upregulation of Siglec15 and promotion of osteoclast differentiation. However, the loss of Arid1a reprograms the chromatin structure to restrict Siglec15 expression in osteoclast precursors, thereby inhibiting BMDM differentiation into mature osteoclasts. Deleting Arid1a after ovariectomy (a model for postmenopausal bone loss) alleviated bone loss and maintained bone mass. In summary, epigenetic reprogramming mediated by Arid1a loss suppresses osteoclast differentiation and may serve as a promising therapeutic strategy for treating bone loss diseases.
Language	English
Publishing date	2024-03-11
Publishing country	England
Document type	Journal Article
ZDB-ID	632783-7
ISSN	1523-4681 ; 0884-0431
ISSN (online)	1523-4681
ISSN	0884-0431
DOI	10.1093/jbmr/zjae042
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Article: Jun Dimerization Protein 2 (JDP2) Increases p53 Transactivation by Decreasing MDM2.

Price, Kasey / Yang, William H / Cardoso, Leticia / Wang, Chiung-Min / Yang, Richard H / Yang, Wei-Hsiung

Cancers

2024 Volume 16, Issue 5

Abstract: The AP-1 protein complex primarily consists of several proteins from the c-Fos, c-Jun ... activating transcription factor (ATF), and Jun dimerization protein (JDP) families. JDP2 has been shown to interact with the cAMP ...

Abstract	The AP-1 protein complex primarily consists of several proteins from the c-Fos, c-Jun, activating transcription factor (ATF), and Jun dimerization protein (JDP) families. JDP2 has been shown to interact with the cAMP response element (CRE) site present in many cis-elements of downstream target genes. JDP2 has also demonstrates important roles in cell-cycle regulation, cancer development and progression, inhibition of adipocyte differentiation, and the regulation of antibacterial immunity and bone homeostasis. JDP2 and ATF3 exhibit significant similarity in their C-terminal domains, sharing 60-65% identities. Previous studies have demonstrated that ATF3 is able to influence both the transcriptional activity and p53 stability via a p53-ATF3 interaction. While some studies have shown that JDP2 suppresses p53 transcriptional activity and in turn, p53 represses JDP2 promoter activity, the direct interaction between JDP2 and p53 and the regulatory role of JDP2 in p53 transactivation have not been explored. In the current study, we provide evidence, for the first time, that JDP2 interacts with p53 and regulates p53 transactivation. First, we demonstrated that JDP2 binds to p53 and the C-terminal domain of JDP2 is crucial for the interaction. Second, in p53-null H1299 cells, JDP2 shows a robust increase of p53 transactivation in the presence of p53 using p53 (14X)RE-Luc. Furthermore, JDP2 and ATF3 together additively enhance p53 transactivation in the presence of p53. While JDP2 can increase p53 transactivation in the presence of WT p53, JDP2 fails to enhance transactivation of hotspot mutant p53. Moreover, in CHX chase experiments, we showed that JDP2 slightly enhances p53 stability. Finally, our findings indicate that JDP2 has the ability to reverse MDM2-induced p53 repression, likely due to decreased levels of MDM2 by JDP2. In summary, our results provide evidence that JDP2 directly interacts with p53 and decreases MDM2 levels to enhance p53 transactivation, suggesting that JDP2 is a novel regulator of p53 and MDM2.
Language	English
Publishing date	2024-02-29
Publishing country	Switzerland
Document type	Journal Article
ZDB-ID	2527080-1
ISSN	2072-6694
ISSN	2072-6694
DOI	10.3390/cancers16051000
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Article: A study related to the treatment of gastric cancer with Xiang-Sha-Liu-Jun-Zi-Tang based on network analysis.

Jiang, Ke / Liu, Heli / Ge, Jie / Yang, Bo / Wang, Yu / Wang, Wenbo / Wen, Yuqi / Zeng, Siqing / Chen, Quan / Huang, Jun / Xiong, Xingui

Heliyon

2023 Volume 9, Issue 9, Page(s) e19546

Abstract: Purpose: Xiang-Sha-Liu-Jun-Zi-Tang(XSLJZT) is a common formula for the treatment of Gastric Cancer ...

Abstract	Purpose: Xiang-Sha-Liu-Jun-Zi-Tang(XSLJZT) is a common formula for the treatment of Gastric Cancer(GC) and is widely used in clinical practice, however, there is a lack of investigation into its mechanism. Methods: We collected and organized drug and disease targets, constructed the "XSLJZT-Active Ingredient-Target" visualization network, and performed GO and KEGG functional enrichment analysis of crossover genes, followed by molecular docking of active ingredients and core targets. The best docked monomers were combined with weighted gene co-expression network analysis(WGCNA) and macroscopically analyzed by GO and KEGG enrichment techniques. The results of cluster gene difference analysis, ROC evaluation, and CIBERSORT immune infiltration analysis were evaluated and finally supported by cellular experiments. Results: The main components of XSLJZT are quercetin, stigmasterol, and naringenin, effectively treat GC by targeting STAT3, TP53 and MAPK3, which are involved in IL-17, TNF and HIF-1 signaling pathways. The results of molecular docking showed that quercetin bound better to the core targets. We performed an in-depth analysis of this monomer and found that quercetin acts on the core targets of TP53, MMP9, TIMP1 and MYC, and is involved in two key signaling pathways, TNF and IL-17, thus effectively treating GC. The experimental results are consistent with our analysis that quercetin inhibits the proliferation of GC cells and promotes apoptosis, and TP53, MYC and TIMP1 are the quercetin targets for the treatment of GC. Conclusion: The present study tentatively suggests that quercetin, the main active ingredient in XSLJZT, can exert a therapeutic effect on GC by targeting TIMP1.
Language	English
Publishing date	2023-08-28
Publishing country	England
Document type	Journal Article
ZDB-ID	2835763-2
ISSN	2405-8440
ISSN	2405-8440
DOI	10.1016/j.heliyon.2023.e19546
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Article ; Online: NOD2/c-Jun NH

Luo, Haixia / Wu, Xixi / Xu, Zhaokun / Hao, Xiujing / Wang, Yongyu / Li, Min

Journal of bacteriology

2020 Volume 202, Issue 20

Abstract: Mycoplasma ... ...

Abstract	Mycoplasma ovipneumoniae
MeSH term(s)	Animals ; Autophagy ; MAP Kinase Signaling System ; Macrophages/microbiology ; Mice ; Mycoplasma ovipneumoniae/pathogenicity ; Nod2 Signaling Adaptor Protein/metabolism ; Phosphorylation ; RAW 264.7 Cells
Chemical Substances	Nod2 Signaling Adaptor Protein ; Nod2 protein, mouse
Language	English
Publishing date	2020-09-23
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2968-3
ISSN	1098-5530 ; 0021-9193
ISSN (online)	1098-5530
ISSN	0021-9193
DOI	10.1128/JB.00689-19
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Article ; Online: Cooperation of MLL1 and Jun in controlling H3K4me3 on enhancers in colorectal cancer.

Lin, Xiang / Chen, Ji-Dong / Wang, Chen-Yu / Cai, Zhen / Zhan, Rui / Yang, Chen / Zhang, La-Ying / Li, Lian-Yun / Xiao, Yong / Chen, Ming-Kai / Wu, Min

Genome biology

2023 Volume 24, Issue 1, Page(s) 268

Abstract: ... on the identified Vm3Es. We demonstrate that the transcription factor AP1/JUN interacts with MLL1 and regulates m3E ...

Abstract	Background: Enhancer dysregulation is one of the important features for cancer cells. Enhancers enriched with H3K4me3 have been implicated to play important roles in cancer. However, their detailed features and regulatory mechanisms have not been well characterized. Results: Here, we profile the landscape of H3K4me3-enriched enhancers (m3Es) in 43 pairs of colorectal cancer (CRC) samples. M3Es are widely distributed in CRC and averagely possess around 10% of total active enhancers. We identify 1322 gain variant m3Es and 367 lost variant m3Es in CRC. The target genes of the gain m3Es are enriched in immune response pathways. We experimentally prove that repression of CBX8 and RPS6KA5 m3Es inhibits target gene expression in CRC. Furthermore, we find histone methyltransferase MLL1 is responsible for depositing H3K4me3 on the identified Vm3Es. We demonstrate that the transcription factor AP1/JUN interacts with MLL1 and regulates m3E activity. Application of a small chemical inhibitor for MLL1 activity, OICR-9429, represses target gene expression of the identified Vm3Es, enhances anti-tumor immunity and inhibits CRC growth in an animal model. Conclusions: Taken together, our study illustrates the genome-wide landscape and the regulatory mechanisms of m3Es in CRC, and reveals potential novel strategies for cancer treatment.
MeSH term(s)	Animals ; Colorectal Neoplasms/genetics ; Enhancer Elements, Genetic ; Histones/metabolism ; Myeloid-Lymphoid Leukemia Protein/genetics ; Myeloid-Lymphoid Leukemia Protein/metabolism ; Transcription Factor AP-1/metabolism ; Humans ; Proto-Oncogene Proteins c-jun/genetics ; Proto-Oncogene Proteins c-jun/metabolism
Chemical Substances	histone H3 trimethyl Lys4 ; Histones ; Myeloid-Lymphoid Leukemia Protein (149025-06-9) ; Transcription Factor AP-1 ; KMT2A protein, human ; JUN protein, human ; Proto-Oncogene Proteins c-jun
Language	English
Publishing date	2023-11-27
Publishing country	England
Document type	Journal Article
ZDB-ID	2040529-7
ISSN	1474-760X ; 1474-760X
ISSN (online)	1474-760X
ISSN	1474-760X
DOI	10.1186/s13059-023-03108-3
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Article ; Online: TYRO3 protects podocyte via JNK/c-jun-P53 pathway.

Zhang, Liwen / Jiang, Song / Shi, Jinsong / Xu, Xiaodong / Wang, Ling / Zhai, Xiuwen / Hou, Qin / Qin, Weisong / Chen, Zhaohong

Archives of biochemistry and biophysics

2023 Volume 739, Page(s) 109578

Abstract: ... conferred antiapoptotic effects through the activation of JNK/c-jun-P53 in podocytes. Our results revealed ...

Abstract	Podocyte injury plays a critical role in diabetic kidney disease (DKD). Our previous work demonstrated a protective role of tyrosine-protein kinase receptor TYRO3 in glomerular disease; However, the downstream signaling of TYRO3 remains unclear. Our data showed that genetic ablation of tyro3 in zebrafish recapitulated a nephrotic syndrome phenotype. TYRO3 expression was suppressed by high glucose and TGF-β, which may contribute to the decreased TYRO3 expression in progressive DKD. Moreover, knockdown of TYRO3 expression with siRNA induced podocytes apoptosis and cytoskeleton rearrangement. Further study revealed that TYRO3 conferred antiapoptotic effects through the activation of JNK/c-jun-P53 in podocytes. Our results revealed a novel signaling module of TYRO3 in podocyte homeostasis, which provides a new molecular insight of TYRO3 effect in podocyte protection.
MeSH term(s)	Animals ; Podocytes/metabolism ; Tumor Suppressor Protein p53/genetics ; Tumor Suppressor Protein p53/metabolism ; Zebrafish/metabolism ; Diabetic Nephropathies/genetics ; Diabetic Nephropathies/metabolism ; Signal Transduction ; Apoptosis
Chemical Substances	Tumor Suppressor Protein p53
Language	English
Publishing date	2023-03-21
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	523-x
ISSN	1096-0384 ; 0003-9861
ISSN (online)	1096-0384
ISSN	0003-9861
DOI	10.1016/j.abb.2023.109578
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Article ; Online: c-Jun phosphorylated by JNK is required for protecting Gli2 from proteasomal-ubiquitin degradation by PGE2-JNK signaling axis.

Yang, Jun / Wang, Juan / Zhang, Yu / Huang, Wenjing / Zhang, Shaoqing / Yin, Peihao / Tan, Wenfu

Biochimica et biophysica acta. Molecular cell research

2022 Volume 1870, Issue 3, Page(s) 119418

Abstract: ... signaling pathway. In this study, we showed that c-Jun, a classic substrate of JNK, increased Gli2 protein stability ... after phosphorylated by PGE2. Suppressing the function of c-Jun or JNK indicated that c-Jun prevents ... of Gli2 was detected in colorectal cancer cells treated with PGE2 while suppression of c-Jun restored ...

Abstract	Hedgehog (Hh) signaling pathway includes canonical and non-canonical activation manners. In colorectal cancer, we have previously shown that PGE2-JNK could initiate non-canonical activation of the Hh signaling pathway. In this study, we showed that c-Jun, a classic substrate of JNK, increased Gli2 protein stability after phosphorylated by PGE2. Suppressing the function of c-Jun or JNK indicated that c-Jun prevents Gli2 from protease degradation caused by PGE2-JNK. Moreoer, we revealed that less ubiquitination of Gli2 was detected in colorectal cancer cells treated with PGE2 while suppression of c-Jun restored the ubiquitination of Gli2. In addition, we observed that suppression of c-Jun significantly decreased Gli2 expression no matter when Gli2 remained in phosphorylation or non-phosphorylation state. These phenomena were recapitulated, when the endpoint of Gli2 expression was replaced by Gli2 ubiquitination. Furthermore, we demonstrated that restricting c-Jun function ablated the PGE2-provoked Hh activity and proliferation of colorectal cancer cells. These results elucidated that the evasion of Gli2 with phosphorylation from proteasomal-ubiquitin degradation needed the cooperation of phosphorylated c-Jun by kinase JNK, which contributed to promoting Hh activation and the proliferation of colorectal cancer cells. This study provides a theoretical foundation to target PGE2 downstream for the prevention and treatment of colorectal cancer.
MeSH term(s)	Humans ; Colorectal Neoplasms ; Dinoprostone ; Hedgehog Proteins/metabolism ; Kruppel-Like Transcription Factors/metabolism ; Nuclear Proteins ; Ubiquitin/metabolism ; Zinc Finger Protein Gli2 ; Proto-Oncogene Proteins c-jun/metabolism ; JNK Mitogen-Activated Protein Kinases/metabolism
Chemical Substances	Dinoprostone (K7Q1JQR04M) ; GLI2 protein, human ; Hedgehog Proteins ; Kruppel-Like Transcription Factors ; Nuclear Proteins ; Ubiquitin ; Zinc Finger Protein Gli2 ; Proto-Oncogene Proteins c-jun ; JNK Mitogen-Activated Protein Kinases (EC 2.7.11.24)
Language	English
Publishing date	2022-12-27
Publishing country	Netherlands
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	60-7
ISSN	1879-2596 ; 1879-260X ; 1872-8006 ; 1879-2642 ; 1879-2618 ; 1879-2650 ; 0006-3002 ; 0005-2728 ; 0005-2736 ; 0304-4165 ; 0167-4838 ; 1388-1981 ; 0167-4889 ; 0167-4781 ; 0304-419X ; 1570-9639 ; 0925-4439 ; 1874-9399
ISSN (online)	1879-2596 ; 1879-260X ; 1872-8006 ; 1879-2642 ; 1879-2618 ; 1879-2650
ISSN	0006-3002 ; 0005-2728 ; 0005-2736 ; 0304-4165 ; 0167-4838 ; 1388-1981 ; 0167-4889 ; 0167-4781 ; 0304-419X ; 1570-9639 ; 0925-4439 ; 1874-9399
DOI	10.1016/j.bbamcr.2022.119418
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Article ; Online: Jun/Fos promotes migration and invasion of hepatocellular carcinoma cells by enhancing BORIS promoter activity.

Xian, Longjun / Xiong, Yimei / Qin, Lu / Wei, Ling / Zhou, Siqi / Wang, Qinda / Fu, Qiang / Chen, Mingmei / Qin, Yang

The international journal of biochemistry & cell biology

2024 Volume 169, Page(s) 106540

Abstract: ... engages in interactions with the Hippo pathway. Thus, we attempt to prove whether Jun and Fos, a major ... revealed the existence of binding sites for Jun and Fos within the BORIS promoter. Through a series ... of overexpression and knockdown experiments, we corroborated that Jun and Fos have the capacity to augment BORIS ...

Abstract	The Brother of the Regulator of Imprinted Sites (BORIS), as a specific indicator of hepatocellular carcinoma, exhibits a significant increase in expression. However, its upstream regulatory network remains enigmatic. Previous research has indicated a strong correlation between the Hippo pathway and the progression of hepatocellular carcinoma. It is well established that the Activator Protein-1 (AP-1) frequently engages in interactions with the Hippo pathway. Thus, we attempt to prove whether Jun and Fos, a major member of the AP-1 family, are involved in the regulation of BORIS expression. Bioinformatics analysis revealed the existence of binding sites for Jun and Fos within the BORIS promoter. Through a series of overexpression and knockdown experiments, we corroborated that Jun and Fos have the capacity to augment BORIS expression, thereby fostering the migration and invasion of hepatocellular carcinoma cells. Moreover, Methylation-Specific PCR and Bisulfite Sequencing PCR assays revealed that Jun and Fos do not have a significant impact on the demethylation of the BORIS promoter. However, luciferase reporter and chromatin immunoprecipitation experiments substantiated that Jun and Fos could directly bind to the BORIS promoter, thereby enhancing its transcription. In conclusion, these results suggest that Jun and Fos can promote the development of hepatocellular carcinoma by directly regulating the expression of BORIS. These findings may provide experimental evidence positioning BORIS as a novel target for the clinical intervention of hepatocellular carcinoma.
MeSH term(s)	Humans ; Carcinoma, Hepatocellular/pathology ; Transcription Factor AP-1/genetics ; Transcription Factor AP-1/metabolism ; Liver Neoplasms/pathology ; Cell Line ; Promoter Regions, Genetic/genetics
Chemical Substances	Transcription Factor AP-1
Language	English
Publishing date	2024-01-26
Publishing country	Netherlands
Document type	Journal Article
ZDB-ID	1228429-4
ISSN	1878-5875 ; 1357-2725
ISSN (online)	1878-5875
ISSN	1357-2725
DOI	10.1016/j.biocel.2024.106540
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