Related Experiment Video
Updated: May 7, 2026

10:23
Lipid Droplet Isolation for Quantitative Mass Spectrometry Analysis
Published on: April 17, 2017
Dictyostelium lipid droplets host novel proteins
Xiaoli Du1, Caroline Barisch, Peggy Paschke
1Abteilung Zellbiologie.
Eukaryotic Cell
|September 17, 2013
Summary
This study investigates lipid droplets in Dictyostelium discoideum, revealing similar lipid composition to mammals. Novel proteins, including Dictyostelium-specific LdpA and Net4, were identified, supporting their formation on the endoplasmic reticulum.
Area of Science:
- Cell Biology
- Biochemistry
- Molecular Biology
Background:
- Lipid droplets are vital organelles for cellular energy storage across all life forms.
- They feature a hydrophobic core of triglycerides and steryl esters, enclosed by a single membrane leaflet from the endoplasmic reticulum (ER).
- Specific proteins are associated with the ER-derived membrane of lipid droplets.
Purpose of the Study:
- To determine the kinetics of lipid droplet formation and degradation in Dictyostelium discoideum.
- To identify the specific lipid constituents and protein components of lipid droplets in this model organism.
- To compare the lipid droplet characteristics of Dictyostelium discoideum with those found in mammalian cells.
Main Methods:
- Utilized Dictyostelium discoideum as a model system for studying lipid droplet dynamics.
- Performed detailed analysis of lipid composition, including phospholipids and neutral lipids.
- Identified and characterized novel protein components associated with lipid droplets using proteomic techniques.
Main Results:
- The lipid composition of Dictyostelium discoideum lipid droplets closely resembles that of mammalian lipid droplets.
- Phospholipids in these droplets are predominantly composed of saturated fatty acids.
- Neutral lipids are enriched in unsaturated fatty acids, and novel proteins LdpA and Net4 were identified.
Conclusions:
- Lipid droplets in Dictyostelium discoideum share conserved lipid features with mammalian counterparts.
- The identification of LdpA and Net4 provides new insights into the protein machinery of lipid droplets.
- Observed protein movement from the ER to lipid droplets supports the model of lipid droplet biogenesis originating on the ER membrane.
Related Concept Videos
Membrane Domains
The membrane domains concentrate specific lipids and proteins at one place within the membrane, which helps in cell signaling, adhesion, and other critical cellular processes. These domains can differ in size, composition, function, and lifespan.
Protein Domains
The membrane comprises a group of distinct proteins responsible for carrying out a cell's specific function. For example, the plasma membrane of the human sperm, or a single germ cell, contains a unique set of proteins in the anterior...
Protein Domains
The membrane comprises a group of distinct proteins responsible for carrying out a cell's specific function. For example, the plasma membrane of the human sperm, or a single germ cell, contains a unique set of proteins in the anterior...
Biosynthesis of Lipids
Microbial membranes exhibit remarkable diversity in lipid composition, reflecting evolutionary adaptations to various environmental conditions. The three domains of life—Bacteria, Archaea, and Eukarya—synthesize membrane lipids through distinct biosynthetic pathways, leading to fundamental structural differences that impact membrane stability, function, and adaptability.Fatty Acid-Based Lipids in Bacteria and EukaryaBacteria and eukaryotes share a common fatty acid biosynthesis pathway, which...
Membrane Fluidity
Membrane fluidity is explained by the fluid mosaic model of the cell membrane, which describes the plasma membrane structure as a mosaic of components—including phospholipids, cholesterol, proteins, and carbohydrates—that gives the membrane a fluid character.
Mosaic nature of the membrane
The mosaic characteristic of the membrane helps the plasma membrane remain fluid. The integral proteins and lipids exist as separate but loosely-attached molecules in the membrane. The membrane is a relatively...
Mosaic nature of the membrane
The mosaic characteristic of the membrane helps the plasma membrane remain fluid. The integral proteins and lipids exist as separate but loosely-attached molecules in the membrane. The membrane is a relatively...
Mechanisms of Membrane Domain Formation
Different physical properties of lipids and proteins allow them to localize and form distinct islands or domains in the membrane. Some membrane domains are formed due to protein-protein interactions, whereas others are formed due to the presence of specific lipids such as sphingolipids and sterols—for example, large proteins, such as bacteriorhodopsin, aggregate and create distinct domains.
Another mechanism for membrane domain formation involves membrane proteins interacting with cytoskeletal...
Another mechanism for membrane domain formation involves membrane proteins interacting with cytoskeletal...
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%...
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...
The carboxy-terminal of most of the prenylated proteins, such as Ras proteins, contains the...

