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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...

Lipids as Anchors

Lipids as Anchors

In the plasma membrane, the lipids forming the bilayer can also act as an anchor to tether proteins to the membrane. The three main types of lipid anchors found in eukaryotes are – prenyl groups, fatty acyl groups, and glycosylphosphatidylinositol or GPI groups. Prenyl and fatty acyl groups act as anchors on the cytosolic surface of the membrane, whereas GPI anchors proteins on the extracellular side.
The carboxy-terminal of most of the prenylated proteins, such as Ras proteins, contains the...

Surface Active Agents

Surface Active Agents

Surfactants, named for their behavior at interfaces, positively adsorb at the interfaces of two phases, reducing interfacial tension. Their versatility as emulsifiers, detergents, and foaming agents stems from this ability. Surfactants, often termed amphiphiles, share the property of amphipathy, with molecules having both hydrophilic and hydrophobic portions. The hydrophilic part is called the head, and the hydrophobic part, including an elongated alkyl substituent, forms the tail.Surfactants...

Asymmetric Lipid Bilayer

Asymmetric Lipid Bilayer

Biological membranes show uneven distribution of different types of lipids in the inner and outer layers, resulting in transverse asymmetric membranes. The treatment of the erythrocyte membrane with the enzyme phospholipase confirmed the asymmetric nature of the lipid bilayer. The enzyme hydrolyzes lipids into fatty acids and hydrophilic groups. The phospholipase acts only on the outer layer of the membrane, while the inner layer remains intact. The phospholipase treatment resulted in 80%...

Protein-protein Interfaces

Protein-protein Interfaces

Many proteins form complexes to carry out their functions, making protein-protein interactions (PPIs) essential for an organism's survival. Most PPIs are stabilized by numerous weak noncovalent chemical forces. The physical shape of the interfaces determines the way two proteins interact. Many globular proteins have closely-matching shapes on their surfaces, which form a large number of weak bonds. Additionally, many PPIs occur between two helices or between a surface cleft and a polypeptide...

Membrane Asymmetry Regulating Transporters

Membrane Asymmetry Regulating Transporters

Enzymes like flippase, floppase, and scramblase transfer phospholipids from one layer to another in the membrane, thereby affecting membrane asymmetry.
Flippase
Eukaryotic flippases are type-IV P-type ATPases or P4-ATPases belonging to P-type ATPase family proteins that are membrane-bound pumps involved in the ATP-mediated transport of ions and molecules across the membrane. Flippases flip specific phospholipids from the outer to the inner leaflet of a membrane. All P4-ATPases have one...

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Related Experiment Video

Updated: Jul 20, 2026

A Liposome Membrane Permeability Assay for Investigating the Effects of Phosphatidylinositol Phosphate Groups on Membranotropic Action of Venom PLA2

A Liposome Membrane Permeability Assay for Investigating the Effects of Phosphatidylinositol Phosphate Groups on Membranotropic Action of Venom PLA₂

Published on: September 26, 2025

The interfacial binding surface of phospholipase A2s.

Jason M Winget¹, Ying H Pan, Brian J Bahnson

¹Department of Chemistry and Biochemistry, University of Delaware, Newark, DE 19716, USA.

Biochimica Et Biophysica Acta

|September 12, 2006

Summary

Understanding interfacial enzymes like Phospholipase A2 (PLA2) is key for membrane-associated catalysis. This study models PLA2 interfacial faces, revealing conserved structures but divergent sequences that influence substrate selectivity.

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Last Updated: Jul 20, 2026

A Liposome Membrane Permeability Assay for Investigating the Effects of Phosphatidylinositol Phosphate Groups on Membranotropic Action of Venom PLA2

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Defining Substrate Specificities for Lipase and Phospholipase Candidates

Defining Substrate Specificities for Lipase and Phospholipase Candidates

Published on: November 23, 2016

Area of Science:

Biochemistry
Biophysics
Enzymology

Background:

Membrane-associated enzymes require partitioning to phospholipid interfaces for catalysis.
Interfacial recognition and adsorption mechanisms remain poorly understood.
The enzyme's interfacial binding surface (i-face) is crucial for substrate access and allosteric activation.

Purpose of the Study:

To review current knowledge on i-face structure and function for secreted Phospholipase A2 (PLA2).
To develop, characterize, and compare models of the PLA2 i-face across five homologous groups (IA, IB, IIA, V, X).
To explore the potential of homology modeling for investigating interfacial function in other PLA2 family members.

Main Methods:

Literature review on PLA2 i-face structure and function.
Development and characterization of computational models for PLA2 i-faces.
Comparative analysis of five homologous PLA2 family members (groups IA, IB, IIA, V, X).
Homology modeling of human group-V PLA2.

Main Results:

Structural homology and sequence similarity are conserved among the studied PLA2 family members.
Interfacial residues are structurally conserved but show low sequence conservation.
Divergence in interfacial residues has implications for enzyme selectivity.

Conclusions:

Computational modeling provides insights into PLA2 interfacial function.
Conserved structures with divergent interfacial residues suggest mechanisms for substrate selectivity.
The approach can be extended to study other PLA2 family members and interfacial enzymes.