Casein Kinase Iepsilon
Casein Kinases
Casein Kinase Ialpha
Period Circadian Proteins
Casein Kinase II
Protein Kinases
Caseins
Casein Kinase I
Casein Kinase Idelta
Requirement of circadian genes for cocaine sensitization in Drosophila. (1/96)
The circadian clock consists of a feedback loop in which clock genes are rhythmically expressed, giving rise to cycling levels of RNA and proteins. Four of the five circadian genes identified to date influence responsiveness to freebase cocaine in the fruit fly, Drosophila melanogaster. Sensitization to repeated cocaine exposures, a phenomenon also seen in humans and animal models and associated with enhanced drug craving, is eliminated in flies mutant for period, clock, cycle, and doubletime, but not in flies lacking the gene timeless. Flies that do not sensitize owing to lack of these genes do not show the induction of tyrosine decarboxylase normally seen after cocaine exposure. These findings indicate unexpected roles for these genes in regulating cocaine sensitization and indicate that they function as regulators of tyrosine decarboxylase. (+info)double-time is identical to discs overgrown, which is required for cell survival, proliferation and growth arrest in Drosophila imaginal discs. (2/96)
We have isolated the discs overgrown gene of Drosophila and shown that it encodes a homolog of the Casein kinase I(delta)/(epsilon) subfamily and is identical to the double-time gene. However, in contrast to the weak double-time alleles, which appear to affect only the circadian rhythm, discs overgrown alleles, including bona fide null alleles, show strong effects on cell survival and growth control in imaginal discs. Analysis of their phenotypes and molecular lesions suggests that the Discs overgrown protein is a crucial component in the mechanism that links cell survival during proliferation to growth arrest in imaginal discs. This work provides the first analysis in a multicellular organism of Casein kinase I(delta)/(epsilon) functions necessary for survival. Since the amino acid sequences and three-dimensional structures of Casein kinase I(delta)/(epsilon) enzymes are highly conserved, the results suggest that these proteins may also function in controlling cell growth and survival in other organisms. (+info)Two novel doubletime mutants alter circadian properties and eliminate the delay between RNA and protein in Drosophila. (3/96)
Phosphorylation is an important feature of pacemaker organization in Drosophila. Genetic and biochemical evidence suggests involvement of the casein kinase I homolog doubletime (dbt) in the Drosophila circadian pacemaker. We have characterized two novel dbt mutants. Both cause a lengthening of behavioral period and profoundly alter period (per) and timeless (tim) transcript and protein profiles. The PER profile shows a major difference from the wild-type program only during the morning hours, consistent with a prominent role for DBT during the PER monomer degradation phase. The transcript profiles are delayed, but there is little effect on the protein accumulation profiles, resulting in the elimination of the characteristic lag between the mRNA and protein profiles. These results and others indicate that light and post-transcriptional regulation play major roles in defining the temporal properties of the protein curves and suggest that this lag is unnecessary for the feedback regulation of per and tim protein on per and tim transcription. (+info)Short-period mutations of per affect a double-time-dependent step in the Drosophila circadian clock. (4/96)
Circadian (24 hour) PERIOD (PER) protein oscillation is dependent on the double-time (dbt) gene, a casein kinase Ivarepsilon homolog [1-3]. Without dbt activity, hypophosphorylated PER proteins over-accumulate, indicating that dbt is required for PER phosphorylation and turnover [3,4]. There is evidence of a similar role for casein kinase Ivarepsilon in the mammalian circadian clock [5,6]. We have isolated a new dbt allele, dbt(ar), which causes arrhythmic locomotor activity in homozygous viable adults, as well as molecular arrhythmicity, with constitutively high levels of PER proteins, and low levels of TIMELESS (TIM) proteins. Short-period mutations of per, but not of tim, restore rhythmicity to dbt(ar) flies. This suppression is accompanied by a restoration of PER protein oscillations. Our results suggest that short-period per mutations, and mutations of dbt, affect the same molecular step that controls nuclear PER turnover. We conclude that, in wild-type flies, the previously defined PER'short domain' [7,8] may regulate the activity of DBT on PER. (+info)Phosphorylation of period is influenced by cycling physical associations of double-time, period, and timeless in the Drosophila clock. (5/96)
The clock gene double-time (dbt) encodes an ortholog of casein kinase Iepsilon that promotes phosphorylation and turnover of the PERIOD protein. Whereas the period (per), timeless (tim), and dClock (dClk) genes of Drosophila each contribute cycling mRNA and protein to a circadian clock, dbt RNA and DBT protein are constitutively expressed. Robust circadian changes in DBT subcellular localization are nevertheless observed in clock-containing cells of the fly head. These localization rhythms accompany formation of protein complexes that include PER, TIM, and DBT, and reflect periodic redistribution between the nucleus and the cytoplasm. Nuclear phosphorylation of PER is strongly enhanced when TIM is removed from PER/TIM/DBT complexes. The varying associations of PER, DBT and TIM appear to determine the onset and duration of nuclear PER function within the Drosophila clock. (+info)The Drosophila double-timeS mutation delays the nuclear accumulation of period protein and affects the feedback regulation of period mRNA. (6/96)
The Drosophila double-time (dbt) gene, which encodes a protein similar to vertebrate epsilon and delta isoforms of casein kinase I, is essential for circadian rhythmicity because it regulates the phosphorylation and stability of period (per) protein. Here, the circadian phenotype of a short-period dbt mutant allele (dbt(S)) was examined. The circadian period of the dbt(S) locomotor activity rhythm varied little when tested at constant temperatures ranging from 20 to 29 degrees C. However, per(L);dbt(S) flies exhibited a lack of temperature compensation like that of the long-period mutant (per(L)) flies. Light-pulse phase-response curves were obtained for wild-type, the short-period (per(S)), and dbt(S) genotypes. For the per(S) and dbt(S) genotypes, phase changes were larger than those for wild-type flies, the transition period from delays to advances was shorter, and the light-insensitive period was shorter. Immunohistochemical analysis of per protein levels demonstrated that per protein accumulates in photoreceptor nuclei later in dbt(S) than in wild-type and per(S) flies, and that it declines to lower levels in nuclei of dbt(S) flies than in nuclei of wild-type flies. Immunoblot analysis of per protein levels demonstrated that total per protein accumulation in dbt(S) heads is neither delayed nor reduced, whereas RNase protection analysis demonstrated that per mRNA accumulates later and declines sooner in dbt(S) heads than in wild-type heads. These results suggest that dbt can regulate the feedback of per protein on its mRNA by delaying the time at which it is translocated to nuclei and altering the level of nuclear PER during the declining phase of the cycle. (+info)The doubletime and CKII kinases collaborate to potentiate Drosophila PER transcriptional repressor activity. (7/96)
In all genetically studied model organisms, a negative feedback loop of gene expression contributes to the circadian rhythm mechanism. In the Drosophila system, it has been proposed that the delay between the synthesis and function of clock proteins is due to phosphorylation-regulated nuclear entry. To test this hypothesis, we assayed the relationship between PER phosphorylation, nuclear localization, and transcriptional repression activity in cultured S2 cells. The results indicate that the two putative PER kinases DBT and CKII work together to phosphorylate PER and increase repression activity. Experiments combining kinase inhibition with inhibition of PER nuclear export suggest that phosphorylation directly affects PER repression activity and that PER nuclear localization is an indirect consequence of the association of active PER with DNA or chromatin. This interpretation suggests further that the circadian regulation of PER nuclear localization in flies reflects changes in PER transcriptional activity rather than in PER nuclear import or export activity. (+info)Casein kinase Iepsilon modulates the signaling specificities of dishevelled. (8/96)
Wnt signaling is critical to many aspects of development, and aberrant activation of the Wnt signaling pathway can cause cancer. Dishevelled (Dvl) protein plays a central role in this pathway by transducing the signal from the Wnt receptor complex to the beta-catenin destruction complex. Dvl also plays a pivotal role in the planar cell polarity pathway that involves the c-Jun N-terminal kinase (JNK). How functions of Dvl are regulated in these two distinct pathways is not clear. We show that deleting the C-terminal two-thirds of Dvl, which includes the PDZ and DEP domains and is essential for Dvl-induced JNK activation, rendered the molecule a much more potent activator of the beta-catenin pathway. We also found that casein kinase Iepsilon (CKIepsilon), a previously identified positive regulator of Wnt signaling, stimulated Dvl activity in the Wnt pathway, but dramatically inhibited Dvl activity in the JNK pathway. Consistent with this, overexpression of CKIepsilon in Drosophila melanogaster stimulated Wnt signaling and disrupted planar cell polarity. We also observed a correlation between the localization and the signaling activity of Dvl in the beta-catenin pathway and the JNK pathway. Furthermore, by using RNA interference, we demonstrate that the Drosophila CKIepsilon homologue Double time positively regulates the beta-catenin pathway through Dvl and negatively regulates the Dvl-induced JNK pathway. We suggest that CKIepsilon functions as a molecular switch to direct Dvl from the JNK pathway to the beta-catenin pathway, possibly by altering the conformation of the C terminus of Dvl. (+info)Casein Kinase 1 Epsilon (CSNK1E or CK1ε) is a serine/threonine protein kinase that plays a role in various cellular processes, including the regulation of circadian rhythms, DNA damage response, and Wnt signaling pathway. It phosphorylates specific serine and threonine residues on its target proteins, thereby modulating their activity, localization, or stability. Mutations in the CSNK1E gene have been associated with certain human diseases, such as Familiial Advanced Sleep Phase Disorder (FASPD).
Casein kinases are a family of protein kinases that play important roles in various cellular processes, including signal transduction, cell cycle regulation, and DNA damage repair. These enzymes phosphorylate serine and threonine residues on their target proteins by transferring a phosphate group from ATP to the hydroxyl side chain of these amino acids.
There are several isoforms of casein kinases, including Casein Kinase 1 (CK1) and Casein Kinase 2 (CK2), which differ in their structure, substrate specificity, and cellular functions. CK1 is involved in various signaling pathways, such as the Wnt signaling pathway, and regulates processes such as gene transcription, DNA repair, and circadian rhythm. CK2, on the other hand, is a highly conserved serine/threonine protein kinase that plays a role in many cellular processes, including cell division, apoptosis, and transcriptional regulation.
Dysregulation of casein kinases has been implicated in various diseases, including cancer, neurodegenerative disorders, and cardiovascular disease. Therefore, these enzymes are considered important targets for the development of new therapeutic strategies.
Casein Kinase 1 Alpha (CK1α) is a serine/threonine protein kinase that plays a crucial role in various cellular processes, including the regulation of circadian rhythms, DNA damage response, and Wnt signaling pathway. It phosphorylates specific serine and threonine residues on its target proteins, thereby modulating their activity, stability, or localization. CK1α is widely expressed in different tissues and has been implicated in several diseases, such as cancer and neurodegenerative disorders. Inhibition of CK1α has emerged as a potential therapeutic strategy for treating these conditions.
Period (PER) circadian proteins are a group of proteins that play a crucial role in the regulation of circadian rhythms, which are physical, mental, and behavioral changes that follow a daily cycle. They are named after the PERIOD gene, whose protein product is one of the key components of the molecular circadian clock mechanism.
The molecular clock is a self-sustaining oscillator present in most organisms, from cyanobacteria to humans. In mammals, the molecular clock consists of two interlocking transcriptional-translational feedback loops that generate rhythmic expression of clock genes and their protein products with a period of approximately 24 hours.
The primary loop involves the positive regulators CLOCK and BMAL1, which heterodimerize and bind to E-box elements in the promoter regions of target genes, including PERIOD (PER) and CRYPTOCHROME (CRY) genes. Upon transcription and translation, PER and CRY proteins form a complex that translocates back into the nucleus, where it inhibits CLOCK-BMAL1-mediated transcription, thereby suppressing its own expression. After a certain period, the repressive complex dissociates, allowing for another cycle of transcription and translation to occur.
The second loop involves the regulation of additional clock genes such as REV-ERBα and RORα, which compete for binding to ROR response elements (ROREs) in the BMAL1 promoter, thereby modulating its expression level. REV-ERBα also represses PER and CRY transcription by recruiting histone deacetylases (HDACs) and nuclear receptor corepressor 1 (NCOR1).
Overall, Period circadian proteins are essential for the proper functioning of the molecular clock and the regulation of various physiological processes, including sleep-wake cycles, metabolism, hormone secretion, and cellular homeostasis. Dysregulation of these proteins has been implicated in several diseases, such as sleep disorders, metabolic syndromes, and cancer.
Casein Kinase II (CK2) is a serine/threonine protein kinase that is widely expressed in eukaryotic cells and is involved in the regulation of various cellular processes. It is a heterotetrameric enzyme, consisting of two catalytic subunits (alpha and alpha') and two regulatory subunits (beta).
CK2 phosphorylates a wide range of substrates, including transcription factors, signaling proteins, and other kinases. It is known to play roles in cell cycle regulation, apoptosis, DNA damage response, and protein stability, among others. CK2 activity is often found to be elevated in various types of cancer, making it a potential target for cancer therapy.
Protein kinases are a group of enzymes that play a crucial role in many cellular processes by adding phosphate groups to other proteins, a process known as phosphorylation. This modification can activate or deactivate the target protein's function, thereby regulating various signaling pathways within the cell. Protein kinases are essential for numerous biological functions, including metabolism, signal transduction, cell cycle progression, and apoptosis (programmed cell death). Abnormal regulation of protein kinases has been implicated in several diseases, such as cancer, diabetes, and neurological disorders.
Caseins are a group of phosphoproteins found in the milk of mammals, including cows and humans. They are the major proteins in milk, making up about 80% of the total protein content. Caseins are characterized by their ability to form micelles, or tiny particles, in milk when it is mixed with calcium. This property allows caseins to help transport calcium and other minerals throughout the body.
Caseins are also known for their nutritional value, as they provide essential amino acids and are easily digestible. They are often used as ingredients in infant formula and other food products. Additionally, caseins have been studied for their potential health benefits, such as reducing the risk of cardiovascular disease and improving bone health. However, more research is needed to confirm these potential benefits.
Casein Kinase 1 (CK1) is a type of serine/threonine protein kinase that plays a crucial role in various cellular processes, including the regulation of circadian rhythms, signal transduction, and DNA damage response. CK1 phosphorylates specific serine or threonine residues on its target proteins, thereby modulating their activity, localization, or stability.
There are several isoforms of CK1, including CK1α, CK1δ, CK1ε, and CK1γ, which exhibit distinct subcellular distributions and functions. Dysregulation of CK1 has been implicated in several human diseases, such as cancer, neurodegenerative disorders, and metabolic syndromes. Therefore, understanding the molecular mechanisms underlying CK1 function is essential for developing novel therapeutic strategies to treat these conditions.
Casein Kinase 1 Delta (CK1δ) is a serine/threonine protein kinase that plays a crucial role in various cellular processes, including the regulation of circadian rhythms, DNA damage response, and Wnt signaling pathway. It phosphorylates specific target proteins on serine or threonine residues, thereby modulating their activity, stability, or localization. CK1δ is widely expressed in various tissues and has been implicated in several diseases, such as cancer, neurodegenerative disorders, and inflammatory conditions. Inhibitors of CK1δ are being investigated as potential therapeutic agents for these diseases.
Protein-Serine-Threonine Kinases (PSTKs) are a type of protein kinase that catalyzes the transfer of a phosphate group from ATP to the hydroxyl side chains of serine or threonine residues on target proteins. This phosphorylation process plays a crucial role in various cellular signaling pathways, including regulation of metabolism, gene expression, cell cycle progression, and apoptosis. PSTKs are involved in many physiological and pathological processes, and their dysregulation has been implicated in several diseases, such as cancer, diabetes, and neurodegenerative disorders.
Casein kinase 1 isoform epsilon
Casein kinase 1
Basic helix-loop-helix ARNT-like protein 1
CSNK1D
Glycogen synthase kinase-3 beta
List of MeSH codes (D08)
List of MeSH codes (D12.776.476)
List of MeSH codes (D12.644)
CSNK1E
Casein kinase 1 isoform epsilon - Wikipedia
Joerg Huelsken - People - EPFL
Molecular Cogs of the Insect Circadian Clock
Salt-inducible kinase 3 regulates the mammalian circadian clock by destabilizing PER2 protein | eLife
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Lrp6 is required for convergent extension during Xenopusgastrulation | Development | The Company of Biologists
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Comprar primobolan en argentina anabolika pulver kaufen, casein protein dm | maclake20
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Mitogen-activa1
- Insulin signaling affects multiple downstream pathways including mitogen-activated protein kinase (MAPK), which controls growth, sterol regulatory element-binding protein 1 (SREBP-1), which stimulates the synthesis of lipid and cholesterol as well as the family of Forkhead (FOXO) transcription factors regulating metabolism and autophagy [ 9 ] [ 10 ] . (encyclopedia.pub)
Epsilon4
- Casein kinase I isoform epsilon or CK1ε, is an enzyme that is encoded by the CSNK1E gene in humans. (wikipedia.org)
- The protein encoded by the casein kinase 1 epsilon gene is a serine/threonine protein kinase and a member of the casein kinase I protein family, whose members have been implicated in the control of cytoplasmic and nuclear processes, including DNA replication and repair. (wikipedia.org)
- Like other casein kinase 1 protein family members, casein kinase 1 epsilon recognizes the Ser(p)XXSer/Thr motif for phosphorylation. (wikipedia.org)
- The Casein kinase 1 epsilon protein is part of the mammalian oscillator, a group of proteins that keep cells on a roughly 24-hour schedule. (wikipedia.org)
Protein2
- Previous reports have suggested that protein kinases play important roles in the regulation of circadian clocks ( Reischl and Kramer, 2011 ). (elifesciences.org)
- The ankyrin repeat protein Diversin recruits Casein kinase Iepsilon to the beta-catenin degradation complex and acts in both canonical Wnt and Wnt/JNK signaling. (knaw.nl)
Mammalian1
- therefore, this kinase is very similar to other members of the casein kinase 1 family, of which there are seven mammalian isoforms (α, β, γ1, γ2, γ3, δ and ε). (wikipedia.org)
Protein dm2
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Regulates2
- 15. Akt/protein kinase b and glycogen synthase kinase-3beta signaling pathway regulates cell migration through the NFAT1 transcription factor. (nih.gov)
- Casein kinase iepsilon is a protein kinase that regulates the circadian clock by periodic phosphorylation of the proteins per1 and per2, controlling their. (dranandbabu.com)
Steroide1
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Anabolika5
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Phosphorylation1
- 18. Alleviating the suppression of glycogen synthase kinase-3beta by Akt leads to the phosphorylation of cAMP-response element-binding protein and its transactivation in intact cell nuclei. (nih.gov)
Proteins2
- A casein kinase I isoenzyme with specificity for proteins involved the regulation of the CIRCADIAN RHYTHM . (nih.gov)
- which includes casein and the whey proteins) which is rich in essential amino acids (7. (dranandbabu.com)
Regulation1
- 9. GSK-3beta acts upstream of Fyn kinase in regulation of nuclear export and degradation of NF-E2 related factor 2. (nih.gov)
Nuclear1
- 5. Aberrant nuclear accumulation of glycogen synthase kinase-3beta in human pancreatic cancer: association with kinase activity and tumor dedifferentiation. (nih.gov)
Family3
- therefore, this kinase is very similar to other members of the casein kinase 1 family, of which there are seven mammalian isoforms (α, β, γ1, γ2, γ3, δ and ε). (wikipedia.org)
- It was officially identified as an isoform of the casein kinase 1 family. (wikipedia.org)
- The casein kinase 1 family (ec 2. (maclake20.com)
Activity1
- This autophosphorylation occurs in the protein's C-Terminal domain, a region believed to behave as a pseudosubstrate, and inhibits kinase activity. (wikipedia.org)
Total1
- Sures total true protein and assumes that casein. (maclake20.com)