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MAP kinase interacting serine/threonine kinase 1

This gene encodes a Ser/Thr protein kinase that interacts with, and is activated by ERK1 and p38 mitogen-activated protein kinases, and thus may play a role in the response to environmental stress and cytokines. This kinase may also regulate transcription by phosphorylating eIF4E via interaction with the C-terminal region of eIF4G. Alternatively spliced transcript variants have been noted for this gene. [provided by RefSeq, Jan 2012] (from NCBI)
Top mentioned proteins: eIF4E, MAPK, p38, ATP7B, ERK
Papers using Mnk1 antibodies
p38 MAP kinase mediates stress-induced internalization of EGFR: implications for cancer chemotherapy
Fuchs Serge Y et al., In Oncogene, 2005
... Mnk1 inhibitor CGP57380 was purchased from Tocris.
Molecular targets for modulating lung inflammation and injury
Fuchs Sebastien, In PLoS ONE, 2003
... Anti-human Mknk2 was purchased from Sigma (St Louis, MO), Anti-phospho-mnk1 was purchased from Cell Signaling (Beverly, MA) ...
Papers on Mnk1
Inhibition of MAP Kinase-Interacting Kinase (MNK) Preferentially Affects Translation of mRNAs Containing both a 5'-Terminal Cap and Hairpin.
Rhoads et al., Shreveport, United States. In J Biol Chem, Jan 2016
UNASSIGNED: The mitogen-activated protein kinase-interacting kinases 1 and 2 (MNK1 and MNK2) are activated by extracellular-signal-regulated kinases 1 and 2 (ERK1/2) or p38 in response to cellular stress and extracellular stimuli that include growth factors, cytokines, and hormones.
Characterization of MNK1b DNA Aptamers That Inhibit Proliferation in MDA-MB231 Breast Cancer Cells.
González et al., Madrid, Spain. In Mol Ther Nucleic Acids, Dec 2015
The selected aptamers were highly specific against MNK1, showing higher affinity to MNK1b than to MNK1a.
Requirement of the eukaryotic translation initiation factor 4F complex in hepatitis E virus replication.
Pan et al., Rotterdam, Netherlands. In Antiviral Res, Dec 2015
Notably, phosphorylation of eIF4E induced by MNK1/2 activation is not involved in HEV replication.
Src Inhibition Blocks c-Myc Translation and Glucose Metabolism to Prevent the Development of Breast Cancer.
Yu et al., Houston, United States. In Cancer Res, Dec 2015
Mechanistic investigations revealed that Src blockade reduced glucose metabolism as a result of an inhibition in ERK1/2-MNK1-eIF4E-mediated cap-dependent translation of c-Myc and transcription of the glucose transporter GLUT1, thereby limiting energy available for cell growth.
Translational control of PML contributes to TNFα-induced apoptosis of MCF7 breast cancer cells and decreased angiogenesis in HUVECs.
Kao et al., Cleveland, United States. In Cell Death Differ, Oct 2015
In this study, we uncover a novel mechanism of PML gene regulation in which the p38 MAPK and its downstream kinase MAP kinase-activated protein kinase 1 (MNK1) mediate TNFα-induced PML protein accumulation and PML NB formation.
Ribosome biogenesis adaptation in resistance training-induced human skeletal muscle hypertrophy.
Blazevich et al., Auckland, New Zealand. In Am J Physiol Endocrinol Metab, Aug 2015
Acute RE-induced activation of the ERK and mTOR pathways were similar before and after RT, as assessed by phosphorylation of ERK, MNK1, p70S6K, and S6 ribosomal protein 1 h postexercise.
Therapeutic potential of targeting IRES-dependent c-myc translation in multiple myeloma cells during ER stress.
Lichtenstein et al., Los Angeles, United States. In Oncogene, Jun 2015
IRES activity was dependent on upstream MAPK (mitogen-activated protein kinase) and MNK1 (MAPK-interacting serine/threonine kinase 1) signaling.
Ligustrazine Suppresses the Growth of HRPC Cells through the Inhibition of Cap- Dependent Translation Via Both the mTOR and the MEK/ERK Pathways.
Xu et al., Chongqing, China. In Anticancer Agents Med Chem, 2014
In addition, the transient overexpression of eIF4E or MNK1 prevents the Ligustrazine-induced inhibition of proliferation and confers significant protection against Ligustrazine-induced apoptosis.
Simplified molecular input line entry system-based: QSAR modelling for MAP kinase-interacting protein kinase (MNK1).
Achary et al., Bhubaneshwar, India. In Sar Qsar Environ Res, 2014
Quantitative structure-activity relationship (QSAR) models were built for the prediction of inhibition (pIC50, i.e. negative logarithm of the 50% effective concentration) of MAP kinase-interacting protein kinase (MNK1) by 43 potent inhibitors.
Structure and function of MK5/PRAK: the loner among the mitogen-activated protein kinase-activated protein kinases.
Kostenko et al., Tromsø, Norway. In Biol Chem, 2013
Eleven mammalian MAPK-activated protein kinases have been identified, and they are divided into five subgroups: the ribosomal-S6-kinases RSK1-4, the MAPK-interacting kinases MNK1 and 2, the mitogen- and stress-activated kinases MSK1 and 2, the MAPK-activated protein kinases MK2 and 3, and the MAPK-activated protein kinase MK5 (also referred to as PRAK).
Notch-RBP-J signaling regulates the transcription factor IRF8 to promote inflammatory macrophage polarization.
Hu et al., New York City, United States. In Nat Immunol, 2012
RBP-J promoted the synthesis of IRF8 protein by selectively augmenting kinase IRAK2-dependent signaling via TLR4 to the kinase MNK1 and downstream translation-initiation control through eIF4E.
MNK1 expression increases during cellular senescence and modulates the subcellular localization of hnRNP A1.
Hubbard et al., New York City, United States. In Exp Cell Res, 2012
These data suggest that MNK1 regulates the phosphorylation and the subcellular distribution of hnRNP A1 and that MNK1 may play a role in the induction of senescence
Phosphorylation of eukaryotic translation initiation factor 4G1 (eIF4G1) by protein kinase C{alpha} regulates eIF4G1 binding to Mnk1.
Gromeier et al., Durham, United States. In Mol Cell Biol, 2011
Data show that PKCalpha activation elicits a cascade of orchestrated phosphorylation events that may modulate eIF4G1 structure and control interaction with the eIF4E kinase, Mnk1.
MAP kinase-interacting kinase 1 regulates SMAD2-dependent TGF-β signaling pathway in human glioblastoma.
Hemmings et al., Basel, Switzerland. In Cancer Res, 2011
Findings offer insights into how MNK1 pathways control translation of cancer-related mRNAs including SMAD2, a key component of the TGF-beta signaling pathway.
Essential role for Mnk kinases in type II interferon (IFNgamma) signaling and its suppressive effects on normal hematopoiesis.
Platanias et al., Chicago, United States. In J Biol Chem, 2011
siRNA-mediated Mnk1/2 knockdown results in partial reversal of the suppressive effects of IFNgamma on human CD34+-derived myeloid (CFU-GM) and erythroid (BFU-E) progenitors.
Cross-talk between protein kinase A and the MAPK-activated protein kinases RSK1 and MK5.
Moens et al., Tromsø, Norway. In J Recept Signal Transduct Res, 2011
The MAPKAPK family includes the ribosomal-S6-kinases (RSK1-4), the MAPK-interacting kinases (MNK1 and 2), the mitogen-and stress-activated kinases (MSK1 and 2), and the MAPKAPK (MK2, 3, and 5) subfamilies.
Simultaneous inhibition of mTOR-containing complex 1 (mTORC1) and MNK induces apoptosis of cutaneous T-cell lymphoma (CTCL) cells.
Wasik et al., Philadelphia, United States. In Plos One, 2010
These findings indicate that the combined inhibition of mTORC1 and MNK may prove beneficial in the treatment of cutaneous T-cell lymphoma and other malignancies.
Protein kinases as small molecule inhibitor targets in inflammation.
Asadullah et al., Hannover, Germany. In Curr Med Chem, 2006
We describe the progress made to develop inhibitors against Toll-like receptor associated kinases (IRAKs), against the MAPK kinase kinases Cot/Tpl-2 and TAK1, against Inhibitor-kappaB kinases (IKKs), against MAPK kinases (MEKs, MKKs), against MAPKs (ERK2, p38, JNKs) and against their downstream kinases MNK1 and MK2/3.
A conserved docking motif in MAP kinases common to substrates, activators and regulators.
Nishida et al., Kyoto, Japan. In Nat Cell Biol, 2000
A docking domain in extracellular-signal-regulated kinase (ERK), a MAPK, serves as a common site for binding to the MAPK kinase MEK1, the MAPK-activated protein kinase MNK1 and the MAPK phosphatase MKP3.
eIF4E activity is regulated at multiple levels.
Gingras et al., Montréal, Canada. In Int J Biochem Cell Biol, 1999
(2) eIF4E is phosphorylated following activation of the MNK1 kinase, a substrate of the ERK and p38 MAPKs.
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