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Related Experiment Video

Updated: May 31, 2026

High-Resolution Complexome Profiling by Cryoslicing BN-MS Analysis

High-Resolution Complexome Profiling by Cryoslicing BN-MS Analysis

Published on: October 15, 2019

Latex beads internalization and quantitative proteomics join forces to decipher the endosomal proteome.

Mariana Eça Guimarães de Araújo¹, Lukas Alfons Huber, Taras Stasyk

¹Division of Cell Biology, Biocenter, Innsbruck Medical University, Fritz-Pregl Str. 3, A-6020 Innsbruck, Austria.

Expert Review of Proteomics

|June 18, 2011

Summary

Researchers developed a new method for purifying endosomes, enabling detailed proteome analysis. This advance aids in understanding endosomal functions and diseases linked to endosomal defects.

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Last Updated: May 31, 2026

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Area of Science:

Cell biology
Proteomics
Biochemistry

Background:

Limited purity of endosomal fractions hinders proteome analysis using current biochemical methods.
Accurate proteome profiling is crucial for understanding endosomal function and associated diseases.

Discussion:

A novel method using latex beads and gradient centrifugation achieves highly purified endosomal organelles.
This technique was combined with redundant peptide counting for quantitative proteome comparison.
The approach validates its applicability through identification of known markers and novel endosomal proteins.

Key Insights:

Achieved high purity of endosomal organelles, overcoming previous limitations.
Successfully quantified relative protein abundance within endosomes.
Identified novel proteins associated with endosomal compartments.

Outlook:

Enables creation of a comprehensive endosomal proteome chart.
Facilitates study of time- and signaling-dependent proteome dynamics.
Offers potential to uncover molecular mechanisms of diseases involving endosomal biogenesis defects.