MAP3K2
MAP3K2| MAP3K2 | |||||||||||||||||||||||||
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| 별칭 | MAP3K2, MEKK2, MEK2B, 미토겐 활성 단백질 키나제 키나제 키나제2 | ||||||||||||||||||||||||
| 외부 ID | OMIM: 609487 MGI: 1346873 HomoloGene: 74576 GeneCard: MAP3K2 | ||||||||||||||||||||||||
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| 직교체 | |||||||||||||||||||||||||
| 종 | 인간 | 마우스 | |||||||||||||||||||||||
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| 앙상블 | |||||||||||||||||||||||||
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| RefSeq(mRNA) | |||||||||||||||||||||||||
| RefSeq(단백질) | |||||||||||||||||||||||||
| 위치(UCSC) | Chr 2: 127.3 – 127.39Mb | Cr 18: 32.3 – 32.37Mb | |||||||||||||||||||||||
| PubMed 검색 | [3] | [4] | |||||||||||||||||||||||
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MEKK2(Mitgene-actived Statene Kinase Kinase 2)로도 알려진 미토겐활성 단백질 키나제 2는 인간에서 MAP3K2 유전자에 의해 암호화된 효소다.[5][6][7]
함수
이 유전자에 의해 인코딩된 단백질은 세린/트레오닌 단백질 키나아제 계열의 일원이다.이 키나제는 MAP 키나제 신호 경로에 관련된 다른 키나제를 우선적으로 활성화한다.이 키나제는 IkappaB 키나제를 직접 인산화하여 활성화하는 것으로 보여져 NF-kappa B 신호 경로에 역할을 한다.이 키나아제는 또한 단백질 키나아제 C 관련 키나아제 2를 결합하고 활성화시키는 것으로 밝혀졌는데, 이는 규제된 신호 과정에 관여함을 시사한다.[7]
활성화
MEKK2는 MEK2-S519에서 호모디머화와 후속 트랜스인산화를 통해 활성화된다.[8][9]
MEKK2는 MEK2-phosphoT283과 결합하는 14-3-3 단백질에 의해 조절된다.[10]
MEK2는 MEK2-K260을 바인딩 및 메틸레이트하는 SMYD3에 의해 규제된다.[11]
상호작용
MAP3K2는 다음과 상호 작용하는 것으로 나타났다.
참조
- ^ a b c GRCh38: 앙상블 릴리스 89: ENSG00000169967 - 앙상블, 2017년 5월
- ^ a b c GRCm38: 앙상블 릴리스 89: ENSMUSG000024383 - 앙상블, 2017년 5월
- ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
- ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
- ^ Blank JL, Gerwins P, Elliott EM, Sather S, Johnson GL (Mar 1996). "Molecular cloning of mitogen-activated protein/ERK kinase kinases (MEKK) 2 and 3. Regulation of sequential phosphorylation pathways involving mitogen-activated protein kinase and c-Jun kinase". The Journal of Biological Chemistry. 271 (10): 5361–8. doi:10.1074/jbc.271.10.5361. PMID 8621389.
- ^ Zhao Q, Lee FS (Mar 1999). "Mitogen-activated protein kinase/ERK kinase kinases 2 and 3 activate nuclear factor-kappaB through IkappaB kinase-alpha and IkappaB kinase-beta". The Journal of Biological Chemistry. 274 (13): 8355–8. doi:10.1074/jbc.274.13.8355. PMID 10085062.
- ^ a b "Entrez Gene: MAP3K2 mitogen-activated protein kinase kinase kinase 2".
- ^ Cheng, Jinke; Yu, Ling; Zhang, Dongyu; Huang, Qiaojia; Spencer, David; Su, Bing (2005-04-08). "Dimerization through the Catalytic Domain Is Essential for MEKK2 Activation". Journal of Biological Chemistry. 280 (14): 13477–13482. doi:10.1074/jbc.M414258200. ISSN 0021-9258. PMID 15695508.
- ^ Zhang, Dongyu; Facchinetti, Valeria; Wang, Xiaofang; Huang, Qiaojia; Qin, Jun; Su, Bing (2006-01-11). "Identification of MEKK2/3 serine phosphorylation site targeted by the Toll-like receptor and stress pathways". The EMBO Journal. 25 (1): 97–107. doi:10.1038/sj.emboj.7600913. ISSN 0261-4189. PMC 1356356. PMID 16362041.
- ^ Matitau, Adi E.; Gabor, Timothy V.; Gill, R. Montgomery; Scheid, Michael P. (2013-09-27). "MEKK2 kinase association with 14-3-3 protein regulates activation of c-Jun N-terminal kinase". The Journal of Biological Chemistry. 288 (39): 28293–28302. doi:10.1074/jbc.M113.511352. ISSN 1083-351X. PMC 3784737. PMID 23963453.
- ^ a b Mazur, Pawel K.; Reynoird, Nicolas; Khatri, Purvesh; Jansen, Pascal W. T. C.; Wilkinson, Alex W.; Liu, Shichong; Barbash, Olena; Van Aller, Glenn S.; Huddleston, Michael; Dhanak, Dashyant; Tummino, Peter J. (June 2014). "SMYD3 links lysine methylation of MAP3K2 to Ras-driven cancer". Nature. 510 (7504): 283–287. Bibcode:2014Natur.510..283M. doi:10.1038/nature13320. ISSN 1476-4687. PMC 4122675. PMID 24847881.
- ^ a b Cheng J, Yang J, Xia Y, Karin M, Su B (Apr 2000). "Synergistic interaction of MEK kinase 2, c-Jun N-terminal kinase (JNK) kinase 2, and JNK1 results in efficient and specific JNK1 activation". Molecular and Cellular Biology. 20 (7): 2334–42. doi:10.1128/mcb.20.7.2334-2342.2000. PMC 85399. PMID 10713157.
- ^ Deacon, K.; Blank, J. L. (1997-05-30). "Characterization of the mitogen-activated protein kinase kinase 4 (MKK4)/c-Jun NH2-terminal kinase 1 and MKK3/p38 pathways regulated by MEK kinases 2 and 3. MEK kinase 3 activates MKK3 but does not cause activation of p38 kinase in vivo". The Journal of Biological Chemistry. 272 (22): 14489–14496. doi:10.1074/jbc.272.22.14489. ISSN 0021-9258. PMID 9162092.
- ^ a b Sun W, Kesavan K, Schaefer BC, Garrington TP, Ware M, Johnson NL, Gelfand EW, Johnson GL (Feb 2001). "MEKK2 associates with the adapter protein Lad/RIBP and regulates the MEK5-BMK1/ERK5 pathway". The Journal of Biological Chemistry. 276 (7): 5093–100. doi:10.1074/jbc.M003719200. PMID 11073940.
- ^ Fanger, Gary R.; Widmann, Christian; Porter, Amy C.; Sather, Sue; Johnson, Gary L.; Vaillancourt, Richard R. (1998-02-06). "14-3-3 Proteins Interact with Specific MEK Kinases". Journal of Biological Chemistry. 273 (6): 3476–3483. doi:10.1074/jbc.273.6.3476. ISSN 0021-9258. PMID 9452471.
- ^ Winsauer G, Resch U, Hofer-Warbinek R, Schichl YM, de Martin R (Nov 2008). "XIAP regulates bi-phasic NF-kappaB induction involving physical interaction and ubiquitination of MEKK2". Cellular Signalling. 20 (11): 2107–12. doi:10.1016/j.cellsig.2008.08.004. PMID 18761086.
추가 읽기
- Yan M, Dai T, Deak JC, Kyriakis JM, Zon LI, Woodgett JR, Templeton DJ (1995). "Activation of stress-activated protein kinase by MEKK1 phosphorylation of its activator SEK1". Nature. 372 (6508): 798–800. doi:10.1038/372798a0. PMID 7997270. S2CID 4369739.
- Wu Z, Wu J, Jacinto E, Karin M (Dec 1997). "Molecular cloning and characterization of human JNKK2, a novel Jun NH2-terminal kinase-specific kinase". Molecular and Cellular Biology. 17 (12): 7407–16. doi:10.1128/mcb.17.12.7407. PMC 232596. PMID 9372971.
- Fanger GR, Widmann C, Porter AC, Sather S, Johnson GL, Vaillancourt RR (Feb 1998). "14-3-3 proteins interact with specific MEK kinases". The Journal of Biological Chemistry. 273 (6): 3476–83. doi:10.1074/jbc.273.6.3476. PMID 9452471.
- Cheng J, Yang J, Xia Y, Karin M, Su B (Apr 2000). "Synergistic interaction of MEK kinase 2, c-Jun N-terminal kinase (JNK) kinase 2, and JNK1 results in efficient and specific JNK1 activation". Molecular and Cellular Biology. 20 (7): 2334–42. doi:10.1128/MCB.20.7.2334-2342.2000. PMC 85399. PMID 10713157.
- Sun W, Vincent S, Settleman J, Johnson GL (Aug 2000). "MEK kinase 2 binds and activates protein kinase C-related kinase 2. Bifurcation of kinase regulatory pathways at the level of an MAPK kinase kinase". The Journal of Biological Chemistry. 275 (32): 24421–8. doi:10.1074/jbc.M003148200. PMID 10818102.
- Garrington TP, Ishizuka T, Papst PJ, Chayama K, Webb S, Yujiri T, Sun W, Sather S, Russell DM, Gibson SB, Keller G, Gelfand EW, Johnson GL (Oct 2000). "MEKK2 gene disruption causes loss of cytokine production in response to IgE and c-Kit ligand stimulation of ES cell-derived mast cells". The EMBO Journal. 19 (20): 5387–95. doi:10.1093/emboj/19.20.5387. PMC 314024. PMID 11032806.
- Huang J, Tu Z, Lee FS (Apr 2003). "Mutations in protein kinase subdomain X differentially affect MEKK2 and MEKK1 activity". Biochemical and Biophysical Research Communications. 303 (2): 532–40. doi:10.1016/S0006-291X(03)00387-5. PMID 12659851.
- Nakamura K, Johnson GL (Sep 2003). "PB1 domains of MEKK2 and MEKK3 interact with the MEK5 PB1 domain for activation of the ERK5 pathway". The Journal of Biological Chemistry. 278 (39): 36989–92. doi:10.1074/jbc.C300313200. PMID 12912994.
- Hammaker DR, Boyle DL, Chabaud-Riou M, Firestein GS (Feb 2004). "Regulation of c-Jun N-terminal kinase by MEKK-2 and mitogen-activated protein kinase kinase kinases in rheumatoid arthritis". Journal of Immunology. 172 (3): 1612–8. doi:10.4049/jimmunol.172.3.1612. PMID 14734742.
- Raviv Z, Kalie E, Seger R (Apr 2004). "MEK5 and ERK5 are localized in the nuclei of resting as well as stimulated cells, while MEKK2 translocates from the cytosol to the nucleus upon stimulation". Journal of Cell Science. 117 (Pt 9): 1773–84. doi:10.1242/jcs.01040. PMID 15075238.
- Jin J, Smith FD, Stark C, Wells CD, Fawcett JP, Kulkarni S, Metalnikov P, O'Donnell P, Taylor P, Taylor L, Zougman A, Woodgett JR, Langeberg LK, Scott JD, Pawson T (Aug 2004). "Proteomic, functional, and domain-based analysis of in vivo 14-3-3 binding proteins involved in cytoskeletal regulation and cellular organization". Current Biology. 14 (16): 1436–50. doi:10.1016/j.cub.2004.07.051. PMID 15324660. S2CID 2371325.
- Benzinger A, Muster N, Koch HB, Yates JR, Hermeking H (Jun 2005). "Targeted proteomic analysis of 14-3-3 sigma, a p53 effector commonly silenced in cancer". Molecular & Cellular Proteomics. 4 (6): 785–95. doi:10.1074/mcp.M500021-MCP200. PMID 15778465.
- Cheng J, Zhang D, Kim K, Zhao Y, Zhao Y, Su B (Jul 2005). "Mip1, an MEKK2-interacting protein, controls MEKK2 dimerization and activation". Molecular and Cellular Biology. 25 (14): 5955–64. doi:10.1128/MCB.25.14.5955-5964.2005. PMC 1168836. PMID 15988011.
- Pelkmans L, Zerial M (Jul 2005). "Kinase-regulated quantal assemblies and kiss-and-run recycling of caveolae". Nature. 436 (7047): 128–33. Bibcode:2005Natur.436..128P. doi:10.1038/nature03866. PMID 16001074. S2CID 4309375.
- Wissing J, Jänsch L, Nimtz M, Dieterich G, Hornberger R, Kéri G, Wehland J, Daub H (Mar 2007). "Proteomics analysis of protein kinases by target class-selective prefractionation and tandem mass spectrometry". Molecular & Cellular Proteomics. 6 (3): 537–47. doi:10.1074/mcp.T600062-MCP200. PMID 17192257.
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