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Mitogen-activated protein kinase kinase kinase 3

MEKK3, MAP3K3, mitogen-activated protein kinase kinase kinase 3
This gene product is a 626-amino acid polypeptide that is 96.5% identical to mouse Mekk3. Its catalytic domain is closely related to those of several other kinases, including mouse Mekk2, tobacco NPK, and yeast Ste11. Northern blot analysis revealed a 4.6-kb transcript that appears to be ubiquitously expressed. This protein directly regulates the stress-activated protein kinase (SAPK) and extracellular signal-regulated protein kinase (ERK) pathways by activating SEK and MEK1/2 respectively; it does not regulate the p38 pathway. In cotransfection assays, it enhanced transcription from a nuclear factor kappa-B (NFKB)-dependent reporter gene, consistent with a role in the SAPK pathway. Alternatively spliced transcript variants encoding distinct isoforms have been observed. [provided by RefSeq, Jul 2008] (from NCBI)
Top mentioned proteins: MAPK, p38, NF-kappaB, JNK, MEKK2
Papers on MEKK3
Activation of TAK1 by Chemotactic and Growth Factors, and Its Impact on Human Neutrophil Signaling and Functional Responses.
McDonald et al., Sherbrooke, Canada. In J Immunol, Jan 2016
Inhibition of TAK1 also impaired MEKK3 (but not MEKK1) activation by fMLF.
The cerebral cavernous malformation proteins CCM2L and CCM2 prevent the activation of the MAP kinase MEKK3.
Mayadas et al., Boston, United States. In Proc Natl Acad Sci U S A, Dec 2015
In vitro, both CCM2L and CCM2 bind MEKK3 in a complex with CCM1.
A novel IL-17 signaling pathway controlling keratinocyte proliferation and tumorigenesis via the TRAF4-ERK5 axis.
Li et al., Shanghai, China. In J Exp Med, Oct 2015
Here we report a novel IL-17-mediated cascade via the IL-17R-Act1-TRAF4-MEKK3-ERK5 positive circuit that directly stimulates keratinocyte proliferation and tumor formation.
Amino Acid Activation of mTORC1 by a PB1-Domain-Driven Kinase Complex Cascade.
Diaz-Meco et al., Los Angeles, United States. In Cell Rep, Sep 2015
Here, we show that p62 is phosphorylated via a cascade that includes MEK3/6 and p38δ and is driven by the PB1-containing kinase MEKK3.
Association Study of GWAS-Derived Loci with Height in Brazilian Children: Importance of MAP3K3, MMP24 and IGF1R Polymorphisms for Height Variation.
Lima Jorge et al., Fortaleza, Brazil. In Horm Res Paediatr, 2014
BACKGROUND/AIM: The single nucleotide polymorphisms (SNPs) rs2282978 (CDK6), rs2425019 (MMP24), rs8081612 (MAP3K3), rs2871865 (IGF1R) and rs3782415 (SOCS2) were among the SNPs most strongly associated with height in a meta-analysis of 47 genome-wide association studies (GWAS) involving 114,223 adults from six ethnic groups.
KLF4 is a key determinant in the development and progression of cerebral cavernous malformations.
Dejana et al., Milano, Italy. In Embo Mol Med, 2014
Here, we report that Ccm1 ablation leads to the activation of a MEKK3-MEK5-ERK5-MEF2 signaling axis that induces a strong increase in Kruppel-like factor 4 (KLF4) in ECs in vivo.
A macrophage NBR1-MEKK3 complex triggers JNK-mediated adipose tissue inflammation in obesity.
Moscat et al., Los Angeles, United States. In Cell Metab, 2014
Furthermore, we demonstrate that an interaction between the PB1 domains of NBR1 and the mitogen-activated kinase kinase 3 (MEKK3) enables the formation of a signaling complex required for the activation of JNK.
Signaling pathways and the cerebral cavernous malformations proteins: lessons from structural biology.
Boggon et al., New Haven, United States. In Cell Mol Life Sci, 2014
These genes encode for the proteins KRIT1/CCM1 (krev interaction trapped 1/cerebral cavernous malformations 1), cerebral cavernous malformations 2, osmosensing scaffold for MEKK3 (CCM2/malcavernin/OSM), and cerebral cavernous malformations 3/programmed cell death 10 (CCM3/PDCD10).
Exogenous and autocrine growth factors stimulate human intervertebral disc cell proliferation via the ERK and Akt pathways.
Kletsas et al., Athens, Greece. In J Orthop Res, 2012
Proliferation of human IVD cells is regulated by exogenous and autocrine growth factors mainly via the MEK/ERK and PI-3K/Akt pathways.
MEKK3 regulates IFN-gamma production in T cells through the Rac1/2-dependent MAPK cascades.
Su et al., New Haven, United States. In J Immunol, 2011
Using Mekk3-deficient murine T cells, the authors concluded MEKK3 expression is required for mounting optimal T cell responses in vivo and is involved in mediating the TCR-dependent Rac1/2 signals for IFN-gamma production through the MAPK pathways.
The kinases MEKK2 and MEKK3 regulate transforming growth factor-β-mediated helper T cell differentiation.
Su et al., New Haven, United States. In Immunity, 2011
MEKK2 alone can suppress T-cell TGF-beta responses. MEKK2 or MEKK3 can cause ERK1/2 to phosphorylate SMAD2/3 and suppress R-SMAD-dependent transcription. MEKK2 and MEKK3 play overlapping roles in regulating Th-cell differentiation via TGF-beta
Molecular basis of lysophosphatidic acid-induced NF-κB activation.
Yang et al., Houston, United States. In Cell Signal, 2010
PKC, β-arrestin 2, CARMA3, BCL10, MALT1, TRAF6 and MEKK3 are signaling proteins that have a key role in G protein-coupled receptor (GPCR)-mediated activation of nuclear factor-κB (NF-κB) pathway in nonhematopoietic cells in response to lysophosphatidic acid (LPA) stimulation.
MEKK3 overexpression contributes to the hyperresponsiveness of IL-12-overproducing cells and CD4+ T conventional cells in nonobese diabetic mice.
Shen et al., Beijing, China. In J Immunol, 2010
The signaling defect of elevated interleukin (IL)-12 overproducing cells in nonobese diabetic mice could be attributed to, at least partially, the overexpression of a single MAP3K, namely MEKK3.
The epidermal growth factor receptor modulates DNA double-strand break repair by regulating non-homologous end-joining.
Dikomey et al., Hamburg, Germany. In Dna Repair (amst), 2010
The regulation of NHEJ by EGFR was only blocked when ERK was affected by siRNA but not when AKT was knocked down. These data indicate that EGFR modulates DSB repair by regulating NHEJ via MAPK signalling.
Structure and function of the PB1 domain, a protein interaction module conserved in animals, fungi, amoebas, and plants.
Ito et al., Fukuoka, Japan. In Sci Stke, 2007
The canonical PB1 dimerization is required for the formation of complexes between p40(phox) and p67(phox) (for activation of the NADPH oxidase crucial for mammalian host defense), between the scaffold Bem1 and the guanine nucleotide exchange factor Cdc24 (for polarity establishment in yeasts), and between the polarity protein Par6 and atypical protein kinase C (for cell polarization in animal cells), as well as for the interaction between the mitogen-activated protein kinase kinase kinases MEKK2 or MEKK3 and the downstream target mitogen-activated protein kinase kinase MEK5 (for early cardiovascular development in mammals).
Cell signaling and function organized by PB1 domain interactions.
Campuzano et al., Madrid, Spain. In Mol Cell, 2006
The PB1-domain-containing proteins p62, aPKC, MEKK2/MEKK3, MEK5, and Par-6 play roles in critical cell processes like osteoclastogenesis, angiogenesis, and early cardiovascular development or cell polarity.
Differential regulation of interleukin 1 receptor and Toll-like receptor signaling by MEKK3.
Su et al., Houston, United States. In Nat Immunol, 2004
mekk3 regulates interleukin-1 and toll-like receptor 4 signaling.
Rac-MEKK3-MKK3 scaffolding for p38 MAPK activation during hyperosmotic shock.
Johnson et al., Chapel Hill, United States. In Nat Cell Biol, 2003
We have discovered a novel scaffold protein that binds to actin, the GTPase Rac, and the upstream kinases MEKK3 and MKK3 in the p38 MAPK phospho-relay module.
The essential role of MEKK3 in TNF-induced NF-kappaB activation.
Su et al., Houston, United States. In Nat Immunol, 2001
Using mitogen-activated protein kinase kinase kinase 3 (MEKK3)-deficient fibroblast cells, we found that MEKK3 plays a critical role in TNF-induced NF-kappaB activation.
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