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ATP + 1D-myo-inositol 1,4,5-trisphosphate
ADP + 1D-myo-inositol 1,3,4,5-tetrakisphosphate
ATP + 1D-myo-inositol 1,4,5-trisphosphate
ADP + 1D-myo-inositol 1,3,4,5-tetrakisphosphate
additional information
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isozyme B controls positive selection of T cells and modulates Erk activity, the enzyme is important in Ras signaling which is important for Erk activation, overview
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ATP + 1D-myo-inositol 1,4,5-trisphosphate
ADP + 1D-myo-inositol 1,3,4,5-tetrakisphosphate
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ATP + 1D-myo-inositol 1,4,5-trisphosphate
ADP + 1D-myo-inositol 1,3,4,5-tetrakisphosphate
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ATP + 1D-myo-inositol 1,4,5-trisphosphate
ADP + 1D-myo-inositol 1,3,4,5-tetrakisphosphate
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ATP + 1D-myo-inositol 1,4,5-trisphosphate
ADP + 1D-myo-inositol 1,3,4,5-tetrakisphosphate
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ATP + 1D-myo-inositol 1,4,5-trisphosphate
ADP + 1D-myo-inositol 1,3,4,5-tetrakisphosphate
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ATP + 1D-myo-inositol 1,4,5-trisphosphate
ADP + 1D-myo-inositol 1,3,4,5-tetrakisphosphate
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ATP + 1D-myo-inositol 1,4,5-trisphosphate
ADP + 1D-myo-inositol 1,3,4,5-tetrakisphosphate
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ATP + 1D-myo-inositol 1,4,5-trisphosphate
ADP + 1D-myo-inositol 1,3,4,5-tetrakisphosphate
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ATP + 1D-myo-inositol 1,4,5-trisphosphate
ADP + 1D-myo-inositol 1,3,4,5-tetrakisphosphate
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ATP + 1D-myo-inositol 1,4,5-trisphosphate
ADP + 1D-myo-inositol 1,3,4,5-tetrakisphosphate
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ATP + 1D-myo-inositol 1,4,5-trisphosphate
ADP + 1D-myo-inositol 1,3,4,5-tetrakisphosphate
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production of Ins(1,3,4,5)P4 mediated by the kinase Itpkb inhibits store-operated calcium channels and regulates B cell selection and activation
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ATP + 1D-myo-inositol 1,4,5-trisphosphate
ADP + 1D-myo-inositol 1,3,4,5-tetrakisphosphate
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enzyme phosphorylates the 3'-position of the inositol ring to convert the substrate to the product
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ATP + 1D-myo-inositol 1,4,5-trisphosphate
ADP + 1D-myo-inositol 1,3,4,5-tetrakisphosphate
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reducing the influx of calcium released from endoplasmic reticulum via IP3 receptor signaling
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Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ATP + 1D-myo-inositol 1,4,5-trisphosphate
ADP + 1D-myo-inositol 1,3,4,5-tetrakisphosphate
ATP + 1D-myo-inositol 1,4,5-trisphosphate
ADP + 1D-myo-inositol 1,3,4,5-tetrakisphosphate
additional information
?
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isozyme B controls positive selection of T cells and modulates Erk activity, the enzyme is important in Ras signaling which is important for Erk activation, overview
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?
ATP + 1D-myo-inositol 1,4,5-trisphosphate
ADP + 1D-myo-inositol 1,3,4,5-tetrakisphosphate
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ATP + 1D-myo-inositol 1,4,5-trisphosphate
ADP + 1D-myo-inositol 1,3,4,5-tetrakisphosphate
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ATP + 1D-myo-inositol 1,4,5-trisphosphate
ADP + 1D-myo-inositol 1,3,4,5-tetrakisphosphate
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ATP + 1D-myo-inositol 1,4,5-trisphosphate
ADP + 1D-myo-inositol 1,3,4,5-tetrakisphosphate
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ATP + 1D-myo-inositol 1,4,5-trisphosphate
ADP + 1D-myo-inositol 1,3,4,5-tetrakisphosphate
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ATP + 1D-myo-inositol 1,4,5-trisphosphate
ADP + 1D-myo-inositol 1,3,4,5-tetrakisphosphate
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ATP + 1D-myo-inositol 1,4,5-trisphosphate
ADP + 1D-myo-inositol 1,3,4,5-tetrakisphosphate
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ATP + 1D-myo-inositol 1,4,5-trisphosphate
ADP + 1D-myo-inositol 1,3,4,5-tetrakisphosphate
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ATP + 1D-myo-inositol 1,4,5-trisphosphate
ADP + 1D-myo-inositol 1,3,4,5-tetrakisphosphate
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ATP + 1D-myo-inositol 1,4,5-trisphosphate
ADP + 1D-myo-inositol 1,3,4,5-tetrakisphosphate
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ATP + 1D-myo-inositol 1,4,5-trisphosphate
ADP + 1D-myo-inositol 1,3,4,5-tetrakisphosphate
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production of Ins(1,3,4,5)P4 mediated by the kinase Itpkb inhibits store-operated calcium channels and regulates B cell selection and activation
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ATP + 1D-myo-inositol 1,4,5-trisphosphate
ADP + 1D-myo-inositol 1,3,4,5-tetrakisphosphate
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enzyme phosphorylates the 3'-position of the inositol ring to convert the substrate to the product
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ATP + 1D-myo-inositol 1,4,5-trisphosphate
ADP + 1D-myo-inositol 1,3,4,5-tetrakisphosphate
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reducing the influx of calcium released from endoplasmic reticulum via IP3 receptor signaling
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Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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IP3K-A expression is highly enriched in the central nucleus of the amygdala (CeA), which plays a pivotal role in the processing and expression of emotional phenotypes in mammals. P3K-A is primarily expressed in neurons rather than glia in the amygdala. In the CeA, IP3K-A primarily colocalizes with GAD67-positive GABAergic interneurons, whereas most IP3K-A in the BLA is in CAMKIIalpha-positive excitatory pyramidal neurons
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brain
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low expression level
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tracheal and bronchial, multiciliated tracheal epithelial cells
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inositol trisphosphate 3-kinase B gene is expressed in all hematopoietic stem/progenitor cell populations
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MTEC
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Itpka is particularly active in neurons of the hippocampus and cerebellum
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ITPKA is mainly expressed in pyramidal cells of the hippocampal CA1 region and granule cells of the dentate gyrus
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enzyme expression is highly enriched in the central nucleus of the amygdala
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isozyme inositol-1,4,5-trisphosphate-3-kinase-A is a neuron-specific, actin bundling protein concentrated at dendritic spines
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isozyme IP3K-A is enriched in dendritic spines of mature neurons
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localized to the post-dendritic spines of neurons. Itpka is particularly active in neurons of the hippocampus and cerebellum
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in mature neurons, ITPKA accumulates at postsynaptic densities (PSDs), where the protein is bound to F-actin
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in the CeA, IP3K-A primarily colocalizes with GAD67-positive GABAergic interneurons, whereas most IP3K-A in the BLA is in CAMKIIalpha-positive excitatory pyramidal neurons
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higher expression of isozyme IP3-3KB
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high expression level
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higher expression of isozyme IP3-3KB
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epididymal spermatozoa
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high expression level
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higher expression of isozyme IP3-3KB
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low expression level
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additional information
enzyme activity determined in cell homogenates with Ins(1,4,5)P3 and ATP as substrate is generally very low compared to Ins(1,4,5)P3 5-phosphatase, EC 3.1.3.56, except in a few tissues such as brain, testis, thymus or intestine
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additional information
enzyme activity determined in cell homogenates with Ins(1,4,5)P3 and ATP as substrate is generally very low compared to Ins(1,4,5)P3 5-phosphatase, EC 3.1.3.56, except in a few tissues such as brain, testis, thymus or intestine
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additional information
enzyme activity determined in cell homogenates with Ins(1,4,5)P3 and ATP as substrate is generally very low compared to Ins(1,4,5)P3 5-phosphatase, EC 3.1.3.56, except in a few tissues such as brain, testis, thymus or intestine
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additional information
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enzyme activity determined in cell homogenates with Ins(1,4,5)P3 and ATP as substrate is generally very low compared to Ins(1,4,5)P3 5-phosphatase, EC 3.1.3.56, except in a few tissues such as brain, testis, thymus or intestine
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additional information
isozyme ITPKA is mainly expressed in neurons of the central nervous system and is also overexpressed in tumor cells
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additional information
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tissue-dependent expression of isozyme IP3-3KB
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additional information
enzyme activity determined in cell homogenates with Ins(1,4,5)P3 and ATP as substrate is generally very low compared to Ins(1,4,5)P3 5-phosphatase, EC 3.1.3.56, except in a few tissues such as brain, testis, thymus or intestine. Itpkb and Itpkc are widespread expressed in many different tissues and cell lines
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additional information
enzyme activity determined in cell homogenates with Ins(1,4,5)P3 and ATP as substrate is generally very low compared to Ins(1,4,5)P3 5-phosphatase, EC 3.1.3.56, except in a few tissues such as brain, testis, thymus or intestine. Itpkb and Itpkc are widespread expressed in many different tissues and cell lines
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additional information
enzyme activity determined in cell homogenates with Ins(1,4,5)P3 and ATP as substrate is generally very low compared to Ins(1,4,5)P3 5-phosphatase, EC 3.1.3.56, except in a few tissues such as brain, testis, thymus or intestine. Itpkb and Itpkc are widespread expressed in many different tissues and cell lines
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additional information
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enzyme activity determined in cell homogenates with Ins(1,4,5)P3 and ATP as substrate is generally very low compared to Ins(1,4,5)P3 5-phosphatase, EC 3.1.3.56, except in a few tissues such as brain, testis, thymus or intestine. Itpkb and Itpkc are widespread expressed in many different tissues and cell lines
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additional information
enzyme tissue expression analysis by immunohistochemic analysis and situ hybridization. Cells positive for ITPKC express either a multicilium (tracheal and bronchial epithelia, brain ependymal cells), microvilli forming a brush border (small and large intestine, and kidney proximal tubule cells) or a flagellum (spermatozoa)
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additional information
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enzyme tissue expression analysis by immunohistochemic analysis and situ hybridization. Cells positive for ITPKC express either a multicilium (tracheal and bronchial epithelia, brain ependymal cells), microvilli forming a brush border (small and large intestine, and kidney proximal tubule cells) or a flagellum (spermatozoa)
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additional information
ubiquitous tissue expression of isozyme Itpkb, the Itpkb protein contributes mainly to the majority of the Ins(1,4,5)P3 3-kinase activity in resting T and B lymphocytes as well as in neutrophils and mast cells
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additional information
cells positive for ITPKC in the studied tissues express either a multicilium (tracheal and bronchial epithelia, brain ependymal cells), microvilli forming a brush border (small and large intestine, and kidney proximal tubule cells) or a flagellum (spermatozoa), suggesting a role for ITPKC either in the development or the function of these specialized cellular structures. Tissue expression and localization study, overview
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additional information
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cells positive for ITPKC in the studied tissues express either a multicilium (tracheal and bronchial epithelia, brain ependymal cells), microvilli forming a brush border (small and large intestine, and kidney proximal tubule cells) or a flagellum (spermatozoa), suggesting a role for ITPKC either in the development or the function of these specialized cellular structures. Tissue expression and localization study, overview
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evolution
inositol(1,4,5)trisphosphate 3-kinases (Itpks) occur in three isoenzyme forms, Itpka/b and c, in human, rat and mouse. They share a catalytic domain relatively well conserved at the C-terminal end and a quite isoenzyme specific regulatory domain at the N-terminal end of the protein
metabolism
1D-myo-inositol 1,3,4,5-tetrakisphosphate, Ins(1,3,4,5)P4 can interact with a relatively specific Ins(1,3,4,5)P4 binding protein Rasa3, alternatively, Ins(1,3,4,5)P4 can also compete with phosphoinositides to the binding of PH domain containing proteins such as Akt, protein kinase B. In neutrophils and hematopoietic progenitors, elevated levels of Ins(1,3,4,5)P4 inhibit the recruitment of Akt at the plasma membrane, and its activation, acting as a competitor of PtdIns(3,4,5)P3 binding to its PH domain
malfunction
genetic abrogation of IP3K-A alters amygdala gene expression, particularly in genes involved in key intracellular signaling pathways and genes mediating fear- and anxiety-related behaviors. In agreement with the changes in amygdala gene expression profiles, IP3K-A knockout mice display more robust responses to aversive stimuli and spend less time in the open arms of the elevated plus maze, indicating high levels of innate fear and anxiety. IP3K-A KO mice show decreased excitatory and inhibitory postsynaptic current and reduced c-Fos immunoreactivity in the central nucleus of the amygdala. Overexpression of inositol 1,4,5-trisphosphate 3-kinases isozymes consistently suppresses inositol 1,4,5-trisphosphate-evoked increases in intracellular calcium in response to an agonist, whereas deletion or inactivation of different genes elicits diverse phenotypes depending on cell type. Genetic deletion of IP3K-A produces deficits in long-term potentiation in the dentate gyrus and impairs memory performance. Deletion does not affect spatial learning in the Morris water maze. Phenotypes, overview
malfunction
isozyme Itpka-deficient mice exhibit increased LTP in the CA1 region of the hippocampus
malfunction
ITPKA depletion in mice increases the number of hippocampal spine-synapses while reducing average spine length, depletion of ITPKA reduces the length of dendritic spines of hippocampal pyramidal cells
malfunction
genetic abrogation of IP3K-A alters amygdala gene expression, particularly in genes involved in key intracellular signaling pathways and genes mediating fear- and anxiety-related behaviors. In agreement with the changes in amygdala gene expression profiles, IP3K-A knockout (KO) mice display more robust responses to aversive stimuli and spent less time in the open arms of the elevated plus maze, indicating high levels of innate fear and anxiety. Decreased excitatory and inhibitory postsynaptic current and reduced c-Fos immunoreactivity are found in the CeA of IP3K-A KO mice
malfunction
IP3K-A knockout mice exhibit deficits in some forms of hippocampus-dependent learning and synaptic plasticity, such as long-term potentiation in the dentate gyrus synapses of the hippocampus. Enzyme overexpressing mutant Tg mice show an increase in both presynaptic release probability of evoked responses, along with bigger synaptic vesicle pools, and miniature excitatory postsynaptic current amplitude, although the spine density or the expression levels of the postsynaptic density-related proteins NR2B, synaptotagmin 1, and PSD-95 are not affected. Hippocampal-dependent learning and memory tasks, including novel object recognition and radial arm maze tasks, are partially impaired in Tg mice. (R,S)-3,5-dihydroxyphenylglycine-induced metabotropic glutamate receptor long-term depression is inhibited in Tg mice and this inhibition is dependent on protein kinase C but not on the IP3 receptor. Long-term potentiation and depression dependent on N-methyl-D-aspartate receptor are marginally affected in Tg mice. The CA1 synapse of Tg mouse have greater evoked synaptic transmission efficacy in mutant mice compared too wild-type
malfunction
ITPKA depletion in mice results in altered synaptic plasticity and thus in impaired learning and memory. Stable knockdown of ITPKA in high expressing tumor cells results in decreased cell growth, colony formation and suppression of xenograft growth in immunosuppressed mice. Stable knockdown of ITPKA suppresses xenograft growth in immunosuppressed mice
malfunction
Itpka-deficient mice exhibit a weak metabolic phenotype, in keeping with functional studies revealing no clear role of ITPKA in metabolic organs. Broad phenotypic screening of itpka-deficient mice, Effects of itpka deficiency on brain function, overview. Among the neurobehavioral tests analyzed, itpka-deficient mice reacted faster to a hot plate, prepulse inhibition is impaired and the accelerating rotarod test shows decreased latency of itpka deficient mice to fall. Analysis of extracerebral functions in control and itpka deficient mice reveals significantly reduced glucose, lactate, and triglyceride plasma concentrations in itpka-deficient mice. Itpka deficiency affects energy metabolism, phenotype. Reduced glucose level is measured in plasma of itpka-deficient mice
metabolism
1D-myo-inositol 1,3,4,5-tetrakisphosphate, Ins(1,3,4,5)P4 can interact with a relatively specific Ins(1,3,4,5)P4 binding protein Rasa3, alternatively, Ins(1,3,4,5)P4 can also compete with phosphoinositides to the binding of PH domain containing proteins such as Akt, protein kinase B. In neutrophils and hematopoietic progenitors, elevated levels of Ins(1,3,4,5)P4 inhibit the recruitment of Akt at the plasma membrane, and its activation, acting as a competitor of PtdIns(3,4,5)P3 binding to its PH domain
metabolism
isozyme IP3K-A expression is highly enriched in the central nucleus of the amygdala, which plays a pivotal role in the processing and expression of emotional phenotypes in mammals
physiological function
in addition to cross-linking actin filaments, ITPKA strongly inhibits Arp2/3-complex induced actin filament branching by displacing the complex from F-actin. n vivo ITPKA negatively regulates formation and/or maintenance of synaptic contacts in the mammalian brain. On the molecular level this effect appears to result from the ITPKA-mediated inhibition of Arp2/3-complex F-actin branching activity. ITPKA does not affect the F-actin bundling activity of drebrin A
physiological function
isozyme IP3K-A has a profound influence on the basal activities of fear- and anxiety-mediating amygdala circuitry and plays an important role in regulating affective states by modulating metabotropic receptor signaling pathways and neural activity in the amygdala. Inositol 1,4,5-trisphosphate 3-kinases modulate intracellular calcium signaling induced by the activation of G-protein coupled receptors associated with phospholipase C. Isozyme IP3K-A is enriched in dendritic spines of mature neurons and modulates actin dynamics in the hippocampus
physiological function
isozyme Itpka contains an F-actin binding site at the N-terminal part that confers to Itpka the properties of an F-actin bundling protein with two major consequences: it can reorganize the cytoskeletal network, particularly in dendritic spines, and it can provide an opportunity for Ins(1,3,4,5)P4 to act very locally as second messenger. Isozyme Itpka is an F-actin bundling protein regulating dendritic spines structural plasticity and a scaffold protein for synaptic rac signaling, Itpka overexpression induces cytoskeletal reorganization, high expression of Itpka in cancer cells increases invasion and migration in vitro
physiological function
among the ITPK-isoforms ITPKA is the most specialized one. In cells it is exclusively bound to F-actin resulting in cross-linking of actin filaments. ITPKA has two very distinct functions, regulating both, calcium signaling and actin dynamics. Isoform A of ITPK is an oncogene, it is involved in cancer progression, tumor growth is stimulated by the InsP3Kinase activity of ITPKA and metastasis by its actin bundling activity. ITPKA regulates actin dynamics by binding with its homodimeric N-terminal actin binding domain (ABD) to F-actin
physiological function
inositol 1,4,5-trisphosphate 3-kinase A (IP3K-A) is enriched in the brain and neurons that regulates intracellular calcium levels via signaling through the inositol trisphosphate receptor. IP3K-A expression is highly enriched in the central nucleus of the amygdala (CeA), which plays a pivotal role in the processing and expression of emotional phenotypes in mammals. IP3K-A has a profound influence on the basal activities of fear- and anxiety-mediating amygdala circuitry. IP3K-A plays an important role in regulating affective states by modulating metabotropic receptor signaling pathways and neural activity in the amygdala
physiological function
inositol 1,4,5-trisphosphate 3-kinase A (IP3K-A) regulates the level of the inositol polyphosphates, inositol trisphosphate (IP3) and inositol tetrakisphosphate to modulate cellular signaling and intracellular calcium homeostasis in the central nervous system. IP3K-A binds to F-actin in an activity-dependent manner and accumulates in dendritic spines, where it is involved in the regulation of synaptic plasticity. Overexpressed IP3K-A plays a role in some forms of hippocampus-dependent learning and memory tasks as well as in synaptic transmission and plasticity by regulating both presynaptic and postsynaptic functions
physiological function
isozyme ITPKA is involved in the regulation of nociceptive pathways, sensorimotor gating, and motor learning. Inositol-1,4,5-trisphosphate 3-kinase-A (ITPKA) is the neuronal isoform of ITPKs and exhibits both actin bundling and InsP3 kinase activity. In addition to neurons, ITPKA is ectopically expressed in tumor cells, where its oncogenic activity increases tumor cell malignancy. ITPKA is involved in the regulation of nociceptive pathways, sensorimotor gating and motor learning. ITPKA plays a functional role in calcium signaling of CaCo-2 cells
evolution
a member of the inositol 1,4,5-trisphosphate 3-kinases family
evolution
inositol(1,4,5)trisphosphate 3-kinases (Itpks) occur in three isoenzyme forms, Itpka/b and c, in human, rat and mouse. They share a catalytic domain relatively well conserved at the C-terminal end and a quite isoenzyme specific regulatory domain at the N-terminal end of the protein
evolution
inositol 1,4,5-trisphosphate 3-kinase C (ITPKC) is the last identified member of the inositol 1,4,5-trisphosphate 3-kinases family which phosphorylates inositol 1,4,5-trisphosphate into inositol 1,3,4,5-tetrakisphosphate
malfunction
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disruption of InsP3KB leads to impaired T cell and B cell development as well as hyperactivation of neutrophils, in InsP3KB null mice, the bone marrow granulocyte monocyte progenitor (GMP) population is expanded, and GMP cells proliferated significantly faster, neutrophil production in the bone marrow is enhanced, and the peripheral blood neutrophil count is also substantially elevated, neutrophil apoptotic death is enhanced in enzyme knock-out mice, disruption of enzyme promotes myeloid differentiation
malfunction
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enzyme knock-out mice show deficits of synaptic plasticity in perforant path and in hippocampal-dependent memory performances
malfunction
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In transgenic mice that also express soluble hen egg lysozyme, lack of inositol 1,4,5-trisphosphate 3-kinase B converts anergy induction to deletion, mice lacking inositol 1,4,5-trisphosphate 3-kinase B have normal B cell development in the bone marrow, but reduced numbers of all splenic B cell subsets and a shift in the developmental fate toward compartments that are normally selected by strong B cell receptor signals, mature B cells lacking the enzyme fail to proliferate in response to B cell receptor stimulation but show normal responses to the TLR4 ligand LPS or agonistic Abs to CD40. At the immature stage, inositol 1,4,5-trisphosphate 3-kinase B-deficient mice possess a 60% increase in the numbers of immature B cells compared with wild type mice. Examination of splenic B cell populations in inositol 1,4,5-trisphosphate 3-kinase B-deficient/IgHEL tg mice reveals that while the total numbers of B220+ cells are relatively normal, the numbers of follicular mature B cells are increased 2.2fold, while the number of T2 and marginal zone cells are reduced 3- and 3.8fold
malfunction
mice deficient for Itpkb have a severe defect in thymocytes differentiation and thus lack peripheral T cells
malfunction
mice genetically-deficient for the B isoform of the inositol 1,4,5-trisphosphate 3-kinase have a severe defect in thymocytes differentiation and thus lack peripheral T cells. Mutant T cells show an increased activated/memory phenotype as well as a decreased proliferative capacity and survival, Itpkb-deficient peripheral T cells have also an increased capacity to secrete cytokines upon stimulation
physiological function
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inositol 1,4,5-trisphosphate 3-kinase B converts inositol 1,4,5-trisphosphate to inositol 1,3,4,5-tetrakisphosphate upon Ag receptor activation and controls the fate and function of lymphocytes
physiological function
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on neural activation, inositol 1,4,5-trisphosphate 3-kinase A binds directly to activated Rac1 and recruits it to the actin cytoskeleton in the postsynaptic area, enzyme is critical for the spatial and temporal regulation of spine actin remodeling, synaptic plasticity, and learning and memory via an activity-dependent Rac scaffolding mechanism, inositol 1,4,5-trisphosphate 3-kinase A catalytic activity regulates calcium levels by modulating the metabolism of 1D-myo-inositol 1,4,5-trisphosphate
physiological function
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physiological modulator of myelopoiesis, enzyme plays a crucial role in hematopoiesis
physiological function
isoform inositol 1,4,5-trisphosphate 3-kinase B is important for the control of Bim protein expression and B cell survival rather than for the control of B cell development from one stage to another. B cell receptor transgenic inositol 1,4,5-trisphosphate 3-kinase B-/- B cells exhibit an anergic phenotype with the notable exception of their enhanced antigen-induced calcium signalling. On a deleting H2-Kb genetic background, inositol 1,4,5-trisphosphate 3-kinase B is not essential for B cell receptor editing or negative selection
physiological function
functional role of isozyme Itpkb in peripheral T cells, potential role for Itpkb in autoimmunity
physiological function
in natural killer (NK) cells, isozyme Itpkb promotes NK-cell terminal maturation but limits NK-cell effector functions. Itpkb controls hematopoietic stem cell homeostasis and prevents lethal hematopoietic failure in mice
physiological function
role for ITPKC either in the development or the function of these specialized cellular structures
physiological function
cells positive for ITPKC in the studied tissues express either a multicilium (tracheal and bronchial epithelia, brain ependymal cells), microvilli forming a brush border (small and large intestine, and kidney proximal tubule cells) or a flagellum (spermatozoa), suggesting a role for ITPKC either in the development or the function of these specialized cellular structures
additional information
isozyme Itpkb contains an F-actin binding site at the N-terminal part
additional information
isozyme Itpkb contains an F-actin binding site at the N-terminal part
additional information
isozyme Itpkb contains an F-actin binding site at the N-terminal part
additional information
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isozyme Itpkb contains an F-actin binding site at the N-terminal part
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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125000
-
x * 53000, recombinant isozyme IP3-3KA, SDS-PAGE, x * 98000, recombinant isozyme IP3-3KC, SDS-PAGE, x * 125000, recombinant isozyme IP3-3KB, SDS-PAGE, x * 48000, native brain isozyme IP3-3KA, SDS-PAGE, x * 110000-120000, native isozyme IP3-3KB, tissue-dependent, SDS-PAGE
48000
-
x * 53000, recombinant isozyme IP3-3KA, SDS-PAGE, x * 98000, recombinant isozyme IP3-3KC, SDS-PAGE, x * 125000, recombinant isozyme IP3-3KB, SDS-PAGE, x * 48000, native brain isozyme IP3-3KA, SDS-PAGE, x * 110000-120000, native isozyme IP3-3KB, tissue-dependent, SDS-PAGE
53000
-
x * 53000, recombinant isozyme IP3-3KA, SDS-PAGE, x * 98000, recombinant isozyme IP3-3KC, SDS-PAGE, x * 125000, recombinant isozyme IP3-3KB, SDS-PAGE, x * 48000, native brain isozyme IP3-3KA, SDS-PAGE, x * 110000-120000, native isozyme IP3-3KB, tissue-dependent, SDS-PAGE
90000
x * 90000, about, SDS-PAGE
98000
-
x * 53000, recombinant isozyme IP3-3KA, SDS-PAGE, x * 98000, recombinant isozyme IP3-3KC, SDS-PAGE, x * 125000, recombinant isozyme IP3-3KB, SDS-PAGE, x * 48000, native brain isozyme IP3-3KA, SDS-PAGE, x * 110000-120000, native isozyme IP3-3KB, tissue-dependent, SDS-PAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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Hascakova-Bartova, R.; Pouillon, V.; Dewaste, V.; Moreau, C.; Jacques, C.; Banting, G.; Schurmans, S.; Erneux, C.
Identification and subcellular distribution of endogenous Ins(1,4,5)P(3) 3-kinase B in mouse tissues
Biochem. Biophys. Res. Commun.
323
920-925
2004
Mus musculus
brenda
Wen, B.G.; Pletcher, M.T.; Warashina, M.; Choe, S.H.; Ziaee, N.; Wiltshire, T.; Sauer, K.; Cooke, M.P.
Inositol (1,4,5) trisphosphate 3 kinase B controls positive selection of T cells and modulates Erk activity
Proc. Natl. Acad. Sci. USA
101
5604-5609
2004
Mus musculus, Mus musculus C57BL/6
brenda
Miller, A.T.; Sandberg, M.; Huang, Y.H.; Young, M.; Sutton, S.; Sauer, K.; Cooke, M.P.
Production of Ins(1,3,4,5)P4 mediated by the kinase Itpkb inhibits store-operated calcium channels and regulates B cell selection and activation [Erratum to document cited in CA146:460525]
Nat. Immunol.
8
780
2007
Mus musculus
-
brenda
Miller, A.T.; Beisner, D.R.; Liu, D.; Cooke, M.P.
Inositol 1,4,5-trisphosphate 3-kinase B is a negative regulator of BCR signaling that controls B cell selection and tolerance induction
J. Immunol.
182
4696-4704
2009
Mus musculus
brenda
Kim, I.H.; Park, S.K.; Hong, S.T.; Jo, Y.S.; Kim, E.J.; Park, E.H.; Han, S.B.; Shin, H.S.; Sun, W.; Kim, H.T.; Soderling, S.H.; Kim, H.
Inositol 1,4,5-trisphosphate 3-kinase a functions as a scaffold for synaptic Rac signaling
J. Neurosci.
29
14039-14049
2009
Mus musculus, Rattus norvegicus (P17105)
brenda
Jia, Y.; Loison, F.; Hattori, H.; Li, Y.; Erneux, C.; Park, S.Y.; Gao, C.; Chai, L.; Silberstein, L.E.; Schurmans, S.; Luo, H.R.
Inositol trisphosphate 3-kinase B (InsP3KB) as a physiological modulator of myelopoiesis
Proc. Natl. Acad. Sci. USA
105
4739-4744
2008
Mus musculus
brenda
Marechal, Y.; Queant, S.; Polizzi, S.; Pouillon, V.; Schurmans, S.
Inositol 1,4,5-trisphosphate 3-kinase B controls survival and prevents anergy in B cells
Immunobiology
216
103-109
2010
Mus musculus (B2RXC2), Mus musculus
brenda
Pouillon, V.; Maréchal, Y.; Frippiat, C.; Erneux, C.; Schurmans, S.
Inositol 1,4,5-trisphosphate 3-kinase B (Itpkb) controls survival, proliferation and cytokine production in mouse peripheral T cells
Adv. Biol. Regul.
53
39-50
2013
Mus musculus (B2RXC2)
-
brenda
Erneux, C.; Ghosh, S.; Koenig, S.
Inositol(1,4,5)P3 3-kinase isoenzymes: catalytic properties and importance of targeting to F-actin to understand function
Adv. Biol. Regul.
60
135-143
2016
Homo sapiens (P23677), Homo sapiens (P27987), Homo sapiens (Q96DU7), Homo sapiens, Mus musculus (B2RXC2), Mus musculus (Q7TS72), Mus musculus (Q8R071), Mus musculus, Rattus norvegicus (P17105), Rattus norvegicus (P42335), Rattus norvegicus (Q80ZG2)
brenda
Scoumanne, A.; Molina-Ortiz, P.; Monteyne, D.; Perez-Morga, D.; Erneux, C.; Schurmans, S.
Specific expression and function of inositol 1,4,5-trisphosphate 3-kinase C (ITPKC) in wild type and knock-out mice
Adv. Biol. Regul.
62
1-10
2016
Mus musculus (Q7TS72), Mus musculus
brenda
Stygelbout, V.; Leroy, K.; Pouillon, V.; Ando, K.; DAmico, E.; Jia, Y.; Luo, H.R.; Duyckaerts, C.; Erneux, C.; Schurmans, S.; Brion, J.P.
Inositol trisphosphate 3-kinase B is increased in human Alzheimer brain and exacerbates mouse Alzheimer pathology
Brain
137
537-552
2014
Homo sapiens (P27987), Homo sapiens, Mus musculus (B2RXC2), Mus musculus
brenda
Koester, J.D.; Leggewie, B.; Blechner, C.; Brandt, N.; Fester, L.; Rune, G.; Schweizer, M.; Kindler, S.; Windhorst, S.
Inositol-1,4,5-trisphosphate-3-kinase-A controls morphology of hippocampal dendritic spines
Cell. Signal.
28
83-90
2016
Mus musculus (Q8R071), Mus musculus C57BL/6 (Q8R071)
brenda
Chung, S.; Kim, I.H.; Lee, D.; Park, K.; Kim, J.Y.; Lee, Y.K.; Kim, E.J.; Lee, H.W.; Choi, J.S.; Son, G.H.; Sun, W.; Shin, K.S.; Kim, H.
The role of inositol 1,4,5-trisphosphate 3-kinase A in regulating emotional behavior and amygdala function
Sci. Rep.
6
23757
2016
Mus musculus (Q8R071), Mus musculus C57BL/6N (Q8R071)
brenda
Scoumanne, A.; Molina-Ortiz, P.; Monteyne, D.; Perez-Morga, D.; Erneux, C.; Schurmans, S.
Specific expression and function of inositol 1,4,5-trisphosphate 3-kinase C (ITPKC) in wild type and knock-out mice
Adv. Biol. Regul.
62
1-10
2016
Mus musculus (Q7TS72), Mus musculus
brenda
Windhorst, S.; Song, K.; Gazdar, A.F.
Inositol-1,4,5-trisphosphate 3-kinase-A (ITPKA) is frequently over-expressed and functions as an oncogene in several tumor types
Biochem. Pharmacol.
137
1-9
2017
Homo sapiens (P23677), Homo sapiens, Mus musculus (Q8R071)
brenda
Blechner, C.; Becker, L.; Fuchs, H.; Rathkolb, B.; Prehn, C.; Adler, T.; Calzada-Wack, J.; Garrett, L.; Gailus-Durner, V.; Morellini, F.; Conrad, S.; Hoelter, S.M.; Wolf, E.; Klopstock, T.; Adamski, J.; Busch, D.; de Angelis, M.H.; Schmeisser, M.J.; Windhorst, S.
Physiological relevance of the neuronal isoform of inositol-1,4,5-trisphosphate 3-kinases in mice
Neurosci. Lett.
735
135206
2020
Mus musculus (Q8R071)
brenda
Choi, B.; Lee, H.W.; Mo, S.; Kim, J.Y.; Kim, H.W.; Rhyu, I.J.; Hong, E.; Lee, Y.K.; Choi, J.S.; Kim, C.H.; Kim, H.
Inositol 1,4,5-trisphosphate 3-kinase A overexpressed in mouse forebrain modulates synaptic transmission and mGluR-LTD of CA1 pyramidal neurons
PLoS ONE
13
e0193859
2018
Mus musculus (Q8R071), Mus musculus
brenda
Chung, S.; Kim, I.H.; Lee, D.; Park, K.; Kim, J.Y.; Lee, Y.K.; Kim, E.J.; Lee, H.W.; Choi, J.S.; Son, G.H.; Sun, W.; Shin, K.S.; Kim, H.
The role of inositol 1,4,5-trisphosphate 3-kinase A in regulating emotional behavior and amygdala function
Sci. Rep.
6
23757
2016
Mus musculus (Q8R071), Mus musculus C57BL/6N (Q8R071)
brenda