This enzyme also phosphorylates Ins(1,4,5)P3 to Ins(1,3,4,5)P4, Ins(1,3,4,5)P4 to Ins(1,3,4,5,6)P5, and Ins(1,3,4,5,6)P4 to Ins(PP)P4, isomer unknown. The enzyme from the plant Arabidopsis thaliana can also phosphorylate Ins(1,3,4,6)P4 and Ins(1,2,3,4,6)P5 at the D-5-position to produce 1,3,4,5,6-pentakisphosphate and inositol hexakisphosphate (InsP6), respectively . Yeast produce InsP6 from Ins(1,4,5)P3 by the actions of this enzyme and EC 2.7.1.158, inositol-pentakisphosphate 2-kinase .
This enzyme also phosphorylates Ins(1,4,5)P3 to Ins(1,3,4,5)P4, Ins(1,3,4,5)P4 to Ins(1,3,4,5,6)P5, and Ins(1,3,4,5,6)P4 to Ins(PP)P4, isomer unknown. The enzyme from the plant Arabidopsis thaliana can also phosphorylate Ins(1,3,4,6)P4 and Ins(1,2,3,4,6)P5 at the D-5-position to produce 1,3,4,5,6-pentakisphosphate and inositol hexakisphosphate (InsP6), respectively [3]. Yeast produce InsP6 from Ins(1,4,5)P3 by the actions of this enzyme and EC 2.7.1.158, inositol-pentakisphosphate 2-kinase [4].
the absence of expression of the three isoenzymes of the inositol 1,4,5-trisphosphate 3-kinase does not prevent the formation of inositol pentakisphosphate and hexakisphosphate
the absence of expression of the three isoenzymes of the inositol 1,4,5-trisphosphate 3-kinase does not prevent the formation of inositol pentakisphosphate and hexakisphosphate
the absence of expression of the three isoenzymes of the inositol 1,4,5-trisphosphate 3-kinase does not prevent the formation of inositol pentakisphosphate and hexakisphosphate
the absence of expression of the three isoenzymes of the inositol 1,4,5-trisphosphate 3-kinase does not prevent the formation of inositol pentakisphosphate and hexakisphosphate
immediate early gene induction by electroconvulsive stimulation is virtually abolished in the brains of IPMK-deleted mice, which also display deficits in spatial memory. Dominant-negative constructs, which prevent IPMK-CBP binding, substantially decrease immediate early gene induction
inositol polyphosphate multikinase is a transcriptional coactivator required for immediate early gene induction. Inositol polyphosphate multikinase acts noncatalytically as a transcriptional coactivator to mediate induction of numerous immediate early genes, IEGs. Neural activity stimulates binding of IPMK to the histone acetyltransferase CBP and enhances its recruitment to IEG promoters, but IPMK regulation of CBP recruitment and IEG induction does not require its catalytic activities. The enzyme's epigenetic regulation of immediate early genes may influence diverse nonneural and neural biologic processes
inositol polyphosphate multikinase IPMK physiologically generates phosphatidylinositol trisphosphate as well as water soluble inositol phosphates. IPMK deletion reduces growth factor-elicited Akt signaling and cell proliferation caused uniquely by loss of its phosphatidylinositol 3-kinase activity. IPMK appears to act as a molecular switch, inhibiting or stimulating Akt via its inositol phosphate kinase or inositol trisphosphate-kinase activities, respectively
inositol polyphosphate multikinase IPMK regulates glucose signaling to AMP-activated kinase in a pathway whereby glucose activates phosphorylation of IPMK at residue Tyr174 enabling the enzyme to bind to AMP-activated kinase and regulate its activation. Refeeding fasted mice rapidly and markedly stimulates transcriptional enhancement of IPMK expression while down-regulating AMP-activated kinase. AMP-activated kinase is up-regulated in mice with genetic depletion of hypothalamic IPMK. IPMK physiologically binds AMP-activated kinase, with binding enhanced by glucose treatment. Regulation by glucose of phospho-AMP-activated kinase in hypothalamic cell lines is prevented by blocking AMP-activated kinase-IPMK binding
inositol polyphosphate multikinase regulates amino acid signaling to mammalian target of rapamycin in complex with raptor, mTORC1. This regulation is independent of IPMK's catalytic function, instead reflecting its binding with mammalian target of rapamycin, mTOR, and raptor, which maintains the mTOR-raptor association. Inositol polyphosphate multikinase appears to be a physiologic mTOR cofactor, serving as a determinant of mTORC1 stability and amino acid-induced mTOR signaling
construction of mutants by disrution of gene ipk2, the resulting enzyme-deficient Ipk2 null mice die around embryonic day 9.5 with multiple morphological defects, including abnormal folding of the neural tube, overview
The absence of expression of the three isoenzymes of the inositol 1,4,5-trisphosphate 3-kinase does not prevent the formation of inositol pentakisphosphate and hexakisphosphate in mouse embryonic fibroblasts