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Related Concept Videos

Assembly of Signaling Complexes01:30

Assembly of Signaling Complexes

Multiprotein signaling complexes are formed in a dynamic process involving protein-protein interactions at the cytoplasmic domain of transmembrane receptors or enzymatic and non-enzymatic proteins associated with the receptor. These complexes ensure the activation and propagation of intracellular signals that regulate cell functions.
Interaction domains in cell signaling
Interaction domains recognize exposed features of their binding partners containing post-translationally modified sequences,...
Protein Networks02:26

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-protein Interfaces02:04

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...
Protein-Protein Interfaces02:04

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...
Protein Complexes with Interchangeable Parts01:57

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 to...
Protein Complexes with Interchangeable Parts01:57

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 to...

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Updated: Jun 16, 2026

Dissecting Multi-protein Signaling Complexes by Bimolecular Complementation Affinity Purification (BiCAP)
06:45

Dissecting Multi-protein Signaling Complexes by Bimolecular Complementation Affinity Purification (BiCAP)

Published on: June 15, 2018

The Beclin 1 interactome.

Congcong He1, Beth Levine

  • 1Howard Hughes Medical Institute, University of Texas Southwestern Medical Center, Dallas, TX 75390, United States.

Current Opinion in Cell Biology
|January 26, 2010
PubMed
Summary
This summary is machine-generated.

Beclin 1 is a key autophagy protein regulating immunity, development, and disease. Its interactions with various partners control autophagy and membrane trafficking in different contexts.

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Last Updated: Jun 16, 2026

Dissecting Multi-protein Signaling Complexes by Bimolecular Complementation Affinity Purification (BiCAP)
06:45

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Published on: June 15, 2018

Identifying Protein-protein Interaction Sites Using Peptide Arrays
07:44

Identifying Protein-protein Interaction Sites Using Peptide Arrays

Published on: November 18, 2014

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09:39

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Published on: October 24, 2025

Area of Science:

  • Molecular Biology
  • Cell Biology
  • Biochemistry

Background:

  • Beclin 1 is an essential autophagy protein, homologous to yeast Atg6/Vps30.
  • It plays critical roles in immunity, development, tumor suppression, lifespan, and protection against cardiac and neurodegenerative diseases.

Purpose of the Study:

  • To review recent advances in understanding Beclin 1 function.
  • To explore the Beclin 1 interactome and its role in regulating autophagy and membrane trafficking.

Main Methods:

  • Identification of Beclin 1/class III phosphatidylinositol 3-kinase complex components.
  • Characterization of Beclin 1 interactions with autophagy inhibitors (Bcl-2/BcL-X(L)).
  • Investigation of viral Beclin 1 antagonists in pathogenesis.

Main Results:

  • Distinct Beclin 1 complexes have been identified.
  • Molecular regulation of Beclin 1 interactions with Bcl-2/BcL-X(L) has been elucidated.
  • Viral antagonists of Beclin 1 contribute to viral pathogenesis.

Conclusions:

  • The Beclin 1 interactome is expanding, supporting a regulatory model.
  • Autophagy and Beclin 1's other membrane trafficking functions are governed by context-dependent interactions.