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Related Concept Videos

Protein Networks02:26

Protein Networks

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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.
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Protein glycosylation starts in the ER lumen and continues in the Golgi apparatus. Glycosyltransferases catalyze the addition of sugar molecules or glycosylation of proteins. Usually, these enzymes add sugars to the hydroxyl groups of selected serine or threonine residues to form O-linked glycans or the amino groups of asparagine residues to form N-linked glycans. Different positions on the same polypeptide chain can contain differently linked glycans.
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Related Experiment Video

Updated: Jul 24, 2025

Glycomics-Guided Glycoproteomics Facilitates Comprehensive Profiling of the Glycoproteome in Complex Tumor Microenvironments
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Functional glycoproteomics by integrated network assembly and partitioning.

Matthew E Griffin1,2, John W Thompson1,2, Yao Xiao1,2

  • 1Division of Chemistry and Chemical Engineering, California Institute of Technology, Pasadena, CA 91125, USA.

Biorxiv : the Preprint Server for Biology
|July 3, 2023
PubMed
Summary
This summary is machine-generated.

Researchers developed Networking of Interactors and Substrates (NISE) to study O-linked N-acetylglucosamine (O-GlcNAcylation) modifications across the proteome. This systems-level approach reveals how multiple O-GlcNAcylation events coordinate cellular functions.

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Area of Science:

  • Biochemistry and Molecular Biology
  • Systems Biology
  • Proteomics

Background:

  • O-linked N-acetylglucosamine (O-GlcNAcylation) is a widespread post-translational modification (PTM) crucial for cellular processes.
  • Previous studies focused on single O-GlcNAcylation sites, neglecting the coordinated roles of multiple modifications.

Approach:

  • Developed Networking of Interactors and Substrates (NISE), a novel systems-level approach.
  • Integrated affinity purification-mass spectrometry (AP-MS) and site-specific chemoproteomics.
  • Utilized network generation and unsupervised partitioning to link upstream regulators with downstream O-GlcNAcylation targets.

Key Points:

  • NISE enables rapid and comprehensive monitoring of O-GlcNAcylation across the entire proteome.
  • The approach successfully connected upstream regulators with downstream targets of O-GlcNAcylation.
  • Revealed conserved roles in epigenetic regulation and tissue-specific functions like synaptic morphology.

Conclusions:

  • NISE provides a data-rich framework for understanding the complex roles of O-GlcNAcylation.
  • This holistic approach is broadly applicable to studying other PTMs and their diverse functions.
  • Facilitates discovery of PTM roles in specific cell types and biological states.