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Data show that the protein kinases MPK3 and MPK6 (show MAPK6 Proteins) can both interact with SPOROCYTELESS/NOZZLE (SPL (show SGPL1 Proteins)) in vitro and in vivo and can phosphorylate the SPL (show SGPL1 Proteins) protein in vitro.
MKK4 (show MAP2K4 Proteins), MKK5 (show MAP2K5 Proteins), MKK7 (show MAP2K7 Proteins), and MKK9, are responsible for the activation of MPK3 and MPK6 (show MAPK6 Proteins) by melatonin, indicating that melatonin-mediated innate immunity is triggered by MAPK (show MAPK1 Proteins) signaling through MKK4 (show MAP2K4 Proteins)/5/7/9-MPK3/6 cascades.
Phosphatase AP2C1, as well as AP2C1-targeted MPK3 and MPK6 (show MAPK6 Proteins), are important regulators of plant-nematode interaction, where the co-ordinated action of these signalling components ensures the timely activation of plant defence.
Results demonstrated the contribution of MPK3 and MPK6 (show MAPK6 Proteins) to riboflavin-induced resistance.
These results indicate that the MVB pathway is positively regulated by pathogen-responsive MPK3/6 through LIP5 phosphorylation and plays a critical role in plant immune system
MKK3-MPK6 is activated by blue light in a MYC2-dependent manner.
MPK3 and MPK6 (show MAPK6 Proteins) target a subclass of 'VQ-motif'-containing proteins to regulate immune responses.
MicroRNA biogenesis factor DRB1 (show EPHX1 Proteins) is a phosphorylation target of mitogen activated protein kinase (show MAPK1 Proteins) MPK3 in both rice and Arabidopsis
MPK3 represses the constitutive and flg22-induced expression of defence genes in Arabidopsis thaliana.
These results suggest that the MKK9-MPK3/MPK6 (show MAPK6 Proteins) cascade is part of the phosphate signaling pathway in plants.
MAPK3/1 is involved in luteinizing hormone-mediated decrease of C-type natriuretic peptide (show NPPC Proteins) and this process is related to the EGFR (show EGFR Proteins) and MAPK3/1 signal pathways
Chronic hypoxia induces Egr-1 via activation of ERK1/2 and contributes to pulmonary vascular remodeling.
ER Ca(2+) release enhances eNOS Ser-635 phosphorylation and function via ERK1/2 activation.
Thrombospondin 1 (show THBS1 Proteins), fibronectin (show FN1 Proteins), and vitronectin (show VTN Proteins) are differentially dependent upon RAS, ERK1/2, and p38 (show MAPK14 Proteins) for induction of vascular smooth muscle cell chemotaxis.
results suggest that Nav1.7-Ca2+ influx-protein kinase C-alpha pathway activated ERK1/ERK2 and p38, which increased phosphorylation of glycogen synthase kinase-3beta, decreasing tau phosphorylation
These data suggest that Gab1-ERK1/2 binding and their nuclear translocation play a crucial role in Egr-1 (show EGR1 Proteins) nuclear accumulation.
data demonstrate that hypoxia-induced adventitial fibroblast proliferation requires activation and interaction of PI3K, Akt, mTOR, p70S6K, and ERK1/2.
This study demonstrates for the first time that cyclic mechanical stretch induces the proliferation of bovine satellite cells and suppresses their myogenic differentiation through the activation of ERK (show MAPK1 Proteins).
findings indicate that exposure to DHEA, at concentrations found in human blood, causes vascular endothelial proliferation by a plasma membrane-initiated activity that is Gi/o and ERK1/2 dependent.
Results suggest that estrogen receptors and the ERK1/2 signaling pathway are involved in the anti-apoptotic action of LY117018 in vascular endothelial cells.
The results suggest that the MPK-1 (show MAPK1 Proteins)/ERK (show MAPK1 Proteins) regulatory network, including FBF-1, FBF-2, and LIP-1 (show CENPJ Proteins), controls the number of sperm by regulating the timing of the sperm-oocyte switch in C. elegans.
Cek2 (show FGFR3 Proteins) has a cryptic role in cell-wall biogenesis and its role is not entirely redundant to Cek1.
knockdown of SUV420H1 (show SUV420H1 Proteins) reduced phosphorylated ERK1 and total ERK1 proteins, and interestingly suppressed ERK1 at the transcriptional level
Secreted aspartic protease-mediated proteolytic cleavage of Msb2 is required for activation of the Cek1 mitogen activated protein kinase (show MAPK1 Proteins) pathway in response to environmental cues.
The authors propose that a Msb2, Cek1 and Ace2 signalling pathway addresses PMT genes as downstream targets and that different modes of regulation have evolved for PMT1 and PMT2/PMT4 genes.
Msb2 is involved in the transmission of the signal toward Cek1 mediated by the Cdc42 (show CDC42 Proteins) GTPase (show RACGAP1 Proteins).
ERK1/2-Akt1 (show AKT1 Proteins) crosstalk regulates arteriogenesis in mice and zebrafish.
eena (show SH3GL1 Proteins) plays an important role in the development of the myeloid cell through activation of the ERK1/ERK2 (show MAPK1 Proteins) pathway
ERK1 and ERK2 (show MAPK1 Proteins) target common and distinct gene sets, confirming diverse roles for these kinases during embryogenesis; for ERK1 different specific genes involved in dorsal-ventral patterning and subsequent embryonic cell migration were identified.
These results demonstrate that induction of Hsp70 (show HSPA1A Proteins) in response to heat stress is dependent on ERK (show MAPK1 Proteins) activation in Pac2 (show PSMG2 Proteins) cells.
Data define distinct roles for ERK1 and ERK2 (show MAPK1 Proteins) in developmental cell migration processes during zebrafish embryogenesis.
GLUL (show GLUL Proteins) knockdown markedly inhibited the p38 MAPK (show MAPK14 Proteins) and ERK1/ERK2 (show MAPK1 Proteins) signaling pathways in cultured breast cancer cells and reduces their proliferation.
These results suggested that HOXB7 (show HOXB7 Proteins) stimulates ERK1/2 phosphorylation and provided evidence that HOXB7 (show HOXB7 Proteins), besides its role in transcriptional regulation, also promotes cell motility and invasiveness.
High ERK1 expression is associated with castration-resistant prostate cancer.
combined use of butyrate and highly specific Syk inhibitor BAY61-3606 does not enhance differentiation and apoptosis of colonocytes. Instead, BAY completely abolishes butyrate-induced differentiation and apoptosis in a Syk- and ERK1/2-dependent manner.
new findings indicating that canonical FGFR-ERK1/2 signaling entrapped hBMSCs in a pre-committed state and arrested further maturation of committed precursors.
mutually exclusive transcriptional regulation by AP-1 (cjun (show JUN Proteins)/cfos) and non-canonical NF-kappaB (show NFKB1 Proteins) (RelB (show RELB Proteins)/p52 (show FKBP4 Proteins)) downstream of MEK (show MAP2K1 Proteins)-ERK (show EPHB2 Proteins) and NIK (show MAP3K14 Proteins)-IKK-alpha (show CHUK Proteins)-NF-kappaB2 (p100 (show CUX1 Proteins)) phosphorylation, respectively was responsible for persistent Ccl20 (show CCL20 Proteins) expression in the colonic cells.
LPS (show IRF6 Proteins)-activated ERK1,2 was at least partly involved in the observed effects on periodontal ligament stem cell differentiation capacity, acquisition of myofibroblastic attributes, and changes of their immunomodulatory features.
The findings indicate that ERK (show EPHB2 Proteins) and JNK (show MAPK8 Proteins) signaling pathways, as well as NF-kappaB (show NFKB1 Proteins)-mediated signaling are important contributors to the pathogenesis of Kashin-Beck disease.
The antitumor activity of scopoletin may be due to its strong anti-angiogenic effect, which may be mediated by its effective inhibition of ERK1, VEGF-A (show VEGFA Proteins), and FGF-2 (show FGF2 Proteins).
High ERK1 expression is associated with melanoma.
pERK1/2 is a regulator of CD44 (show CD44 Proteins) expression, and increased CD44 (show CD44 Proteins) expression leads to a pro-sclerotic and migratory parietal epithelial cell phenotype in focal segmental glomerulosclerosis.
mmLDL increased the serum concentrations and expression of ICAM-1 (show ICAM1 Proteins) and VCAM-1 (show VCAM1 Proteins) by activating the ERK1/2 pathway, resulting in the expression of ETB (show EDNRB Proteins) receptors and the enhancement of contractile function in vascular smooth muscle.
Angiotensin II regulates dendritic cells through activation of p65 NF-kappaB (show NFkBP65 Proteins), ERK1, ERK2 (show MAPK1 Proteins) and STAT1 (show STAT1 Proteins) pathways.
MAPK3/1 participates in primordial follicle activation through mTORC1-KITL (show KITLG Proteins) signaling.
At low oxLDL levels LOX-1 activates the protective Oct-1/SIRT1 pathway, while at higher levels of the lipoprotein switches to the thrombogenic ERK1/2 pathway.
Studies indicate that progesterone receptor transgenic (Pgrcre/+) mitogen inducible gene 6 (Mig-6over) phosphatase and tensin homolog protein (Ptenf/f) knockout mice exhibited an increase of phospho-ERK1/2 and its target genes.
Gpr182 reduction led to increased activation of ERK1/2 in basal and challenge models, demonstrating a potential role for this orphan GPCR in regulating the proliferative capacity of the intestine.
ERK1 underexpression is associated with obesity.
retinoschisin (show RS1 Proteins) is a novel regulator of MAP kinase (show MAPK1 Proteins) signalling and exerts an anti-apoptotic effect on retinal cells.
Postnatal chondrocyte-specific deletion of Hdac3 (show HDAC3 Proteins) with an inducible Col2a1 (show COL2A1 Proteins)-Cre caused premature production of pErk1/2 and Mmp13 (show MMP13 Proteins) in the growth plate.
Pseudorabies virus glycoprotein gE-mediated ERK 1/2 phosphorylation also occurs in epithelial cells and in these cells, gE-mediated ERK 1/2 signaling is associated with degradation of the pro-apoptotic protein Bim (show BCL2L11 Proteins).
Treatment with ERK inhibitors or ERK1/2 knockdown significantly suppressed porcine epidemic diarrhea virus progeny production.
This study reveals a new function of the gE glycoprotein of pseudorabies virus and suggests that pseudorabies virus, through activation of ERK1/2 signaling, has a substantial impact on T cell behavior.
CSF2 (show CSF2 Proteins) stimulates proliferation of trophectoderm cells by activation of the PI3K-and ERK1/2 MAPK (show MAPK1 Proteins)-dependent MTOR (show FRAP1 Proteins) signal transduction cascades.
PGRN (show GRN Proteins) inhibits adipogenesis in porcine preadipocytes partially through ERK (show MAPK1 Proteins) activation mediated PPARgamma (show PPARG Proteins) phosphorylation.
Porcine circovirus type 2 (PCV2) might induce autophagy via the AMPK (show PRKAA1 Proteins)/ERK (show MAPK1 Proteins)/TSC2/mTOR (show FRAP1 Proteins) signaling pathway in the host cells, representing a pivotal mechanism for PCV2 pathogenesis
Data show that proinflammatory cytokines induction was ERK1/2 and JNK1 (show MAPK8 Proteins)/2 dependent.
Saccharomyces cerevisiae inhibits the Enterotoxigenic Escherichia coli-induced expression of pro-inflammatory transcripts and this inhibition was associated to a decrease of ERK1/2 and p38 MAPK (show MAPK14 Proteins) phosphorylation
ERK1 phosphorylation in response to Insulin-like Growth Factor-1 (show IGF1 Proteins) does not require activation of the Insulin-like Growth Factor-1 receptor tyrosine kinase (show IGF1R Proteins)
Retinal ischemia-reperfusion alters expression of mitogen-activated protein kinases, particularly ERK1/2, in the neuroretina and retinal arteries.
The protein encoded by this gene is a member of the MAP kinase family. MAP kinases, also known as extracellular signal-regulated kinases (ERKs), act in a signaling cascade that regulates various cellular processes such as proliferation, differentiation, and cell cycle progression in response to a variety of extracellular signals. This kinase is activated by upstream kinases, resulting in its translocation to the nucleus where it phosphorylates nuclear targets. Alternatively spliced transcript variants encoding different protein isoforms have been described.
extracellular signal-regulated kinase 1
, likely protein kinase
, MAP kinase isoform p44
, MAPK 1
, extracellular signal-related kinase 1
, insulin-stimulated MAP2 kinase
, microtubule-associated protein 2 kinase
, MAP kinase 3
, p44 MAP kinase
, pp42/MAP kinase
, MAP kinase 1
, MAPK 3
, mitogen-activated 3
, mitogen-activated protein kinase 1
, mitogen-activated protein kinase 3
, extracellular signal-regulated kinase-1