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Protein Complexes with Interchangeable Parts

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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...

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Related Experiment Video

Updated: Sep 29, 2025

Combining Chemical Cross-linking and Mass Spectrometry of Intact Protein Complexes to Study the Architecture of Multi-subunit Protein Assemblies

Combining Chemical Cross-linking and Mass Spectrometry of Intact Protein Complexes to Study the Architecture of Multi-subunit Protein Assemblies

Published on: November 28, 2017

Quality control of protein complex composition.

Chris Padovani¹, Predrag Jevtić², Michael Rapé³

¹Department of Molecular and Cell Biology, University of California at Berkeley, Berkeley, CA 94720, USA.

|March 22, 2022

Summary

This summary is machine-generated.

Cells use ubiquitin-dependent quality control to manage protein complexes. This system prevents, corrects, or degrades flawed complexes, ensuring proper cell function and signaling pathways.

Keywords:

aneuploidy dimerization quality control orphan quality control proteasome quality control ubiquitin ubiquitylation

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Published on: April 1, 2017

Area of Science:

Molecular biology
Cellular processes
Protein biochemistry

Background:

Eukaryotic cells assemble numerous multi-subunit protein complexes crucial for development and signaling.
Assembly errors, such as missing or aberrant subunits, can lead to non-functional complexes and disrupt cellular events.
Cells have evolved sophisticated mechanisms to maintain the integrity of these complexes.

Purpose of the Study:

To review the emerging understanding of quality control mechanisms for protein complex composition in eukaryotic cells.
To highlight the role of ubiquitin-dependent pathways in managing protein complex assembly and integrity.
To discuss how cells prevent, correct, or degrade aberrant protein complexes.

Main Methods:

Literature review of current research on protein complex quality control.
Analysis of ubiquitin-dependent pathways involved in complex assembly.
Synthesis of findings on the prevention, correction, and degradation of flawed complexes.

Main Results:

Ubiquitin-dependent pathways are central to quality control of protein complex composition.
These pathways actively monitor complex assembly to ensure fidelity.
Mechanisms exist to either correct assembly errors or target faulty complexes for degradation.

Conclusions:

Cellular quality control systems, particularly those involving ubiquitination, are essential for maintaining functional protein complexes.
Understanding these pathways provides insights into cellular homeostasis and disease mechanisms.
Further research into these complex quality control networks is warranted.