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Related Concept Videos

Phosphorylation01:02

Phosphorylation

53.4K
The addition or removal of phosphate groups from proteins is the most common chemical modification that regulates cellular processes. These modifications can affect the structure, activity, stability, and localization of proteins within cells as well as their interactions with other proteins.
During phosphorylation, protein kinases transfer the terminal phosphate group of ATP to specific amino acid side chains of substrate proteins. Serine, threonine, and tyrosine are the most commonly...
53.4K

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Related Experiment Video

Updated: Dec 29, 2025

Adenofection: A Method for Studying the Role of Molecular Chaperones in Cellular Morphodynamics by Depletion-Rescue Experiments
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Phosphorylation Time-Course Study of the Response during Adenovirus Type 2 Infection.

Alberto Valdés1,2, Hongxing Zhao3, Ulf Pettersson3

  • 1Section of Analytical Chemistry, Department of Chemistry-BMC, Uppsala University, Uppsala, 751 24, Sweden.

Proteomics
|February 8, 2020
PubMed
Summary

Viral infection alters cell signaling and energy production by changing protein phosphorylation. This study reveals key pathways and viral phosphorylation sites during adenovirus infection in human cells.

Keywords:
adenovirus type 2 infectionhuman foetal lung fibroblasts (IMR-90)mass spectrometryphosphoproteomicsstable isotope labeling with amino acids in cell culture (SILAC)

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Area of Science:

  • Cellular Biology
  • Virology
  • Biochemistry

Background:

  • Post-translational modifications (PTMs), particularly phosphorylation, are crucial for cellular signal transduction.
  • Understanding how viral infections impact host cell phosphoproteome dynamics is essential for deciphering virus-host interactions.

Purpose of the Study:

  • To investigate the temporal dynamics of phosphoproteome changes in IMR-90 cells following human adenovirus type 2 (Ad2) infection.
  • To identify host and viral protein phosphorylation sites and their associated signaling pathways.

Main Methods:

  • Time-course quantitative analysis using Stable Isotope Labeling by Amino acids in Cell culture (SILAC)-Mass Spectrometry (MS).
  • Enrichment of phosphopeptides using titanium dioxide (TiO2) particles.
  • Bioinformatic analysis for pathway clustering and kinase prediction.

Main Results:

  • 1552 phosphorylated sites were quantified, with significant alterations in Rho family GTPases, actin cytoskeleton, and cAMP-dependent protein kinase A signaling pathways early post-infection.
  • Changes in glycolysis-related phosphorylation sites suggest virus-induced Warburg effect activation for energy production.
  • 32 novel and 52 known phosphorylation sites on 17 Ad2 proteins were identified, predominantly late post-infection.
  • Kinase predictions indicated activation of PKA, CDK1/2, MAPK, and CKII.

Conclusions:

  • Ad2 infection profoundly impacts host cell signaling and metabolism through dynamic phosphoproteome alterations.
  • Phosphorylation plays a critical role in both host response and viral protein function during Ad2 infection.
  • Observed overlaps in kinase motifs between viral and host proteins highlight conserved phosphorylation mechanisms.