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Protein Kinases and Phosphatases

Protein Kinases and Phosphatases

Proteins undergo chemical modifications that trigger changes in the charge, structure, and conformation of the proteins. Phosphorylation, acetylation, glycosylation, nitrosylation, ubiquitination, lipidation, methylation, and proteolysis are various protein modifications that regulate protein activity. Such modifications are usually enzyme-driven.
Protein kinases
Many proteins in the cell are regulated by phosphorylation, the addition of a phosphate group. A family of enzymes called kinases...

Protein Kinases and Phosphatases

Protein Kinases and Phosphatases

Proteins undergo chemical modifications that trigger changes in the charge, structure, and conformation of the proteins. Phosphorylation, acetylation, glycosylation, nitrosylation, ubiquitination, lipidation, methylation, and proteolysis are various protein modifications that regulate protein activity. Such modifications are usually enzyme-driven.
Protein kinases
Many proteins in the cell are regulated by phosphorylation, the addition of a phosphate group. A family of enzymes called kinases...

cAMP-dependent Protein Kinase Pathways

cAMP-dependent Protein Kinase Pathways

Cyclic Adenosine Monophosphate (cAMP) is an essential second messenger that activates protein kinase A (PKA) and regulates various biological processes. A single epinephrine molecule binds to GPCR and activates several heterotrimeric G proteins, each stimulating multiple adenylyl cyclase, amplifying the signal, and synthesizing large numbers of cAMP molecules. Small changes in cAMP concentration affect PKA activity. The binding of four cAMP molecules induces a conformational change in PKA,...

Receptor Tyrosine Kinases

Receptor Tyrosine Kinases

Receptor tyrosine kinases or RTKs are membrane-bound receptors that phosphorylate specific tyrosine on protein substrates. RTKs regulate cellular growth, differentiation, survival, and migration. They contain an extracellular ligand binding domain, a transmembrane domain, and a cytosolic tail with intrinsic kinase activity. Several extracellular signaling molecules activate RTKs in one or more ways and relay the signal downstream. Ligands such as platelet-derived growth factor (PDGF) or...

Inhibitors of Viral Protein Synthesis

Inhibitors of Viral Protein Synthesis

Protein synthesis is indispensable for viral replication, as viruses lack the cellular machinery required for this process and must hijack the host's translational apparatus. In response, host cells deploy a critical innate immune defense involving interferons, specialized cytokines that play a central role in inhibiting viral propagation.Upon viral detection, infected cells release interferons that bind to receptors on adjacent uninfected cells, activating the JAK-STAT signaling pathway and...

Phosphorylation

Phosphorylation

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...

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Related Experiment Video

Updated: Jun 6, 2026

Assaying Protein Kinase Activity with Radiolabeled ATP

Assaying Protein Kinase Activity with Radiolabeled ATP

Published on: May 26, 2017

Viral serine/threonine protein kinases.

Thary Jacob¹, Céline Van den Broeke, Herman W Favoreel

¹Department of Virology, Parasitology, and Immunology, Faculty of Veterinary Medicine, Ghent University, Salisburylaan 133, 9820 Merelbeke, Belgium.

Journal of Virology

|November 19, 2010

Summary

Viral serine/threonine protein kinases are unique to large DNA viruses and crucial for virulence. Understanding these viral kinases offers potential as antiviral drug targets.

Area of Science:

Biochemistry
Virology
Molecular Biology

Background:

Phosphorylation is a key protein modification, essential for cellular functions and viral processes.
Large DNA viruses uniquely encode their own serine/threonine protein kinases.
These viral kinases significantly impact virus virulence, though their role in replication varies.

Purpose of the Study:

To review viral serine/threonine protein kinases found in large DNA viruses.
To discuss the functions and importance of these viral kinases.
To explore their potential as targets for antiviral drug development.

Main Methods:

Literature review of viral serine/threonine protein kinases.
Analysis of kinase function in viral replication and virulence.

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Analysis of Group IV Viral SSHHPS Using In Vitro and In Silico Methods

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Last Updated: Jun 6, 2026

Assaying Protein Kinase Activity with Radiolabeled ATP

Assaying Protein Kinase Activity with Radiolabeled ATP

Published on: May 26, 2017

Identification of Kinase-substrate Pairs Using High Throughput Screening

Identification of Kinase-substrate Pairs Using High Throughput Screening

Published on: August 29, 2015

Analysis of Group IV Viral SSHHPS Using In Vitro and In Silico Methods

Analysis of Group IV Viral SSHHPS Using In Vitro and In Silico Methods

Published on: December 21, 2019

Evaluation of kinase targets for antiviral therapies.

Main Results:

Identified diverse viral serine/threonine protein kinases across various large DNA viruses.
Confirmed the significant role of these kinases in viral virulence.
Highlighted variability in their importance for virus replication in cell culture.

Conclusions:

Viral serine/threonine protein kinases are critical virulence factors.
Targeting these unique viral enzymes presents a promising strategy for novel antiviral drug discovery.