Search research articles

ABOUT JoVE

Overview Leadership Blog JoVE Help Center

AUTHORS

Publishing Process Editorial Board Scope & Policies Peer Review FAQ Submit

LIBRARIANS

Testimonials Subscriptions Access Resources Library Advisory Board FAQ

RESEARCH

JoVE Journal Methods Collections JoVE Encyclopedia of Experiments Archive

EDUCATION

JoVE Core JoVE Business JoVE Science Education JoVE Lab Manual Faculty Resource Center Faculty Site

Terms & Conditions of Use

Related Concept Videos

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...

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...

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by

Same author

mPFC Synaptosome Proteomics Reveals Novel Pathways and Muscarinic Receptor Changes in a Learned Helplessness Mouse Model.

eNeuro·2026

Same author

mPFC Synaptosome Proteomics Reveals Novel Pathways and Muscarinic Receptor Changes in a Learned Helplessness Mouse Model.

bioRxiv : the preprint server for biology·2026

Same author

Basic Science and Pathogenesis.

Alzheimer's & dementia : the journal of the Alzheimer's Association·2025

Same author

Ryanodine receptor 2-mediated calcium leak is associated with increased glyoxalase I in the aging brain.

JCI insight·2025

Same author

Myelin-axon interface vulnerability in Alzheimer's disease revealed by subcellular proteomics and imaging of human and mouse brain.

Nature neuroscience·2025

Same author

A compilation of reported alterations in the cerebrospinal fluid proteome in Alzheimer's disease.

Brain communications·2025

Search research articles

Related Experiment Video

Updated: Jun 8, 2026

Recombinant α- β- and γ-Synucleins Stimulate Protein Phosphatase 2A Catalytic Subunit Activity in Cell Free Assays

Recombinant α- β- and γ-Synucleins Stimulate Protein Phosphatase 2A Catalytic Subunit Activity in Cell Free Assays

Published on: August 13, 2017

Serine/threonine protein phosphatase assays.

Thomas McAvoy¹, Angus C Nairn

¹The Rockefeller University, New York, New York, USA.

Current Protocols in Molecular Biology

|October 5, 2010

Summary

This study details methods for assaying serine/threonine protein phosphatases using colorimetric or radiometric techniques. These protocols are versatile, applicable to various sample types and adaptable for high-throughput screening or detailed kinetic analysis.

Area of Science:

Biochemistry
Molecular Biology
Enzymology

Background:

Serine/threonine protein phosphatases are crucial enzymes involved in cellular signaling.
Accurate measurement of their activity is essential for understanding biological processes.
Existing assay methods may have limitations in scope or throughput.

Purpose of the Study:

To present and discuss established methods for assaying serine/threonine protein phosphatase activity.
To provide guidance on selecting and applying appropriate assay protocols.
To enable both high-throughput screening and detailed kinetic analysis of these enzymes.

Main Methods:

Detailed description of three commonly employed assay protocols.
Utilization of both colorimetric and radiometric assay formats.

More Related Videos

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

Oligopeptide Competition Assay for Phosphorylation Site Determination

Oligopeptide Competition Assay for Phosphorylation Site Determination

Published on: May 18, 2017

Related Experiment Videos

Last Updated: Jun 8, 2026

Recombinant α- β- and γ-Synucleins Stimulate Protein Phosphatase 2A Catalytic Subunit Activity in Cell Free Assays

Recombinant α- β- and γ-Synucleins Stimulate Protein Phosphatase 2A Catalytic Subunit Activity in Cell Free Assays

Published on: August 13, 2017

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

Oligopeptide Competition Assay for Phosphorylation Site Determination

Oligopeptide Competition Assay for Phosphorylation Site Determination

Published on: May 18, 2017

Adaptability of methods for diverse biological preparations, from crude lysates to purified proteins.

Main Results:

Successful application of presented protocols across various sample matrices.
Demonstration of assay utility in both comparative activity assessments and kinetic data generation.
Versatility confirmed for different experimental objectives and throughput requirements.

Conclusions:

The discussed methods provide robust and flexible approaches for serine/threonine protein phosphatase activity assays.
These assays are suitable for a wide range of research applications, from basic research to drug discovery.
The protocols facilitate efficient and accurate characterization of enzyme function in various contexts.