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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 (show VANGL2 Proteins)-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 (show HTT Proteins) 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 (show IP6K1 Proteins)/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 (show TP53 Proteins) and that it is an integral part of the p53 (show TP53 Proteins) transcriptional complex facilitating cell death.
metformin-mediated activation of AMP (show TMPRSS5 Proteins)-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 (show JUN Proteins) genes.
Inositol polyphosphate multikinase is a transcriptional coactivator required for immediate early (show JUN Proteins) gene induction.
IPMK regulates glucose signaling to AMPK (show PRKAA1 Proteins) in a pathway whereby glucose activates phosphorylation of IPMK at tyrosine 174 enabling the enzyme to bind to AMPK (show PRKAA1 Proteins) and regulate its activation.
Data show that in MEFs lacking IPMK, synthesis of IP5 and IP7 is abolished, but IP6 (show GPRIN2 Proteins) 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.
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 polyphosphate multikinase
, inositol 1,3,4,6-tetrakisphosphate 5-kinase
, inositol polyphosphate kinase 2