- 関
- extracellular signal-regulated kinase 5
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出典(authority):フリー百科事典『ウィキペディア(Wikipedia)』「2013/03/10 15:18:08」(JST)
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Main article: Mitogen-activated protein kinase
Mitogen-activated protein kinase 7 |
Available structures |
PDB |
Ortholog search: PDBe, RCSB |
List of PDB id codes |
4B99, 4IC7, 4IC8
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Identifiers |
Symbols |
MAPK7; BMK1; ERK4; ERK5; PRKM7 |
External IDs |
OMIM: 602521 MGI: 1346347 HomoloGene: 2060 ChEMBL: 5332 GeneCards: MAPK7 Gene |
EC number |
2.7.11.24 |
Gene Ontology |
Molecular function |
• MAP kinase activity
• protein binding
• ATP binding
• mitogen-activated protein kinase binding
|
Cellular component |
• nucleus
• nucleoplasm
• cytosol
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Biological process |
• toll-like receptor signaling pathway
• MyD88-dependent toll-like receptor signaling pathway
• MyD88-independent toll-like receptor signaling pathway
• apoptotic process
• cell cycle
• signal transduction
• Toll signaling pathway
• peptidyl-serine phosphorylation
• cell differentiation
• negative regulation of heterotypic cell-cell adhesion
• 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
• positive regulation of transcription from RNA polymerase II promoter in response to stress
• negative regulation of apoptotic process
• innate immune response
• regulation of angiogenesis
• positive regulation of transcription from RNA polymerase II promoter
• protein autophosphorylation
• nerve growth factor receptor signaling pathway
• negative regulation of inflammatory response
• positive regulation of protein metabolic process
• stress-activated MAPK cascade
• negative regulation of NFAT protein import into nucleus
• negative regulation of cell death
• negative regulation of response to cytokine stimulus
• cellular response to hydrogen peroxide
• ERK5 cascade
• cellular response to growth factor stimulus
• cellular response to laminar fluid shear stress
• cellular response to transforming growth factor beta stimulus
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Sources: Amigo / QuickGO |
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RNA expression pattern |
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More reference expression data |
Orthologs |
Species |
Human |
Mouse |
|
Entrez |
5598 |
23939 |
|
Ensembl |
ENSG00000166484 |
ENSMUSG00000001034 |
|
UniProt |
Q13164 |
Q9WVS8 |
|
RefSeq (mRNA) |
NM_002749 |
NM_011841 |
|
RefSeq (protein) |
NP_002740 |
NP_035971 |
|
Location (UCSC) |
Chr 17:
19.28 – 19.29 Mb |
Chr 11:
61.49 – 61.49 Mb |
|
PubMed search |
[1] |
[2] |
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Mitogen-activated protein kinase 7 also known as MAP kinase 7 is an enzyme that in humans is encoded by the MAPK7 gene.[1][2]
Contents
- 1 Function
- 2 Interactions
- 3 References
- 4 External links
- 5 Further reading
|
Function
MAPK7 is a member of the MAP kinase 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 specifically activated by mitogen-activated protein kinase kinase 5 (MAP2K5/MEK5). It is involved in the downstream signaling processes of various receptor molecules including receptor tyrosine kinases, and G protein-coupled receptors. In response to extracellular signals, this kinase translocates to the cell nucleus, where it regulates gene expression by phosphorylating, and activating different transcription factors. Four alternatively spliced transcript variants of this gene encoding two distinct isoforms have been reported.[3]
MAPK7 is also critical for cardiovascular development [4] and is essential for endothelial cell function.[5] [6]
Interactions
MAPK7 has been shown to interact with SGK,[7] MEF2C,[8] YWHAB,[9] MEF2D,[8] C-Raf,[10] PTPRR,[11] Gap junction protein, alpha 1[12] and MAP2K5.[2]
References
- ^ Purandare SM, Lee JD, Patel PI (Mar 1999). "Assignment of big MAP kinase (PRKM7) to human chromosome 17 band p11.2 with somatic cell hybrids". Cytogenet Cell Genet 83 (3–4): 258–9. doi:10.1159/000015199. PMID 10072598.
- ^ a b Zhou G, Bao ZQ, Dixon JE (Jun 1995). "Components of a new human protein kinase signal transduction pathway". J Biol Chem 270 (21): 12665–9. doi:10.1074/jbc.270.21.12665. PMID 7759517.
- ^ "Entrez Gene: MAPK7 mitogen-activated protein kinase 7". http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5598.
- ^ Hayashi M, Lee JD. (Oct 2004). "Role of the BMK1/ERK5 signaling pathway: lessons from knockout mice". J Mol Med. 82 (12): 800–8. doi:10.1007/s00109-004-0602-8. PMID 15517128.
- ^ Roberts OL, Holmes K, Müller J, Cross DA, Cross MJ. (Dec 2009). "ERK5 and the regulation of endothelial cell function". Biochem Soc Trans. 37 (6): 1254–9. doi:10.1042/BST0371254. PMID 19909257.
- ^ Roberts OL, Holmes K, Müller J, Cross DA, Cross MJ. (Sept 2010). "ERK5 is required for VEGF-mediated survival and tubular morphogenesis of primary human microvascular endothelial cells". J Cell Sci. 123 (18): 3189–3200. doi:10.1242/jcs.072801. PMID 20736307.
- ^ Hayashi, M; Tapping R I, Chao T H, Lo J F, King C C, Yang Y, Lee J D (Mar. 2001). "BMK1 mediates growth factor-induced cell proliferation through direct cellular activation of serum and glucocorticoid-inducible kinase". J. Biol. Chem. (United States) 276 (12): 8631–4. doi:10.1074/jbc.C000838200. ISSN 0021-9258. PMID 11254654.
- ^ a b Yang, C C; Ornatsky O I, McDermott J C, Cruz T F, Prody C A (Oct. 1998). "Interaction of myocyte enhancer factor 2 (MEF2) with a mitogen-activated protein kinase, ERK5/BMK1". Nucleic Acids Res. (ENGLAND) 26 (20): 4771–7. doi:10.1093/nar/26.20.4771. ISSN 0305-1048. PMC 147902. PMID 9753748. //www.ncbi.nlm.nih.gov/pmc/articles/PMC147902/.
- ^ Zheng, Qinlei; Yin Guoyong, Yan Chen, Cavet Megan, Berk Bradford C (Mar. 2004). "14-3-3beta binds to big mitogen-activated protein kinase 1 (BMK1/ERK5) and regulates BMK1 function". J. Biol. Chem. (United States) 279 (10): 8787–91. doi:10.1074/jbc.M310212200. ISSN 0021-9258. PMID 14679215.
- ^ English, J M; Pearson G, Hockenberry T, Shivakumar L, White M A, Cobb M H (Oct. 1999). "Contribution of the ERK5/MEK5 pathway to Ras/Raf signaling and growth control". J. Biol. Chem. (UNITED STATES) 274 (44): 31588–92. doi:10.1074/jbc.274.44.31588. ISSN 0021-9258. PMID 10531364.
- ^ Buschbeck, Marcus; Eickhoff Jan, Sommer Marc N, Ullrich Axel (Aug. 2002). "Phosphotyrosine-specific phosphatase PTP-SL regulates the ERK5 signaling pathway". J. Biol. Chem. (United States) 277 (33): 29503–9. doi:10.1074/jbc.M202149200. ISSN 0021-9258. PMID 12042304.
- ^ Cameron, Scott J; Malik Sundeep, Akaike Masashi, Lerner-Marmarosh Nicole, Yan Chen, Lee Jiing-Dwan, Abe Jun-Ichi, Yang Jay (May. 2003). "Regulation of epidermal growth factor-induced connexin 43 gap junction communication by big mitogen-activated protein kinase1/ERK5 but not ERK1/2 kinase activation". J. Biol. Chem. (United States) 278 (20): 18682–8. doi:10.1074/jbc.M213283200. ISSN 0021-9258. PMID 12637502.
External links
Further reading
- Lee JD, Ulevitch RJ, Han J (1995). "Primary structure of BMK1: a new mammalian map kinase". Biochem. Biophys. Res. Commun. 213 (2): 715–24. doi:10.1006/bbrc.1995.2189. PMID 7646528.
- Warn-Cramer BJ, Lampe PD, Kurata WE, et al. (1996). "Characterization of the mitogen-activated protein kinase phosphorylation sites on the connexin-43 gap junction protein". J. Biol. Chem. 271 (7): 3779–86. doi:10.1074/jbc.271.7.3779. PMID 8631994.
- Kato Y, Kravchenko VV, Tapping RI, et al. (1998). "BMK1/ERK5 regulates serum-induced early gene expression through transcription factor MEF2C". EMBO J. 16 (23): 7054–66. doi:10.1093/emboj/16.23.7054. PMC 1170308. PMID 9384584. //www.ncbi.nlm.nih.gov/pmc/articles/PMC1170308/.
- English JM, Pearson G, Baer R, Cobb MH (1998). "Identification of substrates and regulators of the mitogen-activated protein kinase ERK5 using chimeric protein kinases". J. Biol. Chem. 273 (7): 3854–60. doi:10.1074/jbc.273.7.3854. PMID 9461566.
- Grunwald ME, Yu WP, Yu HH, Yau KW (1998). "Identification of a domain on the beta-subunit of the rod cGMP-gated cation channel that mediates inhibition by calcium-calmodulin". J. Biol. Chem. 273 (15): 9148–57. doi:10.1074/jbc.273.15.9148. PMID 9535905.
- Warn-Cramer BJ, Cottrell GT, Burt JM, Lau AF (1998). "Regulation of connexin-43 gap junctional intercellular communication by mitogen-activated protein kinase". J. Biol. Chem. 273 (15): 9188–96. doi:10.1074/jbc.273.15.9188. PMID 9535909.
- Yang CC, Ornatsky OI, McDermott JC, et al. (1998). "Interaction of myocyte enhancer factor 2 (MEF2) with a mitogen-activated protein kinase, ERK5/BMK1". Nucleic Acids Res. 26 (20): 4771–7. doi:10.1093/nar/26.20.4771. PMC 147902. PMID 9753748. //www.ncbi.nlm.nih.gov/pmc/articles/PMC147902/.
- Kato Y, Tapping RI, Huang S, et al. (1998). "Bmk1/Erk5 is required for cell proliferation induced by epidermal growth factor". Nature 395 (6703): 713–6. doi:10.1038/27234. PMID 9790194.
- Zhao M, New L, Kravchenko VV, et al. (1999). "Regulation of the MEF2 family of transcription factors by p38". Mol. Cell. Biol. 19 (1): 21–30. PMC 83862. PMID 9858528. //www.ncbi.nlm.nih.gov/pmc/articles/PMC83862/.
- Kamakura S, Moriguchi T, Nishida E (1999). "Activation of the protein kinase ERK5/BMK1 by receptor tyrosine kinases. Identification and characterization of a signaling pathway to the nucleus". J. Biol. Chem. 274 (37): 26563–71. doi:10.1074/jbc.274.37.26563. PMID 10473620.
- English JM, Pearson G, Hockenberry T, et al. (1999). "Contribution of the ERK5/MEK5 pathway to Ras/Raf signaling and growth control". J. Biol. Chem. 274 (44): 31588–92. doi:10.1074/jbc.274.44.31588. PMID 10531364.
- Fukuhara S, Marinissen MJ, Chiariello M, Gutkind JS (2000). "Signaling from G protein-coupled receptors to ERK5/Big MAPK 1 involves Galpha q and Galpha 12/13 families of heterotrimeric G proteins. Evidence for the existence of a novel Ras AND Rho-independent pathway". J. Biol. Chem. 275 (28): 21730–6. doi:10.1074/jbc.M002410200. PMID 10781600.
- Kato Y, Zhao M, Morikawa A, et al. (2000). "Big mitogen-activated kinase regulates multiple members of the MEF2 protein family". J. Biol. Chem. 275 (24): 18534–40. doi:10.1074/jbc.M001573200. PMID 10849446.
- Yan C, Luo H, Lee JD, et al. (2001). "Molecular cloning of mouse ERK5/BMK1 splice variants and characterization of ERK5 functional domains". J. Biol. Chem. 276 (14): 10870–8. doi:10.1074/jbc.M009286200. PMID 11139578.
- Hayashi M, Tapping RI, Chao TH, et al. (2001). "BMK1 mediates growth factor-induced cell proliferation through direct cellular activation of serum and glucocorticoid-inducible kinase". J. Biol. Chem. 276 (12): 8631–4. doi:10.1074/jbc.C000838200. PMID 11254654.
- Dong F, Gutkind JS, Larner AC (2001). "Granulocyte colony-stimulating factor induces ERK5 activation, which is differentially regulated by protein-tyrosine kinases and protein kinase C. Regulation of cell proliferation and survival". J. Biol. Chem. 276 (14): 10811–6. doi:10.1074/jbc.M008748200. PMID 11278431.
- Watson FL, Heerssen HM, Bhattacharyya A, et al. (2001). "Neurotrophins use the Erk5 pathway to mediate a retrograde survival response". Nat. Neurosci. 4 (10): 981–8. doi:10.1038/nn720. PMID 11544482.
- Esparís-Ogando A, Díaz-Rodríguez E, Montero JC, et al. (2002). "Erk5 participates in neuregulin signal transduction and is constitutively active in breast cancer cells overexpressing ErbB2". Mol. Cell. Biol. 22 (1): 270–85. doi:10.1128/MCB.22.1.270-285.2002. PMC 134212. PMID 11739740. //www.ncbi.nlm.nih.gov/pmc/articles/PMC134212/.
English Journal
- Modulation of ERK5 Is a Novel Mechanism by Which Cdc42 Regulates Migration of Breast Cancer Cells.
- Zuo Y1, Wu Y, Wehrli B, Chakrabarti S, Chakraborty C.
- Journal of cellular biochemistry.J Cell Biochem.2015 Jan;116(1):124-32. doi: 10.1002/jcb.24950.
- Members of Rho family GTPases including Cdc42 are known to play pivotal roles in cell migration. Cell migration is also known to be regulated by many protein kinases. Kinetworks KPSS 11.0 phospho-site screening of Cdc42-silenced Hs578T breast cancer cells revealed most dramatic change in ERK5 MAP ki
- PMID 25160664
- Tumor suppressors miRNA-143 and miR-145 and predicted target proteins API5, ERK5, KRAS, and IRS-1 are differentially expressed in proximal and distal colon.
- Pekow J1, Meckel K2, Dougherty U2, Butun F2, Mustafi R2, Lim J2, Crofton C2, Chen X2, Joseph LJ2, Bissonnette M3.
- American journal of physiology. Gastrointestinal and liver physiology.Am J Physiol Gastrointest Liver Physiol.2014 Dec 4:ajpgi.00208.2014. doi: 10.1152/ajpgi.00208.2014. [Epub ahead of print]
- The colon differs regionally in local luminal environment, excretory function, and gene expression. Polycistronic miR-143 and miR-145 are down-regulated early in colon cancer. We asked if these miRNA might be differentially expressed in the proximal versus the distal colon, contributing to regional
- PMID 25477374
- A place and a grid in the sun.
- Kandel E.
- Cell.Cell.2014 Dec 4;159(6):1239-42. doi: 10.1016/j.cell.2014.11.033.
- The 2014 Nobel Prize in Physiology or Medicine, awarded to John O'Keefe, May-Britt Moser, and Edvard I. Moser, recognizes the first deep-brain insights into a cognitive function. Their insights established a new view for how the brain represents spatial location. Copyright © 2014 Elsevier Inc. All
- PMID 25480286
Japanese Journal
- Disturbed-Flow-Mediated Vascular Reactive Oxygen Species Induce Endothelial Dysfunction
- Heo Kyung-Sun,Fujiwara Keigi,Abe Jun-ichi
- Circulation Journal 75(12), 2722-2730, 2011
- … Here, we propose a new signaling pathway involving d-flow-induced EC inflammation via PKCζ-ERK5 interaction-mediated downregulation of KLF2/eNOS stability, which leads to PKCζ-mediated p53-SUMOylation and EC apoptosis. …
- NAID 130001275744
- Big Mitogen-Activated Protein Kinase 1 Protects Cultured Rat Aortic Smooth Muscle Cells From Oxidative Damage
- Zhao Jing,Kyotani Yoji,Itoh Satoyasu,Nakayama Hitoshi,Isosaki Minoru,Yoshizumi Masanori
- Journal of Pharmacological Sciences 116(2), 173-180, 2011
- … Big mitogen-activated protein kinase-1 / extracellular signal–regulated kinase 5 (BMK1/ERK5) is a newly identified member of the mitogen-activated protein kinases family. … Like Src tyrosine kinase, BMK1/ERK5 is known to be sensitive to oxidative stress; …
- NAID 130000835861
Related Links
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- 米国CST社の日本法人CSTジャパン株式会社【公式サイト】Erk5 Antibodyページ。高品質の研究用試薬、米国本社の開発研究者による技術的サポートをご提供しております。
- 1.筋分化におけるERK1/2経路ならびにERK5経路の機能 MAPキナーゼ経路は進化において高度に保存された細胞内シグナル伝達経路であり,細胞外からの刺激と核での遺伝子発現の変化を結びつけることに必須の役割をはたしている 4,5) ...
Related Pictures
★リンクテーブル★
[★]
- 英
- MAP kinase, mitogen-activated protein kinase, MAPK
- 同
- マイトジェン活性化プロテインキナーゼ、マップキナーゼ
- 関
- MAPキナーゼスーパーファミリーカスケード。mitogen-activated protein
[★]
- ERK1/ERK2:非リン酸化配列(TEY)
- ストレス応答MAPK:高浸透圧・過酸化水素、熱ショック、タンパク質合成阻害、紫外線、放射線、抗ガン剤、虚血/再灌流・血清除去、LPS、炎症性サイトカイン、TGF-β、Fas
- JNK1/JNK2/JNK3:非リン酸化配列(TPY)
- p38α/p38β/p38γ/p38δ:非リン酸化配列(TGY)
[★]
- 英
- extracellular signal-regulated kinase 5、ERK5
- 関
- マイトジェン活性化プロテインキナーゼ7
[★]
細胞外シグナル制御キナーゼ5
- 関
- ERK5、mitogen-activated protein kinase 7
[★]
- 同
- [[]] extracellular-signal-regulated kinase
- 関
- MAPキナーゼスーパーファミリーカスケード
- MAPKファミリーに含まれるERKファミリーを構成
- キナーゼサブドメインVIIIの活性化ループに存在するリン酸化部位の配列がTEY
- セリンスレオニンキナーゼ
- MAPKKであるMEK1,MEK2によってスレオニンとチロシン残基がリン酸化され、活性化される。
- ERK1/2の基質
- 同
- extracellular-signal-regulated kinase
[★]