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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,...
Assembly of Signaling Complexes01:30

Assembly of Signaling Complexes

Multiprotein signaling complexes are formed in a dynamic process involving protein-protein interactions at the cytoplasmic domain of transmembrane receptors or enzymatic and non-enzymatic proteins associated with the receptor. These complexes ensure the activation and propagation of intracellular signals that regulate cell functions.
Interaction domains in cell signaling
Interaction domains recognize exposed features of their binding partners containing post-translationally modified sequences,...
Amplifying Signals via Enzymatic Cascade01:22

Amplifying Signals via Enzymatic Cascade

When a ligand binds to a cell-surface receptor, the receptor's intracellular domain changes shape, which may either activate its enzyme function or allow its binding to other molecules. The initial signal is amplified by most signal transduction pathways. This means that a single ligand molecule can activate multiple molecules of a downstream target. Proteins that relay a signal are most commonly phosphorylated at one or more sites, activating or inactivating the protein. Kinases catalyze the...
Proteomics01:33

Proteomics

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JUMPn: A Streamlined Application for Protein Co-Expression Clustering and Network Analysis in Proteomics
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Deciphering O‑GlcNAc-Dependent Signaling Via Integrated Proteomics and Phosphoproteomics.

Ci Wu1,2, Chunyan Hou1, Xinyue Wang2

  • 1Department of Oncology, Lombardi Comprehensive Cancer Center, Georgetown University Medical Center, Washington, District of Columbia 20007, United States.

ACS Omega
|June 22, 2026
PubMed
Summary

This study reveals extensive crosstalk between protein phosphorylation and O-linked N-acetylglucosamine (O-GlcNAcylation) modifications. We identified casein kinase 2 α (CK2α) as a key enzyme in regulating this glycosylation-dependent signaling.

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Quantitative Phosphoproteomics in Fatty Acid Stimulated Saccharomyces cerevisiae
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Quantitative Phosphoproteomics in Fatty Acid Stimulated Saccharomyces cerevisiae

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Quantitative Phosphoproteomics in Fatty Acid Stimulated Saccharomyces cerevisiae
15:41

Quantitative Phosphoproteomics in Fatty Acid Stimulated Saccharomyces cerevisiae

Published on: October 12, 2009

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Cellular Signaling

Background:

  • Post-translational modifications (PTMs) are vital for biological processes.
  • Phosphorylation and O-GlcNAcylation are dynamic PTMs crucial for cellular function and disease.
  • The crosstalk between these two modifications is increasingly recognized but poorly understood.

Purpose of the Study:

  • To investigate the crosstalk between phosphorylation and O-GlcNAcylation.
  • To elucidate the molecular mechanisms underlying this crosstalk in pancreatic cancer cells.

Main Methods:

  • Utilized the PANC-1 cell line.
  • Applied proteomic and phosphoproteomic analyses.
  • Used specific inhibitors OSMI-1 and Thiamet G to modulate O-GlcNAc cycling.
  • Conducted kinase inhibition experiments and in vitro kinase assays.

Main Results:

  • Significant alterations in 2289 phosphosites (OSMI-1) and 2201 phosphosites (TMG) were observed, indicating extensive crosstalk.
  • Widespread changes in kinome and phosphatome phosphorylation were detected after short-term inhibitor treatment.
  • Phosphorylation of O-GlcNAcase (OGA) at S364 was identified to be mediated by casein kinase 2 α (CK2α).

Conclusions:

  • This study uncovers significant crosstalk between phosphorylation and O-GlcNAcylation.
  • Demonstrates glycosylation-dependent cellular signaling pathways.
  • Identifies CK2α as a key regulator of OGA phosphorylation, providing insights into multilayered crosstalk mechanisms.