• Emodin specifically causes phosphorylation of cAMP-responsive element binding protein (CREB), an important molecule in the differentiation of neurons. (wikipedia.org)
  • α-lipoic acid (LA) mainly causes N2a differentiation through phosphorylation of the ERK pathway and the Akt pathway. (wikipedia.org)
  • conversely,S98A homozygotes showed enhanced MEF2 function through muscle differentiation within the adult myoblasts associated with the wing imaginal disc. (bvsalud.org)
  • Activity of the myogenic regulatory protein myocyte enhancer factor-2 (MEF2) is modulated by post-translational modification. (bvsalud.org)
  • In the nucleus, phosphorylates the MEF2 repressor HDAC4, promoting its nuclear export and binding to 14-3-3 protein, and expression of MEF2 and genes involved in the hypertrophic program. (icr.ac.uk)
  • Calcium/calmodulin-dependent protein kinase that operates in the calcium-triggered CaMKK-CaMK4 signaling cascade and regulates, mainly by phosphorylation, the activity of several transcription activators, such as CREB1, MEF2D, JUN and RORA, which play pivotal roles in immune response, inflammation, and memory consolidation. (nih.gov)
  • Myofibrillar Z-discs Are a Protein Phosphorylation Hot Spot with Protein Kinase C (PKC? (omicsdi.org)
  • We therefore established, by global phosphoproteomics of EPS-treated contracting myotubes, a comprehensive site-resolved protein phosphorylation map of the Z-disc and found that it is a phosphorylation hotspot in skeletal myocytes, underscoring its functions in signaling and disease-related processes. (omicsdi.org)
  • In this study, we provide multiple lines of evidence showing that the post-translational phosphorylation of MSY3 by Akt kinase modulates the MSY3 repression of myogenin. (biomedcentral.com)
  • Fluorescence recovery after photobleaching experiments indicated that this phosphorylation modulates FLNc dynamics. (omicsdi.org)
  • Skeletal muscle and myogenic C2C12 cells were used to study the effects of MSY3 phosphorylation in vivo and in vitro on its sub-cellular localization and activity, by blocking the IGF1/PI3K/Akt pathway, by Akt depletion and over-expression, and by mutating potential MSY3 phosphorylation sites. (biomedcentral.com)
  • We investigated the in vivo phosphorylation of Drosophila MEF2, and identified serine 98 (S98) as a phosphorylated residue. (bvsalud.org)
  • In CD4 memory T-cells, is required to link T-cell antigen receptor (TCR) signaling to the production of IL2, IFNG and IL4 (through the regulation of CREB and MEF2). (nih.gov)
  • Furthermore, forced expression of Akt in adult skeletal muscle induced MSY3 phosphorylation and myogenin derepression. (biomedcentral.com)
  • May participate in the modulation of skeletal muscle function in response to exercise, by regulating SR Ca(2+) transport through phosphorylation of PLN/PLB and triadin, a ryanodine receptor-coupling factor. (icr.ac.uk)
  • In C2C12 myogenic cells, blocking the IGF1/PI3K/Akt pathway using LY294002 inhibitor reduced MSY3 phosphorylation levels resulting in its accumulation in the nuclei. (biomedcentral.com)
  • Overexpression of ClpP reduces αSyn-induced mitochondrial oxidative stress through enhancing the level of Superoxide Dismutase-2 (SOD2), and suppresses the accumulation of αSyn S129 phosphorylation and promotes neuronal morphology in neurons derived from PD patient iPS cells carrying αSyn A53T mutant. (springer.com)
  • Overall our data indicate that blocking MEF2 S98 phosphorylation in myoblasts enhances its myogenic capability, whereas blocking S98 phosphorylation in differentiating muscles attenuates MEF2 function. (bvsalud.org)
  • Our studies are among the first to assess the functional significance of MEF2 phosphorylation sites in the intact animal, and suggest that the same modification can have profoundly different effects upon MEF2 function depending upon the developmental context. (bvsalud.org)
  • MEF2-dependent transcription is repressed by HDAC-9 by recruiting HDAC-1 and/or HDAC-3. (novusbio.com)
  • 2019 ) A Late Phase of Long-Term Synaptic Depression in Cerebellar Purkinje Cells Requires Activation of MEF2. (neurotree.org)
  • MSY3 phosphorylation by Akt in vitro impaired its binding at the MyogHCE element, while blocking Akt increased MSY3 binding activity. (biomedcentral.com)
  • These results support the hypothesis that MSY3 phosphorylation by Akt interferes with MSY3 repression of myogenin circuit activity during muscle development. (biomedcentral.com)
  • Phospho-mimetic (S98E) and phospho-null (S98A) isoforms of MEF2 did not differ from wild-type in their activity in vitro, so we used CRISPR/Cas9 to generate an S98A allele of the endogenous gene. (bvsalud.org)
  • 2. Cornuside suppresses expression levels of cytokine-induced proinflammatory and adhesion molecules in the human en. (targetmol.jp)
  • Based on yeast genetic studies, we identify the mitochondrial translation factor MEF2 as a mediator of atorvastatin toxicity. (prolekarniky.cz)
  • 7. Cyclic AMP represses pathological MEF2 activation by myocyte-specific hypo-phosphorylation of HDAC5. (nih.gov)
  • Activity of the myogenic regulatory protein myocyte enhancer factor-2 (MEF2) is modulated by post-translational modification. (bvsalud.org)
  • Phosphorylation of HDAC5, a repressor of myocyte enhancer factor 2 (MEF2) leading to nuclear export of HDAC5 and allowing MEF2-mediated transcription. (nih.gov)
  • Activated ERK5 phosphorylates its targets including myocyte enhancer factor 2 (MEF2), Sap1a, c-Myc, and RSK. (umbc.edu)
  • Regular T (Tcon) cells and Foxp3+ T-regulatory (Treg) cells are believed to have differing metabolic requirements but small is well known of mitochondrial functions within these cell populations In murine studies we discovered that activation of both Tcon and Treg cells resulted in myocyte enhancer factor 2 (Mef2)-induced expression of genes vital that you oxidative phosphorylation (OXPHOS). (healthcarecoremeasures.com)
  • In postmitotic myocytes myogenin MRF4 and MyoD regulate procedures including cell fusion and contractile proteins appearance and set up (36 41 48 50 51 The MADS-box binding myocyte enhancer aspect-2 (MEF2) transcription elements are coordinately upregulated with myogenin during differentiation and cooperate with MRFs to modify transcription of skeletal muscles genes and donate to fibers type standards (4). (sciencepop.org)
  • As opposed to proliferating Tcon cells Compact disc8+ memory space T cells rely primarily on oxidative phosphorylation (OXPHOS) for energy creation (10 11 OXPHOS can be thought very important to energy creation by Foxp3+ T-regulatory (Treg) cells (7 8 12 13 a subset of T cells crucial to maintaining immune system homeostasis and suppressing immune system reactions (14). (healthcarecoremeasures.com)
  • Mitochondria serve as power plants that generate adenosine 5'-triphosphate (ATP) through oxidative phosphorylation (OXPHOS) for the cell. (biomedcentral.com)
  • Using this approach, we identify a set of genes involved in oxidative phosphorylation whose expression is coordinately decreased in human diabetic muscle. (gsea-msigdb.org)
  • 12. Neurohormonal regulation of cardiac histone deacetylase 5 nuclear localization by phosphorylation-dependent and phosphorylation-independent mechanisms. (nih.gov)
  • Mef2 can be inhibited by histone/proteins deacetylase-9 (Hdac9) and deletion improved Treg suppressive function. (healthcarecoremeasures.com)
  • CaM kinase II regulates cardiac hemoglobin expression through histone phosphorylation upon sympathetic activation. (uni-heidelberg.de)
  • ERK5 then undergoes a conformational change, facilitating phosphorylation on residues in the C-terminal domain and translocation to the nucleus where it regulates MEF2 transcriptional activity. (brad.ac.uk)
  • Calcium/calmodulin-dependent protein kinase that operates in the calcium-triggered CaMKK-CaMK4 signaling cascade and regulates, mainly by phosphorylation, the activity of several transcription activators, such as CREB1, MEF2D, JUN and RORA, which play pivotal roles in immune response, inflammation, and memory consolidation. (nih.gov)
  • Mondru AK, Aljasir MA, Alrumayh A et al (2023) VEGF stimulates activation of ERK5 in the absence of C-terminal phosphorylation preventing nuclear localization and facilitating AKT activation in endothelial cells. (brad.ac.uk)
  • ERK5 is activated in response to growth factors and stress by a cascade that leads to its phosphorylation by the MAP2K MEK5, which in turn is regulated by the MAP3Ks MEKK2 and MEKK3. (umbc.edu)
  • Previous studies have defined a canonical pathway for ERK5 activation, showing that ligand stimulation leads to MEK5 activation resulting in dual phosphorylation of ERK5 on Thr218/Tyr220 residues within the activation loop. (brad.ac.uk)
  • Furthermore, the use of small-molecule inhibitors to MEK5 and ERK5 shows that instead of regulating MEF2 activity, VEGF-mediated ERK5 is important for regulating AKT activity. (brad.ac.uk)
  • Our current data show that in contrast to EGF-stimulated HeLa cells, VEGF-mediated ERK5 activation in human dermal microvascular endothelial cells (HDMECs) does not result in C-terminal phosphorylation of ERK5 and translocation to the nucleus, but instead to a more plasma membrane/cytoplasmic localisation. (brad.ac.uk)
  • Inhibits myogenesis by sequestrating E proteins, inhibiting trans-activation by MEF2, and inhibiting DNA-binding by MYOD1 through physical interaction. (affbiotech.com)
  • Our studies are among the first to assess the functional significance of MEF2 phosphorylation sites in the intact animal, and suggest that the same modification can have profoundly different effects upon MEF2 function depending upon the developmental context. (bvsalud.org)
  • 1995). MAPK3 shows 75% sequence identity to MAPK2 and, like MAPK2, is phosphorylated by p38 but the exact phosphorylation sites are not determined. (reactome.org)