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Regulates inositol phosphate metabolism by phosphorylation of second messenger inositol 1,4,5-trisphosphate to Ins(1,3,4,5)P4.
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Thisstudy shows that overexpressed IP3-kinase 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.
Findings demonstrate that IP3K-A plays an important role in regulating affective states by modulating metabotropic receptor signaling pathways and neural activity in the amygdala.
At synapses of Inositol-1,4,5-trisphosphate 3-kinase-A deficient neurons the levels of Ins (show INS Proteins)(1,4,5)P3-5-phosphatase (inpp5a (show INPP5A Proteins)) and sarcoplasmic/endoplasmic reticulum calcium ATPase pump-2b (serca2b (show ATP2A2 Proteins)) were increased.
Inositol 1,4,5-trisphosphate 3-kinase-A is a new cell motility-promoting protein that increases the metastatic potential of tumor cells by two functional activities.
These data show that the absence of expression of the three isoenzymes of Itpk does not prevent the formation of IP5 and IP6 (show GPRIN2 Proteins), at least in mouse embryonic fibroblasts.[Itpka, Itpkb (show ITPKB Proteins), Itpkc (show ITPKC Proteins)]
Inositol 1,4,5-trisphosphate 3-kinase A is critical for spatial and temporal regulation of spine actin remodeling, synaptic plasticity, and learning and memory via an activity-dependent Rac (show AKT1 Proteins) scaffolding mechanism.
ITPKA is a potential oncogene that it is overexpressed in most tumors, and its overexpression promotes tumorigenesis; ITPKA gene body methylation regulates its expression and serves as a novel and potential biomarker for early cancer detection
Our data indicated that ITPKA expression was significantly up-regulated in hepatocellular carcinoma and could serve as a potential novel prognostic biomarker
describe the crystal structure of the complex between human Ca2+/CaM and the CaM-binding region of human IP3-3K isoform A (residues 158-183)
we conclude that the observed expression of ITPKA early in tumor development increases the metastatic potential of lung adenocarcinoma cells.
results highlight the potential role of the three isoforms of InsP3 3-kinase as direct InsP3 metabolizing enzymes and direct regulators of Ca2 (show CA2 Proteins)+ responses to extracellular signals
We report the structure of an IPK, the human Ins (show INS Proteins)(1,4,5)P3 3-kinase-A, both free and in complexes with substrates and products.
Data suggest that ITPKA may be related to carcinogenesis by the modulation of inositol polyphosphates and Ca2+ homeostasis and that ITPKA may be a potential novel molecular target and biomarker.
the morphological changes induced by IP3K-A are mediated by non-enzymatic activities of the protein.
Regulates inositol phosphate metabolism by phosphorylation of second messenger inositol 1,4,5-trisphosphate to Ins(1,3,4,5)P4. The activity of the inositol 1,4,5-trisphosphate 3-kinase is responsible for regulating the levels of a large number of inositol polyphosphates that are important in cellular signaling. Both calcium/calmodulin and protein phosphorylation mechanisms control its activity. It is also a substrate for the cyclic AMP-dependent protein kinase, calcium/calmodulin- dependent protein kinase II, and protein kinase C in vitro.
1D-myo-inositol-trisphosphate 3-kinase A
, Inositol-trisphosphate 3-kinase A
, IP3 3-kinase A
, IP3-kinase A
, IP3K A
, inositol-trisphosphate 3-kinase A
, insP 3-kinase A
, inositol 1,4,5-trisphosphate 3-kinase A
, inositol 1,4,5-triphosphate 3-kinase
, inositol 145-triphosphate 3-kinase