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Related Concept Videos

IP3/DAG Signaling Pathway01:11

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Membrane lipids such as phosphatidylinositol (PI) are precursors for several membrane-bound and soluble second messengers. Specific kinases phosphorylate PI and produce phosphorylated inositol phospholipids. One such inositol phospholipids are the  phosphatidylinositol-4,5 bisphosphate [PI(4,5)P2], present in the inner half of the lipid bilayer. Upon ligand binding, GPCR stimulates Gq proteins to turn on phospholipase Cꞵ. Activated phospholipase Cꞵ cleaves PI(4,5)P2 and...
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Phosphoinositides are a group of phospholipids containing a glycerol backbone with two fatty acid chains and a phosphate attached to a myoinositol sugar ring. The inositol head group extends into the cytoplasm, where it is modified by adding phosphate groups to form phosphatidylinositol phosphates or PIPs.
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Because many receptor binding ligands are hydrophilic, they do not cross the cell membrane and thus their message must be relayed to a second messenger on the inside. There are several second messenger pathways, each with their own way of relaying information. G-protein coupled receptors can activate both phosphoinositol and cyclic AMP (cAMP) second messenger pathways. The phosphoinositol path is active when the receptor induces phospholipase C to hydrolyze the phospholipid,...
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Calmodulin (CaM) is a calcium-binding protein in eukaryotes that controls various calcium-regulated cellular processes. It has four calcium-binding sites that bind calcium to form the calcium-calmodulin ( Ca2+-CaM) complex. GPCR stimulation increases the calcium levels in the cells that bind to CaM and induces a conformational change.
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G-protein coupled receptors are ligand binding receptors that indirectly affect changes in the cell. The actual receptor is a single polypeptide that transverses the cell membrane seven times creating intracellular and extracellular loops. The extracellular loops create a ligand specific pocket which binds to neurotransmitters or hormones. The intracellular loops holds onto the G-protein.
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Related Experiment Video

Updated: Aug 4, 2025

Identification of Inositol Phosphate or Phosphoinositide Interacting Proteins by Affinity Chromatography Coupled to Western Blot or Mass Spectrometry
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Non-inositol 1,4,5-trisphosphate (IP3) receptor IP3-binding proteins.

John James Mackrill1

  • 1Department of Physiology, University College Cork, Western Gateway Building, Western Road, Cork T12 XF62, Ireland.

Biochimica Et Biophysica Acta. Molecular Cell Research
|April 3, 2023
PubMed
Summary

Myo-D-inositol 1,4,5-trisphosphate (IP3) may interact with proteins beyond IP3 receptors. This study identified 26 diverse proteins, including enzymes and ion channels, that bind IP3, suggesting broader roles in cell signaling.

Keywords:
Ligand-protein interactionMyo-D-inositol 1,4,5-trisphosphateProtein structureSignal transduction

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Radiolabeling and Quantification of Cellular Levels of Phosphoinositides by High Performance Liquid Chromatography-coupled Flow Scintillation
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Area of Science:

  • Cellular Biology
  • Molecular Signaling
  • Biochemistry

Background:

  • Myo-D-inositol 1,4,5-trisphosphate (IP3) is traditionally known as a second messenger that gates IP3 receptor (IP3R) Ca2+ channels.
  • Emerging evidence suggests IP3 may interact with non-IP3R proteins, hinting at broader cellular functions.

Purpose of the Study:

  • To investigate the potential for IP3 to interact with proteins other than IP3 receptors.
  • To identify novel IP3-binding proteins and explore their implications in cellular signaling pathways.

Main Methods:

  • A comprehensive search of the Protein Data Bank was conducted using the term "IP3".
  • Protein structures complexed with IP3 were analyzed for interactions with the carbon-1 phosphate of IP3.
  • The identified structures were categorized to understand the diversity of IP3-interacting proteins.

Main Results:

  • Out of 203 retrieved protein structures, 49 were complexed with IP3.
  • Analysis focused on IP3's carbon-1 phosphate interaction, reducing the list to 35 structures.
  • Nine of these were IP3 receptors; the remaining 26 included enzymes, signal transducers, cytoskeletal proteins, and the TRPV4 ion channel.

Conclusions:

  • IP3 interacts with a diverse range of proteins beyond its canonical receptors.
  • These novel interactions suggest IP3 plays a more extensive role in cellular signaling and function.
  • Further research into these non-IP3R interactions is warranted to fully elucidate IP3's cellular roles.