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Related Experiment Video

Updated: May 5, 2026

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

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

Published on: October 15, 2016

Short-chain phosphoinositide partitioning into plasma membrane models.

Marcus D Collins¹, Sharona E Gordon

¹University of Washington School of Medicine, Department of Physiology and Biophysics, Seattle, WA.

Biophysical Journal

|December 10, 2013

Summary

This summary is machine-generated.

Short-chain phosphoinositides partition into neuronal membranes, reaching physiological levels. This partitioning influences ion channel activity, affecting cellular electrophysiology and requiring reinterpretation of previous findings.

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

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

Published on: July 27, 2017

Area of Science:

Cellular Biology
Biophysics
Neuroscience

Background:

Phosphoinositides are crucial signaling molecules in cellular processes.
Short-chain phosphoinositides are commonly used to manipulate cellular phosphoinositide levels.
Understanding their membrane partitioning is key to interpreting experimental results.

Purpose of the Study:

To quantify the partitioning of abundant phosphoinositides (PI(4)P and PI(4,5)P2) into neuronal membrane models.
To determine if physiological membrane mole fractions can be achieved with common experimental solution concentrations.
To explore the implications of this partitioning for cellular electrophysiology and ion channel function.

Main Methods:

Isothermal titration calorimetry (ITC) was employed to measure lipid partitioning.
Neuronal plasma membrane models were used to simulate intracellular and extracellular leaflets.
The partitioning of PI(4)P and PI(4,5)P2 was analyzed.

Main Results:

Phosphoinositide mole fractions in the lipid membrane reached physiological levels at equilibrium with achievable solution concentrations.
TRPV1 channels demonstrated higher selectivity for PI(4,5)P2 over PI(4)P.
Extremely low membrane mole fractions of phosphoinositides were sufficient for TRPV1 activation.

Conclusions:

The partitioning behavior of short-chain phosphoinositides is critical for their function in cellular signaling and electrophysiology.
Previous models of PI(4,5)P2 regulation for K(+) channels may need revision based on lipid acyl chain length and partitioning.
The interpretation of experiments involving inward rectifier K(+) channels requires re-evaluation considering differential phosphoinositide membrane partitioning.