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Related Experiment Video

Updated: May 10, 2026

Radiolabeling and Quantification of Cellular Levels of Phosphoinositides by High Performance Liquid Chromatography-coupled Flow Scintillation
10:52

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

Published on: January 6, 2016

Recognizing phosphatidylinositol 3-phosphate.

S Misra1, G J Miller, J H Hurley

  • 1Laboratory of Molecular Biology, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD 20892, USA.

Cell
|December 6, 2001
PubMed
Summary
This summary is machine-generated.

Phosphatidylinositol 3-phosphate (PI3P) guides endosomal protein localization via FYVE and PX domains. New structures reveal how PI3P’s specific chemical interactions distinguish it from other lipids.

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Identification of Inositol Phosphate or Phosphoinositide Interacting Proteins by Affinity Chromatography Coupled to Western Blot or Mass Spectrometry
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Last Updated: May 10, 2026

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Single-molecule Super-resolution Imaging of Phosphatidylinositol 4,5-bisphosphate in the Plasma Membrane with Novel Fluorescent Probes
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Identification of Inositol Phosphate or Phosphoinositide Interacting Proteins by Affinity Chromatography Coupled to Western Blot or Mass Spectrometry
08:07

Identification of Inositol Phosphate or Phosphoinositide Interacting Proteins by Affinity Chromatography Coupled to Western Blot or Mass Spectrometry

Published on: July 26, 2019

Area of Science:

  • Biochemistry
  • Cell Biology
  • Structural Biology

Background:

  • Phosphatidylinositol 3-phosphate (PI3P) is a key signaling lipid in endosomal trafficking.
  • FYVE and PX domains are known to bind PI3P, mediating protein localization.
  • Understanding the molecular basis of PI3P recognition is crucial for deciphering endosomal sorting mechanisms.

Purpose of the Study:

  • To elucidate the structural basis of PI3P recognition by FYVE and PX domains.
  • To understand how these domains differentiate PI3P from other phosphoinositides.
  • To provide insights into the role of PI3P in directing endosomal protein localization.

Main Methods:

  • X-ray crystallography was used to determine the structures of FYVE and PX domains in complex with PI3P.
  • Structural analysis focused on the interactions between the protein domains and the phosphoinositide headgroup.
  • Comparative analysis with other phosphoinositides was performed.

Main Results:

  • Novel structures reveal detailed interactions between FYVE/PX domains and the PI3P headgroup.
  • Specific hydrogen bonds and electrostatic interactions involving phosphate and hydroxyl groups were identified.
  • These interactions precisely discriminate PI3P from other phosphoinositides, such as PI(4,5)P2.

Conclusions:

  • The elucidated structures provide a molecular explanation for PI3P specificity.
  • These findings highlight the critical role of PI3P-binding domains in endosomal protein targeting.
  • The study offers a framework for understanding lipid-mediated regulation of endosomal function.