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Related Concept Videos

Proteomics01:33

Proteomics

A proteome is the entire set of proteins that a cell type produces. We can study proteomes using the knowledge of genomes because genes code for mRNAs, and the mRNAs encode proteins. Although mRNA analysis is a step in the right direction, not all mRNAs are translated into proteins.
Proteomics is the study of proteomes' function. It involves the large-scale systematic study of the proteome to denote the protein complement expressed by a genome. Scientist Mark Wilkins coined the term proteomics...
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,...

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JUMPn: A Streamlined Application for Protein Co-Expression Clustering and Network Analysis in Proteomics
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Quantitative Proteomics Unveils Comprehensive Tissue-Specific VCP Interaction Networks in Mice.

Nannan Wang1,2, Yining Li2, Na Li2

  • 1Department of Laboratory Medicine, Nanjing Drum Tower Hospital, The Affiliated Hospital of Nanjing University Medical School, Medical School of Nanjing University, Nanjing, Jiangsu, 210008, China.

Scientific Data
|June 13, 2026
PubMed
Summary

Valosin-containing protein (VCP) interactomes were mapped across eight mouse tissues using affinity purification and mass spectrometry. This reveals novel VCP partners involved in metabolism and protein quality control, offering insights into VCP-related diseases.

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Area of Science:

  • Biochemistry and Molecular Biology
  • Cellular Biology
  • Genetics

Background:

  • Valosin-containing protein (VCP) is a AAA ATPase hexamer crucial for protein degradation pathways like ERAD.
  • VCP dysregulation is linked to multisystem proteinopathy, ALS, and cancer, but its tissue-specific functions are poorly understood.
  • Understanding VCP's diverse interactomes is key to elucidating its versatile biological roles.

Purpose of the Study:

  • To systematically profile the tissue-specific VCP interactome in vivo.
  • To identify novel VCP-binding partners across various mouse tissues.
  • To provide mechanistic insights into VCP's functional versatility and potential therapeutic targets.

Main Methods:

  • Generation of HA-N-tagged VCP knock-in mice using CRISPR/Cas9.
  • Affinity purification coupled with data-independent acquisition (DIA) mass spectrometry.
  • Systematic profiling of VCP interactors across eight mouse tissues and validation in HepG2 cells.

Main Results:

  • Identification of 923 high-confidence VCP-binding partners.
  • Discovery of established interactors (e.g., UBX2B, UFD1) and novel candidates.
  • Novel interactors implicated in energy metabolism (TCA cycle, oxidative phosphorylation) and protein quality control (proteasome, ERAD).
  • Validation of VCP interactions with hepatic proteins DAXX and PRKAG2.

Conclusions:

  • This study presents the first in vivo atlas of the VCP interaction network.
  • The findings offer mechanistic insights into tissue-specific VCP functions.
  • The identified interactome provides potential therapeutic avenues for VCP-related disorders.