Inositide Evolution: What can it tell us about Functions?

Irvine, Robin F.

doi:10.1042/bst0230027

Cited by 19 publications

(9 citation statements)

References 41 publications

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“…Originally, one of us suggested that the appearance of Ins(1,4,5)P 3 3-kinase was also early and preceded the split between plants and animals [26]. However, the Chlamydomonas Ins(1,4,5)P 3 kinase [25], whose existence led to this suggestion, can now be seen probably to be akin to the Ins-(1,4,5)P 3 3/6-kinases discussed above [6,22,23] in so far as it has a low a¤nity for Ins(1,4,5)P 3 , no detectable regulation by Ca 2 and (assuming it is only one enzyme) it converts its InsP 4 product(s) directly into Ins(1,3,4,5,6)P 5 .…”

Section: Resultsmentioning

confidence: 99%

PiUS (Pi uptake stimulator) is an inositol hexakisphosphate kinase

et al. 1999

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A cDNA cloned from its ability to stimulate inorganic phosphate uptake in Xenopus oocytes (phosphate uptake stimulator (PiUS)) shows significant similarity with inositol 1,4,5-trisphosphate 3-kinase. However, the expressed PiUS protein showed no detectable activity against inositol 1,4,5-trisphosphate, nor the 1,3,4,5-or 3,4,5,6-isomers of inositol tetrakisphosphate, whereas it was very active in converting inositol hexakisphosphate (InsP 6 ) to inositol heptakisphosphate (InsP 7 ). PiUS is a member of a family of enzymes found in many eukaryotes and we discuss the implications of this for the functions of InsP 7 and for the evolution of inositol phosphate kinases.z 1999 Federation of European Biochemical Societies.

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Section: Resultsmentioning

confidence: 99%

PiUS (Pi uptake stimulator) is an inositol hexakisphosphate kinase

et al. 1999

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“…The major metabolic pathway for generating Ins(1,3,4,5)P4 is through Ins(1,4,5)P3 (Irvine, 1995;Irvine and Schell, 2001). Ins(1,4,5)P3 is formed from the hydrolysis of PtdIns(4,5)P2 by phospholipase C (PLC or PI-PLC).…”

Section: Discussionmentioning

confidence: 99%

Inositol 1,3,4,5-Tetrakisphosphate Negatively Regulates Phosphatidylinositol-3,4,5- Trisphosphate Signaling in Neutrophils

et al. 2007

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Many neutrophil functions are regulated by phosphatidylinositol-3,4,5-trisphosphate (PtdIns(3,4,5)P3) that mediates protein membrane translocation via binding to pleckstrin homolog (PH) domains within target proteins. Here we show that inositol 1,3,4,5-tetrakisphosphate (Ins(1,3,4,5)P4), a cytosolic small molecule, bound the same PH domain of target proteins and competed for binding to PtdIns(3,4,5)P3. In neutrophils, chemoattractant stimulation triggered rapid elevation in Ins(1,3,4,5)P4 concentration. Depletion of Ins(1,3,4,5)P4 by deleting the gene encoding InsP3KB, which converts Ins(1,4,5)P3 to Ins(1,3,4,5)P4, enhanced membrane translocation of the PtdIns(3,4,5)P3-specific PH domain. This led to enhanced sensitivity to chemoattractant stimulation, elevated superoxide production, and enhanced neutrophil recruitment to inflamed peritoneal cavity. On the contrary, augmentation of intracellular Ins(1,3,4,5)P4 concentration blocked PH domain-mediated membrane translocation of target proteins and dramatically decreased the sensitivity of neutrophils to chemoattractant stimulation. These findings establish a role for Ins(1,3,4,5)P4 in cellular signal transduction pathways and provide another mechanism for modulating PtdIns(3,4,5)P3 signaling in neutrophils.

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“…Regulation of innate immunity by Ins (1,3,4,5 1,50 It appears that dephosphorylation of InsP5 or InsP6 is not the major source for Ins(1,3,4,5)P4 production, since InsP5 and InsP6 levels are not reduced upon fMLP stimulation. 1,2,16 Ins(1,4,5)P3 is formed from the hydrolysis of PtdIns(4,5)P2 by phospholipase C (PLC or PI-PLC).…”

confidence: 99%