Casein Kinase II
Casein Kinases
Caseins
Casein Kinase I
Protein Kinases
Casein Kinase Iepsilon
Phosphorylation
Protein-Serine-Threonine Kinases
Casein Kinase Idelta
Casein Kinase Ialpha
Calcium-Calmodulin-Dependent Protein Kinase Type 2
Calcium-Calmodulin-Dependent Protein Kinases
Amino Acid Sequence
Molecular Sequence Data
Serine
Peptide Mapping
Substrate Specificity
Dichlororibofuranosylbenzimidazole
Phosphatidylinositol 3-Kinases
Protein Kinase C
MAP Kinase Signaling System
Cyclic AMP-Dependent Protein Kinases
Phosphothreonine
Base Sequence
CDC2 Protein Kinase
Protein Binding
Cattle
Electrophoresis, Polyacrylamide Gel
Cloning, Molecular
Enzyme Activation
src-Family Kinases
Threonine
Isoenzymes
Binding Sites
Macromolecular Substances
Rabbits
Benzylamines
Sequence Homology, Amino Acid
Signal Transduction
DNA-Binding Proteins
Recombinant Fusion Proteins
Phosvitin
Empty Sella Syndrome
p38 Mitogen-Activated Protein Kinases
Mutation
Transfection
Mutagenesis, Site-Directed
Chromatography, Ion Exchange
Precipitin Tests
Enzyme Inhibitors
HeLa Cells
Heparin
Cell Nucleus
Blotting, Western
Mitogen-Activated Protein Kinase 1
Phosphoprotein Phosphatases
Adenosine Triphosphate
JNK Mitogen-Activated Protein Kinases
Glycogen Synthase Kinases
Protein-Tyrosine Kinases
Calmodulin-Binding Proteins
Phosphorus Radioisotopes
Cyclin-Dependent Kinases
Protein Structure, Tertiary
p21-Activated Kinases
Immunoblotting
Transcription Factors
Calcium
Amino Acids
Trypsin
Mitogen-Activated Protein Kinase Kinases
Reticulocytes
DNA
Cells, Cultured
Nuclear Proteins
Peptide Fragments
Parental Consent
Transcription, Genetic
Tumor Cells, Cultured
Peptides
Ribosomal Protein S6 Kinases
Gene Expression Regulation, Enzymologic
Lansoprazole
Proto-Oncogene Proteins
Cytosol
Cytoplasm
Creatine Kinase
Protein Processing, Post-Translational
Saccharomyces cerevisiae
MAP Kinase Kinase Kinases
Guanosine Triphosphate
Nucleoplasmins
Mitogen-Activated Protein Kinases
Chromatography, Affinity
Cyclic AMP
Carrier Proteins
Spermine
DNA Primers
DNA Topoisomerases, Type II
Pyruvate Kinase
Electrophoresis, Gel, Two-Dimensional
Consensus Sequence
Proteins
DNA, Complementary
Brain
RNA, Messenger
Extracellular Signal-Regulated MAP Kinases
MAP Kinase Kinase 1
Structure-Activity Relationship
Sequence Alignment
1-(5-Isoquinolinesulfonyl)-2-Methylpiperazine
Receptor Protein-Tyrosine Kinases
Thymidine Kinase
Liver
Glutathione Transferase
Cell Cycle
Escherichia coli
Coated Vesicles
I-kappa B Kinase
Models, Biological
Phosphotransferases (Alcohol Group Acceptor)
MAP Kinase Kinase 4
3T3 Cells
Saccharomyces cerevisiae Proteins
Intracellular Signaling Peptides and Proteins
Caenorhabditis
Membrane Proteins
Cyclin-Dependent Kinase 5
Xenopus laevis
1-Phosphatidylinositol 4-Kinase
Chromatography, High Pressure Liquid
Cell Membrane
rho-Associated Kinases
CDC2-CDC28 Kinases
Chromatography, Gel
Immunosorbent Techniques
Mitosis
Myosin-Light-Chain Kinase
Autoradiography
Isoquinolines
Cell Division
Aurora Kinases
Calcium-Binding Proteins
Tyrosine
Plasmids
Mass Spectrometry
Proto-Oncogene Proteins c-akt
Protein Kinase C-delta
Glycyrrhizic Acid
Cricetinae
Protein Kinase C-alpha
GAP-43 Protein
Cell Cycle Proteins
Adaptor Proteins, Signal Transducing
Drosophila
Restriction Mapping
Artemia
Period Circadian Proteins
Drosophila melanogaster
Receptor, IGF Type 2
Apoptosis
Diacylglycerol Kinase
Protein Conformation
Protein Transport
Phloroglucinol
Tetradecanoylphorbol Acetate
Cyclic GMP-Dependent Protein Kinases
Fibroblasts
AMP-Activated Protein Kinases
Transcriptional Activation
Catalysis
Sequence Homology, Nucleic Acid
Gene Expression Regulation
Dose-Response Relationship, Drug
Alkaline Phosphatase
Cercopithecus aethiops
NF-kappa B
Insulin
Okadaic Acid
Rats, Sprague-Dawley
Protein Phosphatase 1
Eukaryotic Initiation Factor-2B
Dietary Proteins
Epidermal Growth Factor
Focal Adhesion Kinase 1
Phosphorylation of the DNA repair protein APE/REF-1 by CKII affects redox regulation of AP-1. (1/1209)
The DNA repair protein apurinic endonuclease (APE/Ref-1) exerts several physiological functions such as cleavage of apurinic/apyrimidinic sites and redox regulation of the transcription factor AP-1, whose activation is part of the cellular response to DNA damaging treatments. Here we demonstrate that APE/Ref-1 is phosphorylated by casein kinase II (CKII). This was shown for both the recombinant APE/Ref-1 protein (Km=0.55 mM) and for APE/Ref-1 expressed in COS cells. Phosphorylation of APE/Ref-1 did not alter the repair activity of the enzyme, whereas it stimulated its redox capability towards AP-1, thus promoting DNA binding activity of AP-1. Inhibition of CKII mediated phosphorylation of APE/Ref-1 blocked mutagen-stimulated increase in AP-1 binding. It also abrogated the induction of c-Jun protein and rendered cells more sensitive to induced DNA damage. Thus, phosphorylation of APE/Ref-1 appears to be involved in regulating the different physiological activities of the enzyme. CKII mediated phosphorylation of APE/Ref-1 and concomitant increase in AP-1 binding activity appears to be a novel mechanism of cellular stress response, forcing transcription of AP-1 target gene(s) the product(s) of which may exert protective function. (+info)Allosteric regulation of even-skipped repression activity by phosphorylation. (2/1209)
The Drosophila homeodomain protein Even-skipped (Eve) is a well characterized transcriptional repressor. Here, we show that Eve's ability to function in vitro is negatively regulated by phosphorylation. DNA-binding activity was unaffected by phosphorylation, but phosphorylated Eve was unable to interact with the TATA-binding protein (TBP), a known target for repression. Unexpectedly, phosphorylation of the Eve N terminus, which is dispensable for repression and TBP binding, was necessary and sufficient to inactivate Eve. LiCl, which specifically inhibits glycogen synthase kinase-3 (GSK-3), reduced Eve phosphorylation in nuclear extract and blocked inhibition of repression. In addition, Eve was phosphorylated and inactivated by purified GSK-3 beta plus casein kinase II. Our results suggest a novel mechanism of transcriptional control involving phosphorylation-induced allosteric interference with a repressive protein-protein interaction. (+info)Phosphorylation of yeast TBP by protein kinase CK2 reduces its specific binding to DNA. (3/1209)
Protein kinase CK2 is a ubiquitous Ser/Thr kinase which phosphorylates a large number of proteins including several transcription factors. Recombinant Xenopus laevis CK2 phosphorylates both recombinant Saccharomyces cerevisiae and Schizosaccharomyces pombe TATA binding protein (TBP). The phosphorylation of TBP by CK2 reduces its binding activity to the TATA box. CK2 copurifies with the transcription factor IID (TFIID) complex from HeLa cell extracts and phosphorylates several of the TBP-associated factors within TFIID. Taken together these findings argue for a role of CK2 in the control of transcription by RNA polymerase II through the modulation of the binding activity of TBP to the TATA box. (+info)Phosphorylation of the medium chain subunit of the AP-2 adaptor complex does not influence its interaction with the tyrosine based internalisation motif of TGN38. (4/1209)
Tyrosine based motifs conforming to the consensus YXXphi (where phi represents a bulky hydrophobic residue) have been shown to interact with the medium chain subunit of clathrin adaptor complexes. These medium chains are targets for phosphorylation by a kinase activity associated with clathrin coated vesicles. We have used the clathrin coated vesicle associated kinase activity to specifically phosphorylate a soluble recombinant fusion protein of mu2, the medium chain subunit of the plasma membrane associated adaptor protein complex AP-2. We have tested whether this phosphorylation has any effect on the interaction of mu2 with the tyrosine based motif containing protein, TGN38, that has previously been shown to interact with mu2. Phosphorylation of mu2 was shown to have no significant effect on the in vitro interaction of mu2 with the cytosolic domain of TGN38, indicating that reversible phosphorylation of mu2 does not play a role in regulating its direct interaction with tyrosine based internalisation motifs. In addition, although a casein kinase II-like activity has been shown to be associated with clathrin coated vesicles, we show that mu2 is not phosphorylated by casein kinase II implying that another kinase activity is present in clathrin coated vesicles. Furthermore the kinase activity associated with clathrin coated vesicles was shown to be capable of phosphorylating dynamin 1. Phosphorylation of dynamin 1 has previously been shown to regulate its interaction with other proteins involved in clathrin mediated endocytosis. (+info)Phosphorylation of CD45 by casein kinase 2. Modulation of activity and mutational analysis. (5/1209)
CD45 is a receptor-type protein-tyrosine phosphatase (PTP) that is required for antigen-specific stimulation and proliferation in lymphocytes. This study was designed to determine the nature of specific kinases in lymphocytes that phosphorylate CD45 and to determine the effect of phosphorylation on CD45 PTP activity. A major cytoplasmic lymphocyte kinase that phosphorylated CD45 was identified as casein kinase 2 (CK2) by use of an in-gel kinase assay in combination with immunoprecipitation, immunodepletion, and specific inhibition. Mutational analysis of CK2 consensus sites showed that the target for CK2 was in an acidic insert of 19 amino acids in the D2 domain, and Ser to Ala mutations at amino acids 965, 968, 969, and 973 abrogated CK2 phosphorylation of CD45. CK2 phosphorylation increased CD45 activity 3-fold toward phosphorylated myelin basic protein, and this increase was reversible by PP2A treatment. Mutation of Ser to Glu at the CK2 sites had the same effect as phosphorylation and also tripled the Vmax of CD45. CD45 isolated in vivo was highly phosphorylated and could not be phosphorylated by CK2 without prior dephosphorylation with phosphatase PP2A. We conclude that CK2 is a major lymphocyte kinase that is responsible for in vivo phosphorylation of CD45, and phosphorylation at specific CK2 sites regulates CD45 PTP activity. (+info)A modulatory role for clathrin light chain phosphorylation in Golgi membrane protein localization during vegetative growth and during the mating response of Saccharomyces cerevisiae. (6/1209)
The role of clathrin light chain phosphorylation in regulating clathrin function has been examined in Saccharomyces cerevisiae. The phosphorylation state of yeast clathrin light chain (Clc1p) in vivo was monitored by [32P]phosphate labeling and immunoprecipitation. Clc1p was phosphorylated in growing cells and also hyperphosphorylated upon activation of the mating response signal transduction pathway. Mating pheromone-stimulated hyperphosphorylation of Clc1p was dependent on the mating response signal transduction pathway MAP kinase Fus3p. Both basal and stimulated phosphorylation occurred exclusively on serines. Mutagenesis of Clc1p was used to map major phosphorylation sites to serines 52 and 112, but conversion of all 14 serines in Clc1p to alanines [S(all)A] was necessary to eliminate phosphorylation. Cells expressing the S(all)A mutant Clc1p displayed no defects in Clc1p binding to clathrin heavy chain, clathrin trimer stability, sorting of a soluble vacuolar protein, or receptor-mediated endocytosis of mating pheromone. However, the trans-Golgi network membrane protein Kex2p was not optimally localized in mutant cells. Furthermore, pheromone treatment exacerbated the Kex2p localization defect and caused a corresponding defect in Kex2p-mediated maturation of the alpha-factor precursor. The results reveal a novel requirement for clathrin during the mating response and suggest that phosphorylation of the light chain subunit modulates the activity of clathrin at the trans-Golgi network. (+info)Antisense expression of the CK2 alpha-subunit gene in Arabidopsis. Effects on light-regulated gene expression and plant growth. (7/1209)
The protein kinase CK2 (formerly casein kinase II) is thought to be involved in light-regulated gene expression in plants because of its ability to phosphorylate transcription factors that bind to the promoter regions of light-regulated genes in vitro. To address this possibility in vivo and to learn more about the potential physiological roles of CK2 in plants, we transformed Arabidopsis with an antisense construct of the CK2 alpha-subunit gene and investigated both morphological and molecular phenotypes. Antisense transformants had a smaller adult leaf size and showed increased expression of chs in darkness and of cab and rbcS after red-light treatment. The latter molecular phenotype implied that CK2 might serve as one of several negative and quantitative effectors in light-regulated gene expression. The possible mechanism of CK2 action and its involvement in the phytochrome signal transduction pathway are discussed. (+info)Nuclear matrix targeting of the protein kinase CK2 signal as a common downstream response to androgen or growth factor stimulation of prostate cancer cells. (8/1209)
Protein kinase CK2, a messenger-independent serine/threonine kinase, has been implicated in cell growth. Androgenic stimulus in rat prostate modulates its association with nuclear matrix (NM) and chromatin. Because the growth of human prostate carcinoma cells is influenced by androgens and/or growth factors, we determined the nature of CK2 signaling in the NM in response to androgen and growth factor stimuli. Androgen-sensitive LNCaP and androgen-insensitive PC-3 cells were cultured in media to regulate their growth in the presence of 5alpha-dihydrotestosterone (5alpha-DHT) or growth factors (epidermal growth factor, keratinocyte growth factor, and transforming growth factor alpha). The activity of CK2 was measured in the cytosolic and NM fractions isolated from these cells after treatment with growth stimuli. The changes in CK2 in various fractions were also confirmed by immunoblotting with a specific antibody. LNCaP cells responded to both 5alpha-DHT and growth factors for growth. The presence of these agents in the culture medium evoked a translocation of CK2 to the NM from the cytosol. The PC-3 cells did not respond to 5alpha-DHT for growth but did respond to growth factors. Under these conditions, there was also a translocation of CK2 to the NM concomitant with a decrease in the cytosolic fraction. These results suggest that CK2 translocation to the NM occurs in response to various growth stimuli in cells in culture. Thus, CK2 is a common downstream signal transducer in response to diverse growth stimuli that may relate to the pathobiology of prostate cancer cells. (+info)The symptoms of ESS can vary depending on the specific hormone deficiency present and may include:
1. Growth retardation in children
2. Short stature as an adult
3. Delayed puberty or irregular menstrual cycles in females
4. Hypothyroidism (low thyroid hormone levels)
5. Adrenal insufficiency (low cortisol levels)
6. Infertility or irregular menstrual cycles in females
7. Erectile dysfunction or decreased libido in males
8. Fatigue, weakness, and malaise
9. Headaches, vision problems, or other symptoms related to hormone deficiencies.
The exact cause of empty sella syndrome is not fully understood, but it is believed to be due to a combination of genetic and environmental factors. Some cases have been linked to a family history of the condition, while others may be caused by a tumor or other structural abnormality in the pituitary gland.
There is no specific treatment for empty sella syndrome, but hormone replacement therapy may be recommended to treat any underlying hormone deficiencies. In some cases, surgery may be necessary to remove a tumor or other structural abnormality in the pituitary gland. The prognosis for ESS varies depending on the specific cause of the condition and the presence of any underlying hormone deficiencies. With appropriate treatment, many individuals with ESS can lead normal lives, but some may experience ongoing symptoms or complications related to hormone deficiencies.
Casein kinase 2
Casein kinase 2, alpha 1
Casein kinase 1
Casein kinase 1, alpha 1
Casein kinase 1 isoform epsilon
EEF1B2
Progesterone receptor
BRCA1
Myc
SMIM19
Thymosin α1
Nucleolin
Gap-43 protein
ARR3
AP3B1
TEDDM1
CCDC113
DNA damage-inducible transcript 3
Globozoospermia
Nucleolar phosphoprotein p130
JADE1
Calsequestrin
STARD10
LIG1
HNRNPA2B1
Glial cell line-derived neurotrophic factor
Silmitasertib
Activating transcription factor 2
Epithelial-mesenchymal transition
60S ribosomal protein L5
Herpes simplex virus protein vmw65
WNT3A
Index of biochemistry articles
PF-4800567
Anticancer gene
Cyclin-dependent kinase 1
SCF complex
Period (gene)
Shellfish allergy
CHKA
Glutamate-rich protein 4
FER (gene)
Jay Dunlap
Collagen, type XVII, alpha 1
FKBP3
LOC100287387
Forkhead box protein O1
PSMA3
CDC25B
Facioscapulohumeral muscular dystrophy
Phenolic content in wine
PIN1
Homeobox protein Nkx-2.5
PAK1
CSN1S1
IWS1
AP3B2
CTP synthetase
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Phosphorylation9
- To identify proteins that interact with TH following phosphorylation of serine 19, this amino acid was mutated to alanine and THS19A was used as bait in a yeast two-hybrid system. (nih.gov)
- In vitro kinase assay and bioinformatic analysis indicated phosphorylation of NRL at Ser117 residue by CK2. (nih.gov)
- Phosphorylation site motif analyses implicate casein kinase II and calcium/calmodulin dependent kinases among the primary light-dark transition kinases. (biorxiv.org)
- The majority of the phosphorylation takes place at Ser or Thr residues embedded within acidic sequences, and therefore are targets for casein kinase I (CK1) or casein kinase II (CK2)-like kinases. (northwestern.edu)
- In turn, CK2 activity may be initiated only after an initial phosphorylation of one of the messenger-dependent kinases. (northwestern.edu)
- Synthesized peptide derived from human Casein Kinase IIβ around the non-phosphorylation site of S209. (afgsci.com)
- GlcNAcylation is also often reciprocal to phosphorylation and occurs at protein sites identical to those used by kinases that regulate cell growth (see figure). (nih.gov)
- GlcNAcylation is Thr-58 (see figure), which is also the major phosphorylation site used by glycogen-synthetase-kinase-3 and is the major mutational "hotspot" in human lymphomas. (nih.gov)
- High Expression of Casein Kinase 2 Alpha Is Responsible for Enhanced Phosphorylation of DNA Mismatch Repair Protein MLH1 and Increased Tumor Mutation Rates in Colorectal Cancer. (cdc.gov)
Serine2
- Casein kinase II is a serine/threonine protein kinase that phosphorylates acidic proteins such as casein. (nih.gov)
- Catalytic subunit of a constitutively active serine/threonine-protein kinase complex that phosphorylates a large number of substrates containing acidic residues C-terminal to the phosphorylated serine or threonine. (nih.gov)
Cyclin-depend2
Proteins4
- Casein kinase II has been shown to phosphorylate a large number of substrates, many of which are proteins involved in the regulation of gene expression. (nih.gov)
- Three transcript variants encoding two different proteins have been found for this gene. (nih.gov)
- expression of these proteins is maintained in carcinoma cells lines [6], and expression of these two proteins induces immortalization and transformation in a variety of rodent and human cell types [54]. (nih.gov)
- Figures 2 and 3 illustrate sequence similarities between the E7 proteins of various HPV types, and similarities between the E7 protein and other viral oncoproteins, respectively. (nih.gov)
Subunits3
- A ubiquitous casein kinase that is comprised of two distinct catalytic subunits and dimeric regulatory subunit. (nih.gov)
- The kinase exists as a tetramer and is composed of an alpha, an alpha-prime, and two beta subunits. (nih.gov)
- The active form of CK2 is a tetrameric holoenzyme, with 2 α catalytic subunits and 2 β regulatory subunits. (northwestern.edu)
Regulates3
- Casein kinase 2a regulates glioblastoma brain tumor-initiating cell growth through the ß-catenin pathway. (stanford.edu)
- This gene encodes the beta subunit of casein kinase II, a ubiquitous protein kinase which regulates metabolic pathways, signal transduction, transcription, translation, and replication. (nih.gov)
- Caption: Casein kinase 1 (CK1) regulates PERIOD, a core protein in the biological clock of people. (nih.gov)
Ubiquitous1
- They are ubiquitous, constitutively active, second-messenger-independent kinases. (northwestern.edu)
Phosphoinositide1
- However, the phase 2 trial that led to February 2021 approvals found the drug's safety profile to be "manageable," with serious adverse reactions reported in 18% of patients receiving the dual oral inhibitor of phosphoinositide 3 kinase delta and casein kinase 1 epsilon. (medscape.com)
Genes2
- Loss of CK2α decreased two β-catenin-regulated genes that are involved in GBM-initiating cell growth, OCT4 and NANOG. (stanford.edu)
- La caseína cinasa II fosforila un gran número de sustratos, muchos de los cuales son proteínas implicadas en la regulación de la expresión de los genes. (bvsalud.org)
Gene2
Alpha1
- This domain can be divided into two all-alpha subdomains. (embl.de)
Inhibitor1
- It is an inhibitor of casein kinase I. (mcw.edu)
Regulation1
- During our studies to elucidate NRL-mediated transcriptional regulation, we identified protein kinase CK2 in NRL-enriched complexes bound to Rho promoter-enhancer regions and in NRL-enriched high molecular mass fractions from the bovine retina. (nih.gov)
Vitro1
- Previous research has demonstrated that casein kinase 2 (CK2) interacts with CDK11p110, and both were observed to phosphorylate TH in vitro. (nih.gov)
20211
- The FDA granted accelerated approval to umbralisib in February 2021 for patients with two types of lymphoma: adults with relapsed or refractory marginal zone lymphoma who received at least one prior therapy, and those with relapsed or refractory follicular lymphoma who received at least three prior therapies. (medscape.com)
Regulatory1
- Studies are under way to evaluate the effects of glycosylation on kinase activity and subcellular trafficking of this regulatory protein. (nih.gov)
Enzyme2
Expression3
- Exogenous expression of GGT7 resulted in a 2- to 3-fold reduction in proliferation and anchorage-independent growth under minimal growth conditions (1% serum). (stanford.edu)
- Decreasing GGT7 expression using either short interfering RNA or short hairpin RNA consistently increased proliferation 1.5- to 2-fold. (stanford.edu)
- In addition, intracranial injections of U87-MG cells with reduced GGT7 expression increased tumor growth in mice approximately 2-fold, and decreased mouse survival. (stanford.edu)
Sensitizes1
- 2. Casein kinase 2 inhibition sensitizes medulloblastoma to temozolomide. (nih.gov)
20222
Distinct1
- Gu XL and Wei Lu (2018) Genetic deletion of NMDA receptors suppresses GABAergic synaptic transmission in two distinct types of central neurons . (nih.gov)
Mutations1
- In addition, cancer cells can escape from physiological suppressors and have metastasis properties with the mutations they undergo [ 2 , 3 ]. (hindawi.com)
Asthma2
- 10 A genome wide screen was undertaken using phenotypic data and DNA from 362 families in Wessex and 98 in the USA with at least two siblings with asthma. (bmj.com)
- The addition of 13 more markers at 1-2 cM intervals increased the MLS to 2.94 at D20S482 (12.1 cM) which further increased to 3.93 when BHR was included in the definition of asthma (despite halving the sample size), thereby exceeding the threshold for genome wide significance. (bmj.com)
Shown2
Cell2
- Initial studies showed that two GBM cell lines (U87-MG and U138) transduced with CK2α had enhanced proliferation and anchorage-independent growth. (stanford.edu)
- The phase III PROCLAIM trial, recently published in the Journal of Clinical Oncology entitled "PROCLAIM: randomized phase III trial of pemetrexed-cisplatin or etoposide-cisplatin plus thoracic radiation therapy followed by consolidation chemotherapy in locally advanced nonsquamous non-small-cell lung cancer", compared two different chemotherapy regimens given concurrently with radiotherapy in patients with stage III non-squamous lung cancer: pemetrexed plus cisplatin versus cisplatin plus etoposide [ 2 ]. (oncotarget.com)
Intervals1
- And then sonicate the sample for 1 min (under ice water bath conditions) with 2 s' sonication and 2 s' intervals to make cells fully lysis and reduce the viscosity of sample. (elabscience.com)