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Related Experiment Video

Updated: Nov 18, 2025

Assessing Autophagic Flux by Measuring LC3, p62, and LAMP1 Co-localization Using Multispectral Imaging Flow Cytometry

Assessing Autophagic Flux by Measuring LC3, p62, and LAMP1 Co-localization Using Multispectral Imaging Flow Cytometry

Published on: July 21, 2017

Systematically defining selective autophagy receptor-specific cargo using autophagosome content profiling.

Susanne Zellner¹, Martina Schifferer², Christian Behrends¹

¹Munich Cluster for Systems Neurology (SyNergy), Medical Faculty, Ludwig-Maximilians-University München, Feodor-Lynen Strasse 17, 81377 Munich, Germany.

|February 5, 2021

Summary

This summary is machine-generated.

Cellular protein clearance relies on autophagy, a process that removes damaged proteins. This study maps protein targets of autophagy receptors, revealing how different receptors handle protein aggregates.

Keywords:

APEX2 SQSTM1/p62 TOLLIP aggrephagy autophagosomes autophagy endosomal microautophagy proteostasis imbalance proximity labeling selective autophagy receptors

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Published on: July 27, 2018

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Last Updated: Nov 18, 2025

Assessing Autophagic Flux by Measuring LC3, p62, and LAMP1 Co-localization Using Multispectral Imaging Flow Cytometry

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The Lactate Dehydrogenase Sequestration Assay — A Simple and Reliable Method to Determine Bulk Autophagic Sequestration Activity in Mammalian Cells

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Published on: July 27, 2018

Area of Science:

Cell Biology
Molecular Biology
Biochemistry

Background:

Autophagy is crucial for maintaining cellular proteostasis by clearing protein aggregates.
Selective autophagy pathways, like aggrephagy, utilize receptors with ubiquitin-binding domains (UBDs) to target ubiquitinated proteins.
The specific substrates and receptor redundancy in aggrephagy remain largely unknown.

Purpose of the Study:

To systematically identify aggrephagy substrates and map the autophagic degradome.
To investigate the roles of UBD-containing receptors in substrate recognition and engulfment.
To understand the differential engagement of receptors with substrates under various cellular conditions.

Main Methods:

Utilized proximity labeling and organelle enrichment techniques.
Employed quantitative proteomics to analyze protein cargo.
Studied human cell lines under basal and proteostasis-challenging conditions.

Main Results:

Identified a comprehensive list of autophagy substrates.
Discovered differential engulfment of substrates by autophagosomal (p62) and endosomal (TOLLIP) membranes.
Revealed insights into the substrate specificity and redundancy of UBD-containing receptors.

Conclusions:

Provides a valuable resource for dissecting the proteostasis contribution of autophagy to individual proteins.
Highlights the distinct roles of autophagy receptors in substrate selection and degradation pathways.
Advances the understanding of selective autophagy and its role in cellular quality control.