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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 to...

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 to...

Covalently Linked Protein Regulators

Covalently Linked Protein Regulators

Proteins can undergo many types of post-translational modifications, often in response to changes in their environment. These modifications play an important role in the function and stability of these proteins. Covalently linked molecules include functional groups, such as methyl, acetyl, and phosphate groups, and also small proteins, such as ubiquitin. There are around 200 different types of covalent regulators that have been identified.
These groups modify specific amino acids in a protein.

Covalently Linked Protein Regulators

Covalently Linked Protein Regulators

Proteins can undergo many types of post-translational modifications, often in response to changes in their environment. These modifications play an important role in the function and stability of these proteins. Covalently linked molecules include functional groups, such as methyl, acetyl, and phosphate groups, and also small proteins, such as ubiquitin. There are around 200 different types of covalent regulators that have been identified.
These groups modify specific amino acids in a protein.

Protein Complex Assembly

Protein Complex Assembly

Proteins can form homomeric complexes with another unit of the same protein or heteromeric complexes with different types. Most protein complexes self-assemble spontaneously via ordered pathways, while some proteins need assembly factors that guide their proper assembly. Despite the crowded intracellular environment, proteins usually interact with their correct partners and form functional complexes.
Many viruses self-assemble into a fully functional unit using the infected host cell to...

Protein Complex Assembly

Protein Complex Assembly

Proteins can form homomeric complexes with another unit of the same protein or heteromeric complexes with different types. Most protein complexes self-assemble spontaneously via ordered pathways, while some proteins need assembly factors that guide their proper assembly. Despite the crowded intracellular environment, proteins usually interact with their correct partners and form functional complexes.
Many viruses self-assemble into a fully functional unit using the infected host cell to...

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Related Experiment Video

Updated: Jun 1, 2026

High-Resolution Complexome Profiling by Cryoslicing BN-MS Analysis

High-Resolution Complexome Profiling by Cryoslicing BN-MS Analysis

Published on: October 15, 2019

Analysis of the human endogenous coregulator complexome.

Anna Malovannaya¹, Rainer B Lanz, Sung Yun Jung

¹Department of Molecular and Cellular Biology, Baylor College of Medicine, Houston, TX 77030, USA.

|May 31, 2011

Summary

This summary is machine-generated.

This study maps human protein interaction networks using mass spectrometry, revealing novel protein associations and a tiered organizational structure of cellular proteomes. This provides a resource for understanding transcriptional regulation.

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Last Updated: Jun 1, 2026

High-Resolution Complexome Profiling by Cryoslicing BN-MS Analysis

High-Resolution Complexome Profiling by Cryoslicing BN-MS Analysis

Published on: October 15, 2019

Generation and Purification of Human INO80 Chromatin Remodeling Complexes and Subcomplexes

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Published on: October 23, 2014

Resolving Affinity Purified Protein Complexes by Blue Native PAGE and Protein Correlation Profiling

Resolving Affinity Purified Protein Complexes by Blue Native PAGE and Protein Correlation Profiling

Published on: April 1, 2017

Area of Science:

Proteomics
Systems Biology
Molecular Biology

Background:

Understanding endogenous protein-protein interactions is crucial for biological research.
Existing methods often fail to capture weak or transient interactions.

Purpose of the Study:

To comprehensively map endogenous human coregulator protein complex networks.
To identify novel protein associations and understand their organizational principles.

Main Methods:

Integrative mass spectrometry-based analysis of 3290 affinity purifications.
Preservation of weak protein interactions during complex isolation.
Utilizing high reciprocity in a large dataset.

Main Results:

Identification of numerous unreported protein associations, including a transcriptional network (ZMYND8, ZNF687, ZNF592).
Revealed a tiered interplay within networks, organizing the proteome into minimal endogenous modules (MEMOs), complex isoforms (uniCOREs), and complex-complex interaction networks (CCIs).

Conclusions:

The developed resource provides a conceptual organization of the cellular proteome.
Facilitates linking genomic studies with protein function for hypothesis generation and testing.