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Our findings indicate that MSK1/beta-catenin (show CTNNB1 Proteins) signaling serves as an escape survival signal upon PI3K (show PIK3CA Proteins) inhibition and provides a strong rationale for the combined use of PI3K (show PIK3CA Proteins) and MSK1/beta-catenin (show CTNNB1 Proteins) inhibition to induce lethal growth inhibition in human GBM cells.
Results show that MSK1 phosphorylates H3S10 through p38-MAPK (show MAPK14 Proteins) pathway in gastric cancer patients.
Interrupting MSK1 activation is a new target for antioxidants.
Increased MSK1 activity is critically important for Epstein-Barr virus LMP1 (show PDLIM7 Proteins)-promoted cell proliferation and transformation.
KSHV activates the MSK1/2-CREB1 (show CREB1 Proteins) pathway during primary infection and that it depends on this pathway for viral lytic replication. I
Authors conclude that paramyxoviruses trigger the DNA damage response, a pathway required for MSK1 activation of phospho Ser (show SIGLEC1 Proteins) 276 RelA (show NFkBP65 Proteins) formation to trigger the IRF7 (show IRF7 Proteins)-RIG-I (show DDX58 Proteins) amplification loop necessary for mucosal interferon (show IFNA Proteins) production.
These results highlight the relevance of MSK1 in the up-regulation of RARbeta (show RARB Proteins) by prostaglandin E2.
Data suggest that MSK1 and MSK2 are the major CREB (show CREB1 Proteins) kinases in fibroblast-like synoviocytes from rheumatoid arthritis patients stimulated with lysophosphatidic acid and that phosphorylation of CREB1 (show CREB1 Proteins) at Ser (show SIGLEC1 Proteins)-133 plays a significant role in IL-8 (show IL8 Proteins) production.
MSK1 plays an important role for hormone-dependent breast cancer growth
MSK1 and MSK2 are required for maximal TFF 1 (show TFF1 Proteins) induction.
essential role of the C-terminal domain of MSK1 for its constitutive interaction with group V secretory phospholipase A (show HRASLS Proteins)(2), which appears essential to support VEGF (show VEGFA Proteins)-mediated PAF (show KIAA0101 Proteins) synthesis
chromatin modifier, MSK1/2, has a role in suppressing endocrine and promoting acinar differentiation during pancreatic development
abnormal regulation of MSK1 contributes to the development of L-DOPA-induced dyskinesia and to the concomitant increase in striatal FosB (show FOSB Proteins), which may occur via increased histone H3 (show HIST3H3 Proteins) phosphorylation at the fosB (show FOSB Proteins) promoter
Accelerated apoptotic death and in vivo turnover of erythrocytes have been found in mice lacking functional MSK1/MSK2.
Results suggest that MSK1/2 plays a significant role in the regulation of ischemia-induced progenitor cell proliferation and neurogenesis
MSK1 has a role in malignant transformation and skin cancer development, but is inhibited by chrysin derivative 69407
the impact of MSK1 on glucocorticoid receptor (show NR3C1 Proteins)-mediated transactivation
MSK1 is an important novel molecule involved in RANKL (show TNFSF11 Proteins) signaling and osteoclast differentiation
MSK1/2 knockout results in reduced IL-10 (show IL10 Proteins) secretion.
MSK1-deficient mice exhibit a decreased capacity to entrain to a new light cycle, attenuated Period1 expression, histone phosporylation and CREB (show CREB1 Proteins) phosphorylation.
these data reveal that MSK1 serves as a critical regulator of hippocampal physiology and function
Serine/threonine-protein kinase that is required for the mitogen or stress-induced phosphorylation of the transcription factors CREB1 and ATF1 and for the regulation of the transcription factors RELA, STAT3 and ETV1/ER81, and that contributes to gene activation by histone phosphorylation and functions in the regulation of inflammatory genes. Phosphorylates CREB1 and ATF1 in response to mitogenic or stress stimuli such as UV-C irradiation, epidermal growth factor (EGF) and anisomycin. Plays an essential role in the control of RELA transcriptional activity in response to TNF and upon glucocorticoid, associates in the cytoplasm with the glucocorticoid receptor NR3C1 and contributes to RELA inhibition and repression of inflammatory gene expression. In skeletal myoblasts is required for phosphorylation of RELA at 'Ser-276' during oxidative stress. In erythropoietin-stimulated cells, is necessary for the 'Ser-727' phosphorylation of STAT3 and regulation of its transcriptional potential. Phosphorylates ETV1/ER81 at 'Ser-191' and 'Ser-216', and thereby regulates its ability to stimulate transcription, which may be important during development and breast tumor formation. Directly represses transcription via phosphorylation of 'Ser-1' of histone H2A. Phosphorylates 'Ser-10' of histone H3 in response to mitogenics, stress stimuli and EGF, which results in the transcriptional activation of several immediate early genes, including proto- oncogenes c-fos/FOS and c-jun/JUN. May also phosphorylate 'Ser-28' of histone H3. Mediates the mitogen- and stress-induced phosphorylation of high mobility group protein 1 (HMGN1/HMG14). In lipopolysaccharide-stimulated primary macrophages, acts downstream of the Toll-like receptor TLR4 to limit the production of pro- inflammatory cytokines. Functions probably by inducing transcription of the MAP kinase phosphatase DUSP1 and the anti- inflammatory cytokine interleukin 10 (IL10), via CREB1 and ATF1 transcription factors. Plays a role in neuronal cell death by mediating the downstream effects of excitotoxic injury.
90 kDa ribosomal protein S6 kinase 5
, RSK-like protein kinase
, nuclear mitogen- and stress-activated protein kinase 1
, ribosomal protein S6 kinase alpha-5
, mitogen- and stress-activated protein kinase-1
, ribosomal protein S6 kinase, polypeptide 5
, mitogen and stress-activated protein kinase 1
, ribosomal protein S6 kinase, 90kDa, polypeptide 5