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Protein Networks

Protein Networks

An organism can have thousands of different proteins, and these proteins must cooperate to ensure the health of an organism. Proteins bind to other proteins and form complexes to carry out their functions. Many proteins interact with multiple other proteins creating a complex network of protein interactions.
These interactions can be represented through maps depicting protein-protein interaction networks, represented as nodes and edges. Nodes are circles that are representative of a protein,...

Protein Networks

Protein Networks

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...

Protein-Protein Interfaces

Protein-Protein Interfaces

Protein Complexes with Interchangeable Parts

Protein Complexes with Interchangeable Parts

Groups of proteins may form a complex where each protein in this complex has a different role in the overall execution of the complex’s function. Often some of the proteins in the complex can be replaced by a closely related variant to give a complex that contains many of the same components yet is functionally distinct.
The SCF ubiquitin ligase is a protein complex of five individual proteins. This complex attaches ubiquitin to other target proteins to mark them for degradation. In order...

Protein Complexes with Interchangeable Parts

Protein Complexes with Interchangeable Parts

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Related Experiment Video

Updated: May 4, 2026

Characterization of Neuronal Lysosome Interactome with Proximity Labeling Proteomics

Characterization of Neuronal Lysosome Interactome with Proximity Labeling Proteomics

Published on: June 23, 2022

The LC3 interactome at a glance.

Philipp Wild¹, David G McEwan, Ivan Dikic

¹Institute of Biochemistry II, Goethe University, Theodor-Stern-Kai 7, 60590 Frankfurt am Main, Germany.

Journal of Cell Science

|December 19, 2013

Summary

This summary is machine-generated.

Autophagy relies on proteins like Atg8, specifically the light chain 3 (LC3) and GABARAP families, to manage cellular component turnover and maintain homeostasis. Understanding their interactions is key to regulating this vital degradation process.

Keywords:

AIM Atg8 Autophagy GABARAP LC3 LIR motif

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Last Updated: May 4, 2026

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Mapping Dysfunctional Protein-Protein Interactions in Disease

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Published on: October 24, 2025

Area of Science:

Cell Biology
Molecular Biology
Biochemistry

Background:

Cellular homeostasis requires continuous synthesis and turnover of components.
Eukaryotic cells utilize the ubiquitin-proteasome system and lysosomal pathway for degradation.
Autophagy, a lysosomal pathway, uses autophagosomes to deliver intracellular material for degradation.

Purpose of the Study:

To present the current understanding of the LC3/GABARAP protein interaction network.
To highlight the role of this network in regulating autophagy.
To provide insights into autophagosome initiation and biogenesis.

Main Methods:

Review of existing literature on autophagy proteins.
Analysis of the Atg8 protein family, including LC3 and GABARAP members.
Compilation of the LC3 protein interaction network.

Main Results:

The Atg8 family, comprising LC3 and GABARAP proteins, is central to autophagy.
Deciphering the molecular mechanisms of these proteins has advanced autophagy research.
The LC3 protein interaction network is crucial for understanding autophagy regulation.

Conclusions:

The LC3/GABARAP protein network is vital for orchestrating autophagosome formation.
Continued research into these interactions deepens our knowledge of autophagy.
This network provides a framework for understanding the regulation of cellular degradation.