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Data suggest that IPMK exhibits constrained, horseshoe-shaped substrate pocket, formed from an alpha-helix, a 3(10) helix, and a recently evolved tri-proline loop; headgroups of substrates (inositol 4,5-bisphosphate and inositol 1,4,5-trisphosphate) bind in precisely the same orientation, indicative of evolutionary optimization of 3-kinase activities against both substrates.
IPMK is a versatile regulator of nuclear signaling events. (Review)
No IPMK mutation was found in constitutional or tumor DNA in patients with familial small-intestine neuroendocrine carcinoids. CGH array revealed recurrent chromosome-18 deletions but no alteration in the IPMK region.
This study demonstrated that identified genetic overlap between Alzheimer Disease disease and immune-mediated diseases, implicating the HLA locus and IPMK in the pathobiology of Alzheimer Disease.
a severe loss of IPMK in the striatum of Huntington disease patients and in several cellular and animal models of the disease, is reported.
A hereditary form of small intestinal carcinoid associated with a germline mutation in IPMK.
Future research should focus on the hitherto unknown non-conventional import of IPMK and the potential impact of its dysregulation on IPMK signaling pathways regulating cellular growth and proliferation.
Knockdown of expression and/or inhibition of function of phospholipase Cgamma1, inositol polyphosphate multikinase, which generates inositol 1,3,4,5-tetrakisphosphate (InsP) and InsP, and inositol hexakisphosphate kinase 1/2
Our findings implicate IPMK in a transcript-selective mRNA export pathway controlled by phosphoinositide turnover that preserves genome integrity in humans.
Results suggest that inositol polyphosphate multikinase (IPMK) acts as a transcriptional coactivator for p53 and that it is an integral part of the p53 transcriptional complex facilitating cell death.
overview of possible roles of IPMK in regulation of metabolism: IPMK appears to mediate activation of mammalian target of rapamycin (mTOR) in response to essential amino acids. IPMK appears to mediate hypothalamic control of food intake. [REVIEW]
Data show that inositol polyphosphate multikinase (IPMK) interacts with the nuclear receptor steroidogenic factor 1 (SF-1) and phosphorylates its bound ligand Phosphatidylinositol 4,5-bisphosphate (PIP).
Phosphorylation of S284 by protein kinase CK2 significantly decreases nuclear targeting of IPMK in HEK-293 cells.
cloning of a full-length 1248-bp cDNA encoding a human inositol phosphate multikinase (IPMK); localized predominantly in the nucleus when transiently expressed in mammalian cells
the major activity of human InsP(4) 5-kinase is phosphorylation at the D-5 position [InsP(4) 5-kinase]
IP5 promotes HIF-1alpha prolyl hydroxylation and pVHL-dependent degradation of HIF-1alpha. IPMK deletion in mouse brain increases HIF-1alpha/VEGF levels and vascularization. This disrupts blood-brain barrier and enhances brain blood vessel permeability. IPMK, via its product IP5, negatively regulates angiogenesis by inhibiting VEGF expression. IP5 acts by enhancing HIF-1alpha hydroxylation and thus pVHL-dependent degra...
these findings identify IPMK as a key determinant of TRAF6 stability and elucidate the physiological function of IPMK in TLR-induced innate immunity.
Data show that phospholipase C (PLC)-beta1 (PLC-beta1) overexpression determines an increase in beta-catenin translocation and that PLC-beta1, inositol polyphosphate multikinase (IPMK) and beta-catenin are mediators of the same signaling pathway.
metformin-mediated activation of AMP-Activated Protein Kinases was impaired in the absence of IPMK.
Inositol polyphosphate multikinase is a coactivator for serum response factor-dependent induction of immediate early genes.
Inositol polyphosphate multikinase is a transcriptional coactivator required for immediate early gene induction.
IPMK regulates glucose signaling to AMPK in a pathway whereby glucose activates phosphorylation of IPMK at tyrosine 174 enabling the enzyme to bind to AMPK and regulate its activation.
Data show that in MEFs lacking IPMK, synthesis of IP5 and IP7 is abolished, but IP6 formation is reduced about 90%.
Inositol polyphosphate multikinase (Ipk2) plays a major role in the synthesis of inositol polyphosphate messengers derived from inositol 1,4,5-trisphosphate in embryogenesis and normal development.
Taken together, the findings suggest that AtIPK2beta negatively regulates flowering time by blocking chromatin silencing of FLC.
AtIPK2beta and IP6 are involved in glucose suppression of seed germination and that AtIPK2beta enzyme activity is likely to be regulated by SnRK1.1.
This study discovered that a key Abscisic acid (ABA) signaling component calcium-dependent protein kinase 4 (CPK4) can interact with AtIpk2 beta under ABA treated conditions through affinity purification and mass spectrometry detection.
AtIPK2alpha and AtIPK2beta are involved in pollen development, pollen tube guidance and embryogenesis.
for AtIpk2beta in axillary shoot branching through the auxin signaling pathway
This gene encodes a member of the inositol phosphokinase family. The encoded protein has 3-kinase, 5-kinase and 6-kinase activities on phosphorylated inositol substrates. The encoded protein plays an important role in the biosynthesis of inositol 1,3,4,5,6-pentakisphosphate, and has a preferred 5-kinase activity. This gene may play a role in nuclear mRNA export. Pseudogenes of this gene are located on the long arm of chromosome 13 and the short arm of chromosome 19.
inositol 1,3,4,6-tetrakisphosphate 5-kinase
, inositol polyphosphate multikinase
, inositol polyphosphate kinase 2
, LOW QUALITY PROTEIN: inositol polyphosphate multikinase
, Inositol polyphosphate 6-/3-/5-kinase beta