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Related Concept Videos

Phosphoinositides and PIPs01:42

Phosphoinositides and PIPs

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.
Different phosphoinositides are synthesized and recruited on the cytosolic face of the plasma membrane. The localization of specific phosphoinositides concentrated in separate membrane...

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Related Experiment Video

Updated: Jun 26, 2026

Fluorescence-Based Measurements of Phosphatidylserine/Phosphatidylinositol 4-Phosphate Exchange Between Membranes
08:49

Fluorescence-Based Measurements of Phosphatidylserine/Phosphatidylinositol 4-Phosphate Exchange Between Membranes

Published on: March 14, 2021

Phospholipid-interacting proteins by solution-state NMR spectroscopy.

Keiichiro Kami1, Sundaresan Rajesh, Michael Overduin

  • 1CR-UK Institute for Cancer Studies, School of Medicine, University of Birmingham, Birmingham, UK.

Methods in Molecular Biology (Clifton, N.J.)
|January 24, 2009
PubMed
Summary

New NMR methods enable detailed study of how proteins recognize signaling lipids like phosphatidylinositol 3-phosphate (PtdIns3P) in cell membranes, advancing our understanding of cell signaling and trafficking.

More Related Videos

PIP-on-a-chip: A Label-free Study of Protein-phosphoinositide Interactions
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PIP-on-a-chip: A Label-free Study of Protein-phosphoinositide Interactions

Published on: July 27, 2017

Single-molecule Super-resolution Imaging of Phosphatidylinositol 4,5-bisphosphate in the Plasma Membrane with Novel Fluorescent Probes
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Single-molecule Super-resolution Imaging of Phosphatidylinositol 4,5-bisphosphate in the Plasma Membrane with Novel Fluorescent Probes

Published on: October 15, 2016

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Last Updated: Jun 26, 2026

Fluorescence-Based Measurements of Phosphatidylserine/Phosphatidylinositol 4-Phosphate Exchange Between Membranes
08:49

Fluorescence-Based Measurements of Phosphatidylserine/Phosphatidylinositol 4-Phosphate Exchange Between Membranes

Published on: March 14, 2021

PIP-on-a-chip: A Label-free Study of Protein-phosphoinositide Interactions
10:58

PIP-on-a-chip: A Label-free Study of Protein-phosphoinositide Interactions

Published on: July 27, 2017

Single-molecule Super-resolution Imaging of Phosphatidylinositol 4,5-bisphosphate in the Plasma Membrane with Novel Fluorescent Probes
07:26

Single-molecule Super-resolution Imaging of Phosphatidylinositol 4,5-bisphosphate in the Plasma Membrane with Novel Fluorescent Probes

Published on: October 15, 2016

Area of Science:

  • Biochemistry and Molecular Biology
  • Cell Biology
  • Biophysics

Background:

  • Signaling lipids in cell membranes regulate protein interactions crucial for cellular processes.
  • Studying these lipid-protein interactions is challenging due to technical complexities.
  • Peripheral membrane proteins bind specific lipids to mediate signaling and membrane dynamics.

Purpose of the Study:

  • To develop and validate novel solution-state Nuclear Magnetic Resonance (NMR) methods.
  • To investigate the physical and chemical mechanisms of lipid recognition by membrane proteins.
  • To characterize protein interactions with phosphatidylinositol 3-phosphate (PtdIns3P).

Main Methods:

  • Utilized solution-state NMR spectroscopy.
  • Optimized methods for FYVE and phox (PX) domains of EEA1 and Vam7p proteins.
  • Applied techniques to analyze protein:micelle structures and phospholipid specificities.

Main Results:

  • Characterized phosphoinositide and membrane interaction sites and affinities.
  • Demonstrated the ability to illustrate protein:micelle structures.
  • Confirmed specificity for phosphatidylinositol 3-phosphate (PtdIns3P) binding.

Conclusions:

  • Developed broadly applicable NMR methods for studying membrane protein-lipid interactions.
  • These methods facilitate the discovery and characterization of phospholipid interactions.
  • Enhanced understanding of how proteins like EEA1 and Vam7p recognize PtdIns3P in endocytic membranes.