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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...

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...

Amplifying Signals via Enzymatic Cascade

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...

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...

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: Jul 7, 2026

Identification of Kinase-substrate Pairs Using High Throughput Screening

Identification of Kinase-substrate Pairs Using High Throughput Screening

Published on: August 29, 2015

Understanding and exploiting substrate recognition by protein kinases.

Benjamin E Turk¹

¹Department of Pharmacology, Yale University School of Medicine, P.O. Box 208066, 333 Cedar Street, New Haven, CT 06520, United States. ben.turk@yale.edu

Current Opinion in Chemical Biology

|February 20, 2008

Summary

This summary is machine-generated.

Understanding protein kinase substrate recognition is key to unlocking cellular functions and discovering new drug targets. This knowledge aids in developing tools for studying kinase pathways and phosphoproteomics.

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Last Updated: Jul 7, 2026

Identification of Kinase-substrate Pairs Using High Throughput Screening

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Published on: August 29, 2015

Identification of Novel CK2 Kinase Substrates Using a Versatile Biochemical Approach

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Published on: February 21, 2019

Characterization at the Molecular Level using Robust Biochemical Approaches of a New Kinase Protein

Characterization at the Molecular Level using Robust Biochemical Approaches of a New Kinase Protein

Published on: June 30, 2019

Area of Science:

Biochemistry
Molecular Biology
Cellular Signaling

Background:

Protein kinases regulate cellular processes universally and are crucial drug targets.
The functions of many human kinases remain unknown.
Substrate recognition mechanisms are vital for understanding kinase activity.

Purpose of the Study:

To explore kinase function and discover novel protein substrates.
To develop tools for studying kinase pathways, such as fluorescent biosensors.
To guide bioinformatics and phosphoproteomics for a global understanding of signaling networks.

Main Methods:

Exploiting commonalities in substrate recognition within the ATP nucleotide binding site.
Generating analog-specific mutants of protein kinases.
Analyzing differential interactions between kinases and protein substrates.

Main Results:

Identified conserved and distinct features of kinase-substrate interactions.
Demonstrated the utility of substrate recognition principles in identifying new substrates.
Showcased the application of these principles in creating research tools.

Conclusions:

Kinase substrate recognition is fundamental to cellular regulation and drug discovery.
Understanding these interactions enables the development of advanced tools for pathway analysis.
This knowledge significantly impacts global signaling pathway and network research.