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Publication Detail
Inositol pyrophosphates mediate chemotaxis in Dictyostelium via pleckstrin homology domain-PtdIns(3,4,5)P3 interactions.
  • Publication Type:
    Journal article
  • Publication Sub Type:
    Journal Article
  • Authors:
    Luo HR, Huang YE, Chen JC, Saiardi A, Iijima M, Ye K, Huang Y, Nagata E, Devreotes P, Snyder SH
  • Publication date:
  • Pagination:
    559, 572
  • Journal:
  • Volume:
  • Issue:
  • Country:
    United States
  • Print ISSN:
  • PII:
  • Language:
  • Keywords:
    Amino Acid Sequence, Animals, Blotting, Northern, Blotting, Southern, Blotting, Western, Cell Membrane, Chemotaxis, Chromatography, High Pressure Liquid, Cloning, Molecular, Cyclic AMP, DNA, Dictyostelium, Dose-Response Relationship, Drug, Gene Deletion, Green Fluorescent Proteins, Guanosine 5'-O-(3-Thiotriphosphate), Inositol Phosphates, Luminescent Proteins, Models, Genetic, Molecular Sequence Data, Mutation, Phosphatidylinositol Phosphates, Protein Binding, Protein Structure, Tertiary, Protein Transport, Sequence Homology, Amino Acid, Signal Transduction, Time Factors
Inositol phosphates are well-known signaling molecules, whereas the inositol pyrophosphates, such as diphosphoinositol pentakisphosphate (InsP7/IP7) and bis-diphosphoinositol tetrakisphosphate (InsP8/IP8), are less well characterized. We demonstrate physiologic regulation of Dictyostelium chemotaxis by InsP7 mediated by its competition with PtdIns(3,4,5)P3 for binding pleckstrin homology (PH) domain-containing proteins. Chemoattractant stimulation triggers rapid and sustained elevations in InsP7/InsP8 levels. Depletion of InsP7 and InsP8 by deleting the gene for InsP6 kinase (InsP6K/IP6K), which converts inositol hexakisphosphate (InsP6/IP6) to InsP7, causes rapid aggregation of mutant cells and increased sensitivity to cAMP. Chemotaxis is mediated by membrane translocation of certain PH domain-containing proteins via specific binding to PtdIns(3,4,5)P3. InsP7 competes for PH domain binding with PtdIns(3,4,5)P3 both in vitro and in vivo. InsP7 depletion enhances PH domain membrane translocation and augments downstream chemotactic signaling activity.
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