Search results for "MAP2"

showing 10 items of 17 documents

Activation of a nuclear-localized SIPK in tobacco cells challenged by cryptogein, an elicitor of plant defence reactions.

2009

When a plant cell is challenged by a well-defined stimulus, complex signal transduction pathways are activated to promote the modulation of specific sets of genes and eventually to develop adaptive responses. In this context, protein phosphorylation plays a fundamental role through the activation of multiple protein kinase families. Although the involvement of protein kinases at the plasma membrane and cytosolic levels are now well-documented, their nuclear counterparts are still poorly investigated. In the field of plant defence reactions, no known study has yet reported the activation of a nuclear protein kinase and/or its nuclear activity in plant cells, although some protein kinases, e.…

0106 biological sciencesMAPK/ERK pathwayMolecular Sequence DataActive Transport Cell NucleusBiology01 natural sciencesBiochemistryMAP2K703 medical and health sciencesCytosolTobaccoASK1Protein phosphorylation[SDV.BBM]Life Sciences [q-bio]/Biochemistry Molecular BiologyAmino Acid SequenceNuclear proteinProtein kinase AMolecular BiologyConserved Sequence030304 developmental biologyPlant ProteinsCell Nucleus0303 health sciencesKinasePlant ExtractsAlgal ProteinsLife SciencesCell BiologyCell biologyEnzyme ActivationBiochemistrySignal transductionMitogen-Activated Protein KinasesSequence Alignment010606 plant biology & botanySignal TransductionThe Biochemical journal
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NGS‐based liquid biopsy profiling identifies mechanisms of resistance to ALK inhibitors: a step toward personalized NSCLC treatment

2021

Despite impressive and durable responses, nonsmall cell lung cancer (NSCLC) patients treated with anaplastic lymphoma kinase (ALK) inhibitors (ALK‐Is) ultimately progress due to development of resistance. Here, we have evaluated the clinical utility of circulating tumor DNA (ctDNA) profiling by next‐generation sequencing (NGS) upon disease progression. We collected 26 plasma and two cerebrospinal fluid samples from 24 advanced ALK‐positive NSCLC patients at disease progression to an ALK‐I. These samples were analyzed by NGS and digital PCR. A tool to retrieve variants at the ALK locus was developed (VALK tool). We identified at least one resistance mutation in the ALK locus in ten (38.5%) p…

0301 basic medicineCancer ResearchLung NeoplasmsEML4-ALKAntineoplastic AgentsEML4‐ALKmedicine.disease_causeNSCLCIDH2Circulating Tumor DNA03 medical and health sciencesALK-TKI0302 clinical medicineCarcinoma Non-Small-Cell LungMAP2K1hemic and lymphatic diseasesALK‐TKIGeneticsmedicineHumansAnaplastic lymphoma kinaseAnaplastic Lymphoma KinaseDigital polymerase chain reactionPrecision MedicineLiquid biopsyProtein Kinase InhibitorsneoplasmsResearch ArticlesRC254-282MutationCrizotinibliquid biopsybusiness.industryHigh-Throughput Nucleotide SequencingNeoplasms. Tumors. Oncology. Including cancer and carcinogensGeneral MedicineResistance mutation3. Good health030104 developmental biologyOncologyDrug Resistance Neoplasm030220 oncology & carcinogenesisNGSMutationCancer researchMolecular MedicinebusinessResearch Articlemedicine.drugMolecular Oncology
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Efectos de la exposición crónica al etanol sobre el tráfico intracelular y citoesqueleto como factores implicados en la migración neuronal

2013

El consumo de etanol durante la gestación puede inducir una serie de alteraciones graves en el desarrollo del feto, la manifestación más extrema da lugar al Síndrome Alcohólico Fetal (SAF). La exposición prenatal al alcohol es la causa conocida y, además evitable, más importante de retraso mental en el mundo occidental. Además de déficits cognitivos, los niños con SAF presentan múltiples anomalías estructurales en el sistema nervioso central, como reducción de la masa cerebral, y a nivel celular, daños en la migración neuronal, en el proceso de formación de espinas dendríticas y establecimiento de sinapsis. En la actualidad, los mecanismos moleculares implicados en la teratogénesis inducida…

Central Nervous Systemaparato de Golgietanolespinas dendríticasneuronasneurons:CIENCIAS DE LA VIDA::Neurociencias [UNESCO]migración neuronalMAP2Fetal Alcoholic SyndromeRho GTPasasactinaRho GTPasesendocitosis:CIENCIAS MÉDICAS::Toxicología [UNESCO]endocytosismicrotúbuloneuronal migrationUNESCO::CIENCIAS MÉDICAS::Toxicologíatráfico intracelularUNESCO::CIENCIAS DE LA VIDA::Biología celular::Cultivo celularcytoskeletondendritic spinesSAFSíndrome Alcohólico Fetalcitoesqueleto:CIENCIAS DE LA VIDA::Biología celular::Cultivo celular [UNESCO]Golgi apparatusUNESCO::CIENCIAS DE LA VIDA::Neurocienciasethanolintracellular trafficactinSistema Nervioso Centralmicrotubule
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Interaction of Mitogen-activated Protein Kinases with the Kinase Interaction Motif of the Tyrosine Phosphatase PTP-SL Provides Substrate Specificity …

1999

ERK1 and ERK2 associate with the tyrosine phosphatase PTP-SL through a kinase interaction motif (KIM) located in the juxtamembrane region of PTP-SL. A glutathione S-transferase (GST)-PTP-SL fusion protein containing the KIM associated with ERK1 and ERK2 as well as with p38/HOG, but not with the related JNK1 kinase or with protein kinase A or C. Accordingly, ERK2 showed in vitro substrate specificity to phosphorylate GST-PTP-SL in comparison with GST-c-Jun. Furthermore, tyrosine dephosphorylation of ERK2 by the PTP-SLDeltaKIM mutant was impaired. The in vitro association of ERK1/2 with GST-PTP-SL was highly stable; however, low concentrations of nucleotides partially dissociated the ERK1/2.P…

Cytoplasmanimal structuresProtein Kinase C-alphaRecombinant Fusion ProteinsCèl·lulesNerve Tissue ProteinsProtein tyrosine phosphataseMitogen-activated protein kinase kinaseTransfectionenvironment and public healthBiochemistrySH3 domainReceptor tyrosine kinaseMAP2K7Substrate SpecificitySerineAnimalsc-RafAmino Acid SequenceMolecular BiologyProtein Kinase CSequence DeletionMitogen-Activated Protein Kinase 1Binding SitesMitogen-Activated Protein Kinase 3biologyCyclin-dependent kinase 2Intracellular Signaling Peptides and ProteinsJNK Mitogen-Activated Protein KinasesCell BiologyCyclic AMP-Dependent Protein KinasesIsoenzymesenzymes and coenzymes (carbohydrates)KineticsBiochemistryAmino Acid SubstitutionCOS CellsCalcium-Calmodulin-Dependent Protein Kinasesbiology.proteinMutagenesis Site-DirectedCyclin-dependent kinase 9CattleMitogen-Activated Protein KinasesProtein Tyrosine PhosphatasesProteïnes
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Tumor Necrosis Factor (TNF) Receptor 1 Signaling Downstream of TNF Receptor-associated Factor 2

1997

Like other members of the tumor necrosis factor (TNF) receptor family, p55 TNF receptor 1 (TNF-R1) lacks intrinsic signaling capacity and transduces signals by recruiting associating molecules. The TNF-R1 associated death domain protein interacts with the p55 TNF-R1 cytoplasmic domain and recruits the Fas-associated death domain protein (which directly activates the apoptotic proteases), the protein kinase receptor interacting protein, and TNF receptor-associated factor 2 (TRAF2). TRAF2 has previously been demonstrated to activate both transcription factor nuclear factor kappaB (NFkappaB) and the c-Jun N-terminal kinase/stress-activated protein kinase (JNK/SAPK) pathway, which in turn stimu…

MAP kinase kinase kinasebiologyChemistryCyclin-dependent kinase 2Cell BiologyMitogen-activated protein kinase kinaseBiochemistryProtein kinase RMAP2K7Cancer researchbiology.proteinCyclin-dependent kinase 9ASK1c-RafMolecular BiologyJournal of Biological Chemistry
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Divide and rule: The role of ubiquitination in inactivation of the ERK5-MAPK cascade

2014

Recently, we revealed that ubiquitination of MEKK2 and MEKK3 by inhibitor of apoptosis proteins (IAPs) directly disrupts MEK5/ERK5 interaction and subsequently attenuates ERK5 activation. In addition, loss of XIAP promotes human myogenic differentiation in an ERK5-dependent manner. These results reveal another layer of MAPK regulation and a novel role for XIAP in controlling myogenic differentiation.

MAPK/ERK pathwayInhibitor of apoptosis domainCancer ResearchAkt/PKB signaling pathwayChemistryMAPK cascadeInhibitor of apoptosisMAP2K7XIAPCell biologyCancer researchMolecular MedicineAuthor's ViewProtein kinase BMolecular & Cellular Oncology
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Studies on protein kinases involved in regulation of nucleocytoplasmic mRNA transport

1988

The rate of energy-dependent nucleoside triphosphatase (NTPase)-mediated nucleocytoplasmic translocation of poly(A)-containing mRNA [poly(A)+mRNA] across the nuclear envelope is thought to be regulated by poly(A)-sensitive phosphorylation and dephosphorylation of nuclear-envelope protein. Studying the phosphorylation-related inhibition of the NTPase, we found that phosphorylation of one polypeptide of rat liver envelopes by endogenous NI- and NII-like protein kinase was particularly sensitive to poly(A). This polypeptide (106 kDa) was also phosphorylated by nuclear-envelope-bound Ca2+-activated and phospholipid-dependent protein kinase (protein kinase C). Activation of kinase C by tumour-pr…

MaleCytoplasmNuclear EnvelopeMitogen-activated protein kinase kinasePhosphatidylinositolsBiochemistryMAP2K7AnimalsRNA Messengerc-RafProtein kinase AMolecular BiologyProtein Kinase CProtein kinase CCell NucleusMembrane GlycoproteinsMAP kinase kinase kinasebiologyCyclin-dependent kinase 2Membrane ProteinsNuclear ProteinsBiological TransportRats Inbred StrainsCell BiologyMolecular biologyRatsNuclear Pore Complex ProteinsMicroscopy ElectronLiverBiochemistrybiology.proteinCyclin-dependent kinase 9PeptidesPoly AResearch ArticleBiochemical Journal
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A novel serine/threonine kinase gene, STK33 , on human chromosome 11p15.3

2001

Human chromosomal region 11p15 is known to be associated with several diseases including predispositions to develop various tumor types. In search of candidate genes, a novel human kinase gene is described, STK33, which codes for a serine/threonine protein kinase. The gene was discovered by comparative genome analysis of human chromosome 11p15.3 and its orthologous region on distal mouse chromosome 7. Human STK33 gene contains 12 exons as has been determined by the comparison to the full-length transcript amplified from human uterus RNA. Transcripts are found in a variety of tissues in at least two alternatively spliced forms as revealed by reverse transcriptase-polymerase chain reaction, c…

MaleDNA ComplementaryMolecular Sequence DataGene ExpressionProtein Serine-Threonine KinasesMAP3K7MAP2K7MiceTANK-binding kinase 1GeneticsAnimalsHumansTissue DistributionAmino Acid SequenceRNA Messengerc-RafPhylogenyGeneticsSerine/threonine-specific protein kinaseBase SequenceSequence Homology Amino AcidbiologyChromosomes Human Pair 11Cyclin-dependent kinase 2DNAExonsSequence Analysis DNAGeneral MedicineMolecular biologyIntronsGenesChromosomal regionbiology.proteinFemalePRKCB1Sequence AlignmentGene
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Case report: Noonan syndrome with multiple giant cell lesions and review of the literature.

2012

Noonan syndrome with multiple giant cell lesions (NS/MGCL) was recently shown to be a phenotypic variation within the syndromes of the Ras/MAPK pathway and not an independent entity as previously thought. Here we report on a 13-year-old boy with a typical phenotype of NS including atrial septal defect, pulmonic stenosis, short stature, and combined pectus carinatum/excavatum, pronounced MGCL of both jaws, and a de novo mutation in PTPN11, c.236A>G (which predicts p.Q79R). Mutations in PTPN11 are the most frequent cause of NS and p.Q79R is a recurrent mutation in exon 3. Including this patient, 24 patients with molecularly confirmed NS, LEOPARD, or CFC/MGCL syndrome have been reported to dat…

Maleendocrine systemmedicine.medical_specialtyPathologyAdolescentmedicine.disease_causeShort statureGiant CellsInternal medicineMAP2K1GeneticsmedicineHumansGenetics (clinical)Mutationbusiness.industryNoonan Syndromemedicine.diseasePTPN11EndocrinologyGiant cellSOS1Noonan syndromePectus carinatummedicine.symptombusinessAmerican journal of medical genetics. Part A
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Involvement of protein kinases in the induction of NO synthase II in human DLD-1 cells

1998

Protein phosphorylation is involved in the induction of nitric oxide synthase II (NOS II, iNOS) in several types of animal cells. Here we have investigated the possible involvement of major protein kinases in the induction of NOS II expression in human DLD-1 cells. In DLD-1 cells, interferon-γ alone induced a submaximal NOS II expression; a cytokine mixture consisting of interferon-γ, tumour necrosis factor-α and interleukin-1β produced maximal NOS II induction. Activators of protein kinase A (forskolin, 8-dibutyryl-cyclic AMP), of protein kinase C (tetradecanoylphorbol-13-acetate), and of protein kinase G (8-bromo cyclic GMP) did not induce NOS II mRNA by themselves, nor did they alter NOS…

PharmacologybiologyMAP kinase kinase kinaseCyclin-dependent kinase 4Cyclin-dependent kinase 2biology.proteinCyclin-dependent kinase 9ASK1c-RafMitogen-activated protein kinase kinaseMolecular biologyMAP2K7British Journal of Pharmacology
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