MAP3K1
| Mitogen-aktivirana protein kinaza kinaza kinaza 1 | |||
|---|---|---|---|
| Identifikatori | |||
| Simboli | MAP3K1; MAPKKK1; MEKK; MEKK1 | ||
| Vanjski ID | OMIM: 600982 MGI: 1346872 HomoloGene: 8056 GeneCards: MAP3K1 Gene | ||
| Pregled RNK izražavanja | |||
 | |||
| podaci | |||
| Ortolozi | |||
| Vrsta | Čovek | Miš | |
| Entrez | 4214 | 26401 | |
| Ensembl | ENSG00000095015 | n/a | |
| UniProt | Q13233 | n/a | |
| RefSeq (mRNA) | XM_001128827 | NM_011945 | |
| RefSeq (protein) | XP_001128827 | NP_036075 | |
| Lokacija (UCSC) |
Chr 5: 56.15 - 56.23 Mb | n/a | |
| PubMed pretraga | [1] | [2] | |
Mitogen-aktivirana protein kinaza kinaza kinaza 1 je enzim koji je kod ljudi kodiran MAP3K1 genom.[1][2]
MAP3K, ili MEK kinaza, je serin/treonin kinaza koja ima ključnu ulogu u mreži enzima fosforilacije koji integrišu ćelijske odgovore na brojne mitogene i metaboličke stimuluse, uključujući insulin (MIM 176730) i mnoge faktore rasta.[2]
Genetika miša je ustanovila da je ova kinaza važna u: korektnoj embriogenezi, keratinocit migraciji, T ćelijskoj citokinskoj produkciji i B ćelijskoj produkciji antitela.
Interakcije[уреди | уреди извор]
Za MAP3K1 je bilo pokazano da interaguje sa C-Raf,[3] MAPK8,[4] TRAF2,[5] MAP2K1,[3] Grb2,[6] MAPK1,[3] AXIN1[7][8] i UBE2I.[9]
Reference[уреди | уреди извор]
- ^ Vinik BS, Kay ES, Fiedorek FT Jr (1996). „Mapping of the MEK kinase gene (Mekk) to mouse chromosome 13 and human chromosome 5”. Mamm Genome. 6 (11): 782—3. PMID 8597633.
- ^ а б „Entrez Gene: MAP3K1 mitogen-activated protein kinase kinase kinase 1”.
- ^ а б в Karandikar, M; Xu S; Cobb M H (2000). „MEKK1 binds raf-1 and the ERK2 cascade components”. J. Biol. Chem. UNITED STATES. 275 (51): 40120—7. ISSN 0021-9258. PMID 10969079. doi:10.1074/jbc.M005926200.
- ^ Xu, S; Cobb M H (1997). „MEKK1 binds directly to the c-Jun N-terminal kinases/stress-activated protein kinases”. J. Biol. Chem. UNITED STATES. 272 (51): 32056—60. ISSN 0021-9258. PMID 9405400.
- ^ Baud, V; Liu Z G; et al. (1999). „Signaling by proinflammatory cytokines: oligomerization of TRAF2 and TRAF6 is sufficient for JNK and IKK activation and target gene induction via an amino-terminal effector domain”. Genes Dev. UNITED STATES. 13 (10): 1297—308. ISSN 0890-9369. PMC 316725
. PMID 10346818.
- ^ Pomérance, M; Multon M C; et al. (1998). „Grb2 interaction with MEK-kinase 1 is involved in regulation of Jun-kinase activities in response to epidermal growth factor”. J. Biol. Chem. UNITED STATES. 273 (38): 24301—4. ISSN 0021-9258. PMID 9733714.
- ^ Zhang, Yi; Qiu Wen-Jie; et al. (2002). „Casein kinase I and casein kinase II differentially regulate axin function in Wnt and JNK pathways”. J. Biol. Chem. United States. 277 (20): 17706—12. ISSN 0021-9258. PMID 11884395. doi:10.1074/jbc.M111982200.
- ^ Zhang, Y; Neo S Y; et al. (2000). „Dimerization choices control the ability of axin and dishevelled to activate c-Jun N-terminal kinase/stress-activated protein kinase”. J. Biol. Chem. UNITED STATES. 275 (32): 25008—14. ISSN 0021-9258. PMID 10829020. doi:10.1074/jbc.M002491200.
- ^ Saltzman, A; Searfoss G; et al. (1998). „hUBC9 associates with MEKK1 and type I TNF-alpha receptor and stimulates NFkappaB activity”. FEBS Lett. NETHERLANDS. 425 (3): 431—5. ISSN 0014-5793. PMID 9563508.
Literatura[уреди | уреди извор]
- Lee FS, Hagler J, Chen ZJ, Maniatis T (1997). „Activation of the IkappaB alpha kinase complex by MEKK1, a kinase of the JNK pathway.”. Cell. 88 (2): 213—22. PMID 9008162. doi:10.1016/S0092-8674(00)81842-5.
- Siow YL; Kalmar GB; Sanghera JS; et al. (1997). „Identification of two essential phosphorylated threonine residues in the catalytic domain of Mekk1. Indirect activation by Pak3 and protein kinase C.”. J. Biol. Chem. 272 (12): 7586—94. PMID 9065412. doi:10.1074/jbc.272.12.7586.
- Su YC; Han J; Xu S; et al. (1997). „NIK is a new Ste20-related kinase that binds NCK and MEKK1 and activates the SAPK/JNK cascade via a conserved regulatory domain.”. EMBO J. 16 (6): 1279—90. PMC 1169726 . PMID 9135144. doi:10.1093/emboj/16.6.1279.
- Wu Z, Wu J, Jacinto E, Karin M (1997). „Molecular cloning and characterization of human JNKK2, a novel Jun NH2-terminal kinase-specific kinase.”. Mol. Cell. Biol. 17 (12): 7407—16. PMC 232596 . PMID 9372971.
- Xu S, Cobb MH (1998). „MEKK1 binds directly to the c-Jun N-terminal kinases/stress-activated protein kinases.”. J. Biol. Chem. 272 (51): 32056—60. PMID 9405400. doi:10.1074/jbc.272.51.32056.
- Fanger GR; Widmann C; Porter AC; et al. (1998). „14-3-3 proteins interact with specific MEK kinases.”. J. Biol. Chem. 273 (6): 3476—83. PMID 9452471. doi:10.1074/jbc.273.6.3476.
- Hirai S; Noda K; Moriguchi T; et al. (1998). „Differential activation of two JNK activators, MKK7 and SEK1, by MKN28-derived nonreceptor serine/threonine kinase/mixed lineage kinase 2.”. J. Biol. Chem. 273 (13): 7406—12. PMID 9516438. doi:10.1074/jbc.273.13.7406.
- Saltzman A; Searfoss G; Marcireau C; et al. (1998). „hUBC9 associates with MEKK1 and type I TNF-alpha receptor and stimulates NFkappaB activity.”. FEBS Lett. 425 (3): 431—5. PMID 9563508. doi:10.1016/S0014-5793(98)00287-7.
- Guan Z; Buckman SY; Pentland AP; et al. (1998). „Induction of cyclooxygenase-2 by the activated MEKK1 --> SEK1/MKK4 --> p38 mitogen-activated protein kinase pathway.”. J. Biol. Chem. 273 (21): 12901—8. PMID 9582321. doi:10.1074/jbc.273.21.12901.
- Lee FS, Peters RT, Dang LC, Maniatis T (1998). „MEKK1 activates both IkappaB kinase alpha and IkappaB kinase beta.”. Proc. Natl. Acad. Sci. U.S.A. 95 (16): 9319—24. PMC 21336 . PMID 9689078. doi:10.1073/pnas.95.16.9319.
- Yuasa T, Ohno S, Kehrl JH, Kyriakis JM (1998). „Tumor necrosis factor signaling to stress-activated protein kinase (SAPK)/Jun NH2-terminal kinase (JNK) and p38. Germinal center kinase couples TRAF2 to mitogen-activated protein kinase/ERK kinase kinase 1 and SAPK while receptor interacting protein associates with a mitogen-activated protein kinase kinase kinase upstream of MKK6 and p38.”. J. Biol. Chem. 273 (35): 22681—92. PMID 9712898.
- Pomérance M; Multon MC; Parker F; et al. (1998). „Grb2 interaction with MEK-kinase 1 is involved in regulation of Jun-kinase activities in response to epidermal growth factor.”. J. Biol. Chem. 273 (38): 24301—4. PMID 9733714. doi:10.1074/jbc.273.38.24301.
- Xia Y; Wu Z; Su B; et al. (1998). „JNKK1 organizes a MAP kinase module through specific and sequential interactions with upstream and downstream components mediated by its amino-terminal extension.”. Genes Dev. 12 (21): 3369—81. PMC 317229 . PMID 9808624. doi:10.1101/gad.12.21.3369.
- Nemoto S, DiDonato JA, Lin A (1998). „Coordinate regulation of IkappaB kinases by mitogen-activated protein kinase kinase kinase 1 and NF-kappaB-inducing kinase.”. Mol. Cell. Biol. 18 (12): 7336—43. PMC 109315 . PMID 9819420.
- Yujiri T, Sather S, Fanger GR, Johnson GL (1998). „Role of MEKK1 in cell survival and activation of JNK and ERK pathways defined by targeted gene disruption.”. Science. 282 (5395): 1911—4. PMID 9836645. doi:10.1126/science.282.5395.1911.
- Baud V; Liu ZG; Bennett B; et al. (1999). „Signaling by proinflammatory cytokines: oligomerization of TRAF2 and TRAF6 is sufficient for JNK and IKK activation and target gene induction via an amino-terminal effector domain.”. Genes Dev. 13 (10): 1297—308. PMC 316725 . PMID 10346818. doi:10.1101/gad.13.10.1297.
- Kopp E; Medzhitov R; Carothers J; et al. (1999). „ECSIT is an evolutionarily conserved intermediate in the Toll/IL-1 signal transduction pathway.”. Genes Dev. 13 (16): 2059—71. PMC 316957 . PMID 10465784. doi:10.1101/gad.13.16.2059.
- Ito M; Yoshioka K; Akechi M; et al. (1999). „JSAP1, a novel jun N-terminal protein kinase (JNK)-binding protein that functions as a Scaffold factor in the JNK signaling pathway.”. Mol. Cell. Biol. 19 (11): 7539—48. PMC 84763 . PMID 10523642.
- Minamino T; Yujiri T; Papst PJ; et al. (2000). „MEKK1 suppresses oxidative stress-induced apoptosis of embryonic stem cell-derived cardiac myocytes.”. Proc. Natl. Acad. Sci. U.S.A. 96 (26): 15127—32. PMC 24784 . PMID 10611349. doi:10.1073/pnas.96.26.15127.
- Nicholas C. Price; Lewis Stevens (1999). Fundamentals of Enzymology: The Cell and Molecular Biology of Catalytic Proteins (Third изд.). USA: Oxford University Press. ISBN 019850229X.
- Eric J. Toone (2006). Advances in Enzymology and Related Areas of Molecular Biology, Protein Evolution (Volume 75 изд.). Wiley-Interscience. ISBN 0471205036.
- Branden C; Tooze J. Introduction to Protein Structure. New York, NY: Garland Publishing. ISBN 0-8153-2305-0.
- Irwin H. Segel. Enzyme Kinetics: Behavior and Analysis of Rapid Equilibrium and Steady-State Enzyme Systems (Book 44 изд.). Wiley Classics Library. ISBN 0471303097.
- William P. Jencks (1987). Catalysis in Chemistry and Enzymology. Dover Publications. ISBN 0486654605.
