mitogen-activated protein kinase 8

マイトジェン活性化プロテインキナーゼ8

WordNet

1. aerate (sewage) so as to favor the growth of organisms that decompose organic matter (同)aerate
2. make (substances) radioactive
3. make active or more active; "activate an old file"
4. make more adsorptive; "activate a metal"
5. rendered active; e.g. rendered radioactive or luminescent or photosensitive or conductive
6. (of e.g. a molecule) made reactive or more reactive (同)excited
7. (military) set up and placed on active assignment; "a newly activated unit"
8. (of sewage) treated with aeration and bacteria to aid decomposition
9. any of a large group of nitrogenous organic compounds that are essential constituents of living cells; consist of polymers of amino acids; essential in the diet of animals for growth and for repair of tissues; can be obtained from meat and eggs and milk and legumes; "a diet high in protein"
10. an enzyme that catalyzes the conversion of a proenzyme to an active enzyme
11. an agent that triggers mitosis

PrepTutorEJDIC

1. …'を'活動的にする / …‘に'放射能を与える / 〈物質〉'を'活性化する
2. 蛋白(たんばく)質

Wikipedia preview

出典(authority):フリー百科事典『ウィキペディア（Wikipedia）』「2012/11/15 13:30:26」(JST)

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Mitogen-activated protein kinase 8
PDB rendering based on 1jnk.
Available structures PDB Ortholog search: PDBe, RCSB List of PDB id codes 1UKH, 1UKI, 2G01, 2GMX, 2H96, 2NO3, 2XRW, 2XS0, 3ELJ, 3O17, 3O2M, 3PZE
Identifiers
Symbols	MAPK8; JNK; JNK-46; JNK1; JNK1A2; JNK21B1/2; PRKM8; SAPK1; SAPK1c
External IDs	OMIM: 601158 MGI: 1346861 HomoloGene: 56760 ChEMBL: 2276 GeneCards: MAPK8 Gene
EC number	2.7.11.24
Gene Ontology Molecular function • protein serine/threonine kinase activity • JUN kinase activity • protein binding • ATP binding • histone deacetylase regulator activity • histone deacetylase binding Cellular component • nucleus • nucleoplasm • cytosol Biological process • toll-like receptor signaling pathway • MyD88-dependent toll-like receptor signaling pathway • MyD88-independent toll-like receptor signaling pathway • apoptotic process • response to stress • JNK cascade • JUN phosphorylation • Toll signaling pathway • induction of apoptosis by extracellular signals • activation of pro-apoptotic gene products • response to UV • positive regulation of gene expression • peptidyl-serine phosphorylation • peptidyl-threonine phosphorylation • regulation of histone deacetylation • negative regulation of protein binding • regulation of protein localization • toll-like receptor 1 signaling pathway • toll-like receptor 2 signaling pathway • toll-like receptor 3 signaling pathway • toll-like receptor 4 signaling pathway • TRIF-dependent toll-like receptor signaling pathway • negative regulation of apoptotic process • innate immune response • nerve growth factor receptor signaling pathway • regulation of sequence-specific DNA binding transcription factor activity • stress-activated MAPK cascade • cellular response to mechanical stimulus • positive regulation of deacetylase activity Sources: Amigo / QuickGO
RNA expression pattern
More reference expression data
Orthologs
Species	Human	Mouse
Entrez	5599	26419
Ensembl	ENSG00000107643	ENSMUSG00000021936
UniProt	P45983	Q91Y86
RefSeq (mRNA)	NM_002750.2	NM_016700.4
RefSeq (protein)	NP_002741.1	NP_057909.1
Location (UCSC)	Chr 10: 49.51 – 49.65 Mb	Chr 14: 33.38 – 33.45 Mb
PubMed search	[1]	[2]

Mitogen-activated protein kinase 8 (also known as JNK1) is an enzyme that in humans is encoded by the MAPK8 gene.

The protein encoded by this gene is a member of the MAP kinase and JNK family. MAP kinases act as an integration point for multiple biochemical signals, and are involved in a wide variety of cellular processes such as proliferation, differentiation, transcription regulation and development. This kinase is activated by various cell stimuli, and targets specific transcription factors, and thus mediates immediate-early gene expression in response to cell stimuli. The activation of this kinase by tumor-necrosis factor alpha (TNF-alpha) is found to be required for TNF-alpha-induced apoptosis. This kinase is also involved in UV radiation-induced apoptosis, which is thought to be related to the cytochrome c-mediated cell death pathway. Studies of the mouse counterpart of this gene suggested that this kinase play a key role in T cell proliferation, apoptosis and differentiation. Four alternately spliced transcript variants encoding distinct isoforms have been reported.

Interactions

MAPK8 has been shown to interact with SPIB, DUSP1, Activating transcription factor 2, SH3BP5, GSTP1, MAPK8IP1, MAP2K7, CRK, MAP2K4, DUSP22, Myc, MAP3K2, DUSP10, REL, MAPK8IP3, IRS1, MAP3K1 and C-jun.

References

External links

• MAP Kinase Resource .

Further reading

• Davis RJ (2000). "Signal transduction by the JNK group of MAP kinases". Cell 103 (2): 239–52. doi:10.1016/S0092-8674(00)00116-1. PMID 11057897.
• Liu J, Lin A (2007). "Wiring the cell signaling circuitry by the NF-kappa B and JNK1 crosstalk and its applications in human diseases". Oncogene 26 (22): 3267–78. doi:10.1038/sj.onc.1210417. PMID 17496921.

This article incorporates text from the United States National Library of Medicine, which is in the public domain.

UpToDate Contents

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• 1. 黒色腫（メラノーマ）の分子生物学 the molecular biology of melanoma
• 2. T細胞受容体シグナル伝達 t cell receptor signaling
• 3. リウマチ性疾患におけるサイトカインネットワーク：治療の意味 cytokine networks in rheumatic diseases implications for therapy
• 4. 進行黒色腫に対するマネージメントの概要 overview of the management of advanced melanoma
• 5. 進行非小細胞肺癌に対する遺伝子型による個別治療 personalized genotype directed therapy for advanced non small cell lung cancer

English Journal

• Involvement of autophagy induction in penta-1,2,3,4,6-O-galloyl-β-D-glucose-induced senescence-like growth arrest in human cancer cells.

• Dong Y1, Yin S2, Jiang C3, Luo X4, Guo X2, Zhao C2, Fan L5, Meng Y6, Lu J3, Song X2, Zhang X2, Chen N2, Hu H2.Author information 1Department of Nutrition and Health; College of Food Science and Nutritional Engineering; Beijing Key Laboratory of Functional Food from Plant Resources; China Agricultural University; Beijing, China; Department of Biomedical Sciences; Texas Tech University School of Pharmacy; Amarillo, TX USA.2Department of Nutrition and Health; College of Food Science and Nutritional Engineering; Beijing Key Laboratory of Functional Food from Plant Resources; China Agricultural University; Beijing, China.3Department of Biomedical Sciences; Texas Tech University School of Pharmacy; Amarillo, TX USA.4Department of Hepatobiliary Surgery; The First Affiliated Hospital; Harbin Medical University; Harbin, Heilongjiang China.5College of Veterinary Medicine; China Agricultural University; Beijing, China.6Nanyang Administration of Traditional Chinese Medicine; Nanyang, Henan China.AbstractGrowing evidence has demonstrated that autophagy plays important and paradoxical roles in carcinogenesis, while senescence is considered to be a crucial tumor-suppressor mechanism in cancer prevention and treatment. In the present study we demonstrated that both autophagy and senescence were induced in response to penta-1,2,3,4,6-O-galloyl-β-D-glucose (PGG), a chemopreventive polyphonolic compound, in multiple types of cancer cells. Analysis of these 2 events over the experimental time course indicated that autophagy and senescence occurred in parallel early in the process and dissociated later. The long-term culture study suggested that a subpopulation of senescent cells may have the capacity to reenter the cell cycle. Inhibition of autophagy by either a chemical inhibitor or RNA interference led to a significant reduction of PGG-induced senescence, followed by induction of apoptosis. These results suggested that autophagy promoted senescence induction by PGG and that PGG might exert its anticancer activity through autophagy-mediated senescence. For the first time, these findings uncovered the relationships among autophagy, senescence, and apoptosis induced by PGG. In addition, we identified that unfolded protein response signaling played a pivotal role in the autophagy-mediated senescence phenotype. Furthermore, our data showed that activation of MAPK8/9/10 (mitogen-activated protein kinase 8/9/10/c-Jun N-terminal kinases) was an essential upstream signal for PGG-induced autophagy. Finally, the key in vitro results were validated in vivo in a xenograft mouse model of human HepG2 liver cancer. Our findings provided novel insights into understanding the mechanisms and functions of PGG-induced autophagy and senescence in human cancer cells.
• Autophagy.Autophagy.2014 Feb;10(2):296-310. doi: 10.4161/auto.27210. Epub 2013 Dec 18.
• Growing evidence has demonstrated that autophagy plays important and paradoxical roles in carcinogenesis, while senescence is considered to be a crucial tumor-suppressor mechanism in cancer prevention and treatment. In the present study we demonstrated that both autophagy and senescence were induced
• PMID 24389959

• Intracellular mobility and nuclear trafficking of the stress-activated kinase JNK1 are impeded by hyperosmotic stress.

• Misheva M1, Kaur G2, Ngoei KR1, Yeap YY1, Ng IH3, Wagstaff KM4, Ng DC1, Jans DA4, Bogoyevitch MA5.Author information 1Department of Biochemistry and Molecular Biology, Bio21 Molecular Science and Biotechnology Institute, University of Melbourne, Victoria 3010, Australia.2Department of Biochemistry and Molecular Biology, Monash University, Victoria 3800, Australia; European Molecular Biology Laboratory (EMBL) Australia, Australian Regenerative Medicine Institute, Monash University, Clayton, Victoria 3800, Australia.3Department of Biochemistry and Molecular Biology, Bio21 Molecular Science and Biotechnology Institute, University of Melbourne, Victoria 3010, Australia; Department of Biochemistry and Molecular Biology, Monash University, Victoria 3800, Australia.4Department of Biochemistry and Molecular Biology, Monash University, Victoria 3800, Australia.5Department of Biochemistry and Molecular Biology, Bio21 Molecular Science and Biotechnology Institute, University of Melbourne, Victoria 3010, Australia. Electronic address: marieb@unimelb.edu.au.AbstractThe c-Jun N-terminal kinases (JNKs) are a group of stress-activated protein kinases that regulate gene expression changes through specific phosphorylation of nuclear transcription factor substrates. To address the mechanisms underlying JNK nuclear entry, we employed a semi-intact cell system to demonstrate for the first time that JNK1 nuclear entry is dependent on the importin α2/β1 heterodimer and independent of importins α3, α4, β2, β3, 7 and 13. However, quantitative image analysis of JNK1 localization following exposure of cells to either arsenite or hyperosmotic stress did not indicate its nuclear accumulation. Extending our analyses to define the dynamics of nuclear trafficking of JNK1, we combined live cell imaging analyses with fluorescence recovery after photobleaching (FRAP) protocols. Subnuclear and subcytoplasmic bleaching protocols revealed the slowed movement of JNK1 in both regions in response to hyperosmotic stress. Strikingly, while movement into the nucleus of green fluorescent protein (GFP) or transport of a GFP-T-antigen fusion protein as estimated by initial rates and time to reach half-maximal recovery (t1/2) measures remained unaltered, hyperosmotic stress slowed the nuclear entry of GFP-JNK1. In contrast, arsenite exposure which did not alter the initial rates of nuclear accumulation of GFP, GFP-T-antigen or GFP-JNK1, decreased the t1/2 for nuclear accumulation of both GFP and GFP-JNK1. Thus, our results challenge the paradigm of increased nuclear localization of JNK broadly in response to all forms of stress-activation and are consistent with enhanced interactions of stress-activated JNK1 with scaffold and substrate proteins throughout the nucleus and the cytosol under conditions of hyperosmotic stress.
• Biochimica et biophysica acta.Biochim Biophys Acta.2014 Feb;1843(2):253-64. doi: 10.1016/j.bbamcr.2013.10.017. Epub 2013 Nov 1.
• The c-Jun N-terminal kinases (JNKs) are a group of stress-activated protein kinases that regulate gene expression changes through specific phosphorylation of nuclear transcription factor substrates. To address the mechanisms underlying JNK nuclear entry, we employed a semi-intact cell system to demo
• PMID 24184208

• Natural feed contaminant zearalenone decreases the expressions of important pro- and anti-inflammatory mediators and mitogen-activated protein kinase/NF-κB signalling molecules in pigs.

• Pistol GC1, Gras MA1, Marin DE1, Israel-Roming F2, Stancu M1, Taranu I1.Author information 1Laboratory of Animal Biology, National Institute for Research and Development for Biology and Animal Nutrition, Calea Bucuresti No. 1, Balotesti, Ilfov 077015, Romania.2Biotechnology Department, University of Agriculture and Veterinary Medicine, Bulevardul Marasti No. 59, Bucharest 011464, Romania.AbstractZearalenone (ZEA) is an oestrogenic mycotoxin produced by Fusarium species, considered to be a risk factor from both public health and agricultural perspectives. In the present in vivo study, a feeding trial was conducted to evaluate the in vivo effect of a ZEA-contaminated diet on immune response in young pigs. The effect of ZEA on pro-inflammatory (TNF-α, IL-8, IL-6, IL-1β and interferon-γ) and anti-inflammatory (IL-10 and IL-4) cytokines and other molecules involved in inflammatory processes (matrix metalloproteinases (MMP)/tissue inhibitors of matrix metalloproteinases (TIMP), nuclear receptors: PPARγ and NF-κB1, mitogen-activated protein kinases (MAPK): mitogen-activated protein kinase kinase kinase 7 (TAK1)/mitogen-activated protein kinase 14 (p38α)/mitogen-activated protein kinase 8 (JNK1)/ mitogen-activated protein kinase 9 (JNK2)) in the liver of piglets was investigated. The present results showed that a concentration of 316 parts per billion ZEA leads to a significant decrease in the levels of pro- and anti-inflammatory cytokines at both gene expression and protein levels, correlated with a decrease in the levels of other inflammatory mediators, MMP and TIMP. The results also showed that dietary ZEA induces a dramatic reduction in the expressions of NF-κB1 and TAK1/p38α MAPK genes in the liver of the experimentally intoxicated piglets, and has no effect on the expression of PPARγ mRNA. The present results suggest that the toxic action of ZEA begins in the upstream of the MAPK signalling pathway by the inhibition of TAK1, a MAPK/NF-κB activator. In conclusion, the present study shows that ZEA alters several important parameters of the hepatic cellular immune response. From an economic point of view, these data suggest that, in pigs, ZEA is not only a powerful oestrogenic mycotoxin but also a potential hepatotoxin when administered through the oral route. Therefore, the present results represent additional data from cellular and molecular levels that could be taken into account in the determination of the regulation limit of the tolerance to ZEA.
• The British journal of nutrition.Br J Nutr.2014 Feb;111(3):452-64. doi: 10.1017/S0007114513002675. Epub 2013 Aug 20.
• Zearalenone (ZEA) is an oestrogenic mycotoxin produced by Fusarium species, considered to be a risk factor from both public health and agricultural perspectives. In the present in vivo study, a feeding trial was conducted to evaluate the in vivo effect of a ZEA-contaminated diet on immune response i
• PMID 23962703

Japanese Journal

• ROS Are Required for Mouse Spermatogonial Stem Cell Self-Renewal

• Morimoto Hiroko,Iwata Kazumi,Ogonuki Narumi,Inoue Kimiko,Ogura Atsuo,Kanatsu-Shinohara Mito,Morimoto Takeshi,Yabe-Nishimura Chihiro,Shinohara Takashi
• Cell Stem Cell 12(6), 774-786, 2013-06-00
• … SSCs depleted of ROS stopped proliferating, but they showed enhanced self-renewal when ROS levels were increased by the addition of hydrogen peroxide, which induced the phosphorylation of stress kinases p38 mitogen-activated protein kinase (MAPK) and c-jun N-terminal kinase (JNK). …
• NAID 120005285490

• Roles of FGF20 in dopaminergic neurons and Parkinson's disease.

• Itoh Nobuyuki,Ohta Hiroya
• Frontiers in molecular neuroscience 6, 2013-05-00
• … Fgf20, which acts on proximal cells, significantly enhanced the survival of cultured dopaminergic neurons by activating the mitogen-activated protein kinase (MAPK) pathway through Fgf receptor 1c. …
• NAID 120005289845

• Central role of the exchange factor GEF-H1 in TNF-α–induced sequential activation of Rac, ADAM17/TACE, and RhoA in tubular epithelial cells

• Waheed Faiza,Dan Qinghong,Amoozadeh Yasaman,Zhang Yuqian,Tanimura Susumu,Speight Pam,Kapus András,Szászi Katalin
• Molecular Biology of the Cell 24(7), 1068-1082, 2013-04-01
• … TACE activation requires the mitogen-activated protein kinase p38, which is activated through the small GTPase Rac. …
• NAID 120005231330

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リンク元	「マイトジェン活性化プロテインキナーゼ8」
関連記事	「activated」「activate」「kinase」「protein kinase」

「マイトジェン活性化プロテインキナーゼ8」

　　[★]

英

mitogen-activated protein kinase 8

「activated」

　　[★]

• adj.

• 活性化の、活性化型の、賦活化の

関

activate、activated form、activation、turn on

　 　 　 　

「activate」

　　[★]

• v.

• 活性化する、賦活化する、賦活する

関

activated、activation、turn on

　 　 　 　 　

「kinase」

　　[★] キナーゼ カイネース リン酸化酵素 phosphoenzyme phosphotransferase 　

「protein kinase」

　　[★] プロテインキナーゼ

同

protein kinases