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Study propose that the pathogen-responsive MPK3 (show MAPK3 ELISA Kits)/MPK6 cascade and ABA are two essential signaling pathways that control, respectively, the organic acid metabolism and ion channels, two main branches of osmotic regulation in guard cells that function interdependently to control stomatal opening/closure.
MPK6-mediated regulation of MYB15 plays an important role in cold stress signaling in Arabidopsis.
Data report that MPK3/MPK6 and their substrate ERF6 promote the biosynthesis of IGSs and the conversion of I3G to 4MI3G, a target of PEN2/PEN3-dependent chemical defenses in plant immunity.
Data show that the protein kinases MPK3 (show MAPK3 ELISA Kits) and MPK6 can both interact with SPOROCYTELESS/NOZZLE (SPL (show SGPL1 ELISA Kits)) in vitro and in vivo and can phosphorylate the SPL (show SGPL1 ELISA Kits) protein in vitro.
AIK1-MKK5 (show MAP2K5 ELISA Kits)-MPK6 cascade functions in the abscisic acid regulation of primary root growth and stomatal response.
A novel mechanism for PIN1 phosphorylation involving MKK7 (show MAP2K7 ELISA Kits) and MPK6 in shoot branching regulation in Arabidopsis.
MKK4 (show MAP2K4 ELISA Kits), MKK5 (show MAP2K5 ELISA Kits), MKK7 (show MAP2K7 ELISA Kits), and MKK9, are responsible for the activation of MPK3 (show MAPK3 ELISA Kits) and MPK6 by melatonin, indicating that melatonin-mediated innate immunity is triggered by MAPK (show MAPK1 ELISA Kits) signaling through MKK4 (show MAP2K4 ELISA Kits)/5/7/9-MPK3 (show MAPK3 ELISA Kits)/6 cascades.
Phosphatase AP2C1, as well as AP2C1-targeted MPK3 (show MAPK3 ELISA Kits) and MPK6, are important regulators of plant-nematode interaction, where the co-ordinated action of these signalling components ensures the timely activation of plant defence.
Mitogen-activated protein kinase 6 (MPK6) promoted C-terminal end of ORE3/EIN2 (CEND cleavage and nuclear translocation. Nuclear CEND accumulated ETHYLENE INSENSITIVE3 (EIN3), a transcription factor that accelerates MeJA-induced leaf senescence.
Results demonstrated the contribution of MPK3 (show MAPK3 ELISA Kits) and MPK6 to riboflavin-induced resistance.
There was significant association between p38gamma (show MAPK12 ELISA Kits) expression and esophageal squamous cell carcinoma clinical stage, lymph nodes metastases, and tumor volume. p38delta (show MAPK1/3 ELISA Kits) overexpression can promote tumorigenesis in nude mice model xenografted with Eca109 cells whose basal level of p38delta (show MAPK1/3 ELISA Kits) was stably over-expressed and p38gamma (show MAPK12 ELISA Kits) was stably knocked down.
Study revealed a post-translational regulation of TDP2 (show TDP2 ELISA Kits) activity and discovered a new role of ERK3 (show MAPK4 ELISA Kits) in increasing cancer cells' DNA damage response and chemoresistance to Top2 (show TOP2A ELISA Kits) inhibitors.
This study reveals a novel pathway that directly links ErbB4 (show ERBB4 ELISA Kits) and p38gamma (show MAPK12 ELISA Kits) to the transcriptional machinery of NKx2.5 (show NKX2-5 ELISA Kits)-GATA4 (show GATA4 ELISA Kits) complex which is critical for cardiomyocyte formation during mammalian heart development.
during interphase ERK3 (show MAPK4 ELISA Kits) is mainly resident in the nucleoplasm in association with ribonuclear proteins involved in early pre-mRNA splicing, it undergoes cell cycle-dependent redistribution and, during apoptosis
Taken together our data suggest that as cells initiate adhesion to matrix increasing levels of ERK3 (show MAPK4 ELISA Kits) at the cell periphery are required to orchestrate cell morphology changes which can then drive migratory behavior.
p38gamma (show MAPK12 ELISA Kits) and p38delta (show MAPK1/3 ELISA Kits) reprogram liver metabolism by modulating neutrophil infiltration and provide a potential target for NAFLD (show TSC2 ELISA Kits) therapy
MAPK6 could rescue the cell growth induced by miR499a and HBV
analysis of how allosteric regulation of p38gamma (show MAPK12 ELISA Kits) and PTPN3 (show PTPN3 ELISA Kits) involves a PDZ domain (show INADL ELISA Kits)-modulated complex formation
ERK3 (show MAPK4 ELISA Kits) regulates endothelial cell migration, proliferation and tube formation by upregulating SRC-3 (show NCOA3 ELISA Kits)/SP-1 (show PSG1 ELISA Kits)-mediated VEGFR2 (show KDR ELISA Kits) expression.
These findings further expand distinct roles of cyclin D3 (show CCND3 ELISA Kits) and suggest the potential activity of ERK3 (show MAPK4 ELISA Kits) in cell proliferation.
ERK3 (show RYK ELISA Kits) biological activity is regulated by its cellular abundance through the control of protein stability
Data show that extracellular-regulated kinase 3 (ERK3 (show RYK ELISA Kits)) specifically interacts with the MAPK-activated protein kinase 5 (MK5 (show MAPKAPK5 ELISA Kits) or PRAK (show MAPKAPK5 ELISA Kits)) in vitro and in vivo.
Results demonstrate a specific interaction between extracellular signal-regulated kinase 3 (ERK3) and mitogen-activated protein kinase-activated protein kinase-5 (MK5 (show MAPKAPK5 ELISA Kits)).
p38gamma (show MAPK12 ELISA Kits) MAP kinase (show MAPK1 ELISA Kits) (SAPK3/p38gamma (show MAPK12 ELISA Kits)) was shown to catalyse phosphorylation of SAP97 (show DLG1 ELISA Kits).
Results show that Cdo (show CDO1 ELISA Kits) is important for full Abl kinase activity, and Abl (show ABL1 ELISA Kits) is necessary for full activation of p38 MAPK (show MAPK14 ELISA Kits), during myogenic differentiation.
The protein encoded by this gene is a member of the Ser/Thr protein kinase family, and is most closely related to mitogen-activated protein kinases (MAP kinases). MAP kinases also known as extracellular signal-regulated kinases (ERKs), are activated through protein phosphorylation cascades and act as integration points for multiple biochemical signals. This kinase is localized in the nucleus, and has been reported to be activated in fibroblasts upon treatment with serum or phorbol esters.
, MAP kinase 6
, MAP kinase isoform p97
, MAPK 6
, extracellular signal-regulated kinase 3
, extracellular signal-regulated kinase, p97
, protein kinase, mitogen-activated 5
, protein kinase, mitogen-activated 6
, Erk-3 related
, mitogen activated protein kinase 4
, mitogen activated protein kinase 6
, protein kinase, mitogen activated kinase 4
, extracellular related kinase 3
, mitogen-activated protein kinase 6