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Related Concept Videos

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 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,...
Covalently Linked Protein Regulators02:04

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 Regulators02:04

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.
Nuclear Protein Sorting01:34

Nuclear Protein Sorting

Nuclear protein sorting is the selective trafficking of histones, polymerases, gene regulatory proteins into the nucleus and exporting RNAs and ribosomes to the cytosol. It is a tightly controlled process that regulates gene expression within a cell.
Proteins targeted to the nucleus carry nuclear localization signals or NLS recognized by import receptors in the cytosol. Similarly, proteins with nuclear export signals are recognized by export receptors. Import and export receptors are...
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...

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Related Experiment Video

Updated: May 14, 2026

Visualization of Protein-protein Interaction in Nuclear and Cytoplasmic Fractions by Co-immunoprecipitation and In Situ Proximity Ligation Assay
10:05

Visualization of Protein-protein Interaction in Nuclear and Cytoplasmic Fractions by Co-immunoprecipitation and In Situ Proximity Ligation Assay

Published on: January 16, 2017

USP7 at PML Nuclear Bodies: A Protein Interaction Network Perspective.

Sergey A Silonov1, Ekaterina S Vedeshkina1, Yakov I Mokin1

  • 1The Biomolecular Condensates and Membraneless Organelles Group, Institute of Cytology, Russian Academy of Sciences, 4 Tikhoretsky Ave., 194064 St. Petersburg, Russia.

International Journal of Molecular Sciences
|May 13, 2026
PubMed
Summary

Ubiquitin-specific protease 7 (USP7) interacts with PML nuclear bodies (PML-NBs), revealing shared roles in gene regulation and DNA repair. This study uncovers a novel cellular network linking USP7, PML-NBs, aging, and senescence.

Keywords:
LLPSPML nuclear bodiesUSP7intrinsically disordered proteinsintrinsically disordered regionsmembraneless organellesprotein–protein interactions

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Last Updated: May 14, 2026

Visualization of Protein-protein Interaction in Nuclear and Cytoplasmic Fractions by Co-immunoprecipitation and In Situ Proximity Ligation Assay
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Published on: January 16, 2017

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A Protein Preparation Method for the High-throughput Identification of Proteins Interacting with a Nuclear Cofactor Using LC-MS/MS Analysis
05:43

A Protein Preparation Method for the High-throughput Identification of Proteins Interacting with a Nuclear Cofactor Using LC-MS/MS Analysis

Published on: January 24, 2017

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Cell Biology

Background:

  • Ubiquitin-specific protease 7 (USP7) is a key deubiquitinating enzyme regulating cellular processes and is a therapeutic target.
  • USP7 partially localizes with PML nuclear bodies (PML-NBs), complex organelles involved in post-translational modifications, but their association is uncharacterized.

Purpose of the Study:

  • To investigate the molecular basis and functional significance of USP7's association with PML-NBs.
  • To identify shared proteins and functional contexts between USP7 and PML-NBs.

Main Methods:

  • Comparative interactome analysis of USP7 and PML.
  • Functional enrichment analysis using bioinformatics tools.
  • Network analysis of overlapping proteins with core PML-NB components.

Main Results:

  • A significant overlap of 166 proteins was identified between USP7 and PML interactomes.
  • Shared proteins are involved in transcriptional regulation, chromatin remodeling, DNA damage response, cellular senescence, and aging.
  • A dense network of 61 overlapping proteins with core PML-NB components was identified, characterized by liquid-liquid phase separation and intrinsic disorder.

Conclusions:

  • USP7 and PML-NBs operate within a common molecular context relevant to aging and senescence.
  • PML-NBs provide a crucial cellular environment for understanding USP7's functions and regulation.