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Phosphoinositides and PIPs

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...

Protein Kinases and Phosphatases

Protein Kinases and Phosphatases

Proteins undergo chemical modifications that trigger changes in the charge, structure, and conformation of the proteins. Phosphorylation, acetylation, glycosylation, nitrosylation, ubiquitination, lipidation, methylation, and proteolysis are various protein modifications that regulate protein activity. Such modifications are usually enzyme-driven.
Protein kinases
Many proteins in the cell are regulated by phosphorylation, the addition of a phosphate group. A family of enzymes called kinases...

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Related Experiment Video

Updated: Nov 20, 2025

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

Liposome-Based Methods to Study Protein-Phosphoinositide Interaction.

Mélanie Mansat¹, Mélanie Picot¹, Gaëtan Chicanne¹

¹INSERM U1048 and Université Toulouse 3, Toulouse Cedex, France.

Methods in Molecular Biology (Clifton, N.J.)

|January 22, 2021

Summary

This summary is machine-generated.

Phosphoinositides are key regulators of cell processes. New methods, liposome flotation and protein-lipid interaction by fluorescence (PLIF), characterize how proteins bind to these lipids.

Keywords:

Liposome Liposome flotation Phosphoinositide Protein–lipid interaction Protein–lipid interaction by fluorescence

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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

Area of Science:

Biochemistry
Cell Biology
Molecular Biology

Background:

Phosphoinositides regulate critical cellular functions including cytoskeleton dynamics, membrane trafficking, and gene expression.
Protein domains like PH, PX, and FYVE specifically bind to the inositol head group of phosphoinositides.
Understanding phosphoinositide-protein interactions is crucial for deciphering cellular physiology.

Purpose of the Study:

To describe experimental setups for characterizing phosphoinositide-binding specificities of proteins.
To introduce and detail the protein-lipid interaction by fluorescence (PLIF) assay.
To highlight the utility of liposome-based methods for studying these interactions.

Main Methods:

Liposome flotation assay: a method to separate proteins bound to liposomes based on density.
Protein-lipid interaction by fluorescence (PLIF): a novel fluorescence-based assay for quantifying protein-lipid binding.
Liposome preparation: incorporating phosphoinositides into artificial membranes that mimic cellular compositions.

Main Results:

Established protocols for liposome flotation assay and PLIF are presented.
PLIF enables detailed characterization of phosphoinositide-binding specificities.
Liposome-based assays provide a membrane-mimicking environment for studying these interactions.

Conclusions:

Liposome flotation and PLIF are valuable tools for investigating phosphoinositide-protein interactions.
These methods aid in understanding the specificity of lipid signaling pathways.
Accurate characterization of these interactions is vital for comprehending cellular regulation.