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...

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...

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...

Overview of Protein Metabolism

Overview of Protein Metabolism

Proteins are broken down into amino acids during digestion. Unlike fats and carbohydrates, which are stored for later use, proteins are not. Instead, amino acids are either used to produce ATP through oxidation or contribute to the creation of new proteins for the growth and repair of the body. Any surplus amino acids from the diet are converted into glucose or triglycerides rather than excreted.
Amino acids play various roles in the body once they are absorbed into cells. They are restructured...

Covalently Linked Protein Regulators

Covalently Linked Protein Regulators

Proteins can undergo many types of post-translational modifications, often in response to changes in their environment. These modifications play an important role in the function and stability of these proteins. Covalently linked molecules include functional groups, such as methyl, acetyl, and phosphate groups, and also small proteins, such as ubiquitin. There are around 200 different types of covalent regulators that have been identified.
These groups modify specific amino acids in a protein.

You might also read

Related Articles

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

Sort by

Same author

Labeling cultured cells with 32P(i) and preparing cell lysates for immunoprecipitation.

Current protocols in protein science·2008

Same author

Phosphoamino acid analysis.

Current protocols in protein science·2008

Same author

Detection of phosphorylation by immunological techniques.

Current protocols in protein science·2008

Same author

Detection of phosphorylation by enzymatic techniques.

Current protocols in protein science·2008

Same author

Overview of protein phosphorylation.

Current protocols in molecular biology·2008

Same author

Labeling cultured cells with 32P(i) and preparing cell lysates for immunoprecipitation.

Current protocols in molecular biology·2008

Same journal

De Novo Protein Design Using the Blueprint Builder in Rosetta.

Current protocols in protein science·2020

Same journal

Methods for Expression of Recombinant Proteins Using a Pichia pastoris Cell-Free System.

Current protocols in protein science·2020

Same journal

Histone Purification Combined with High-Resolution Mass Spectrometry to Examine Histone Post-Translational Modifications and Histone Variants in Caenorhabditis elegans.

Current protocols in protein science·2020

Same journal

A Rapid and Facile Purification Method for Glycan-Binding Proteins and Glycoproteins.

Current protocols in protein science·2020

Same journal

Synthesis of Recombinant Human Hemoglobin With NH<sub>2</sub> -Terminal Acetylation in Escherichia coli.

Current protocols in protein science·2020

Same journal

A Fluorescence-Based Assay to Monitor SUMOylation in Real-Time.

Current protocols in protein science·2020

See all related articles

Search research articles

Related Experiment Video

Updated: Jul 5, 2026

A Mass Spectrometry-Based Approach to Identify Phosphoprotein Phosphatases and their Interactors

A Mass Spectrometry-Based Approach to Identify Phosphoprotein Phosphatases and their Interactors

Published on: April 29, 2022

Overview of protein phosphorylation.

B M Sefton¹, S Shenolikar

¹The Salk Institute, San Diego, California, USA.

Current Protocols in Protein Science

|April 23, 2008

Summary

This summary is machine-generated.

This overview details protein phosphorylation research, explaining labeling studies and the roles of kinases and phosphatases. It covers methods for detecting phosphoamino acids, crucial for understanding cellular signaling.

More Related Videos

Identification of Post-translational Modifications of Plant Protein Complexes

Identification of Post-translational Modifications of Plant Protein Complexes

Published on: February 22, 2014

Related Experiment Videos

Last Updated: Jul 5, 2026

A Mass Spectrometry-Based Approach to Identify Phosphoprotein Phosphatases and their Interactors

A Mass Spectrometry-Based Approach to Identify Phosphoprotein Phosphatases and their Interactors

Published on: April 29, 2022

Identification of Post-translational Modifications of Plant Protein Complexes

Identification of Post-translational Modifications of Plant Protein Complexes

Published on: February 22, 2014

Area of Science:

Biochemistry
Molecular Biology
Cell Signaling

Background:

Protein phosphorylation is a fundamental post-translational modification regulating numerous cellular processes.
Understanding the dynamics of phosphorylation is key to deciphering cell signaling pathways.
Research in this area has evolved significantly, necessitating updated overviews.

Purpose of the Study:

To provide a historical perspective on protein phosphorylation research.
To elucidate the methodologies and rationale behind protein phosphorylation labeling studies.
To describe the various sites of protein phosphorylation and the enzymes involved.

Main Methods:

Review of historical and current literature on protein phosphorylation.
Description of enzymatic roles of kinases and phosphatases in regulating phosphorylation.
Overview of detection techniques for phosphoamino acids, including electrophoresis, gel-shift assays, and antibody-based methods.

Main Results:

Detailed explanation of the history and importance of protein phosphorylation studies.
Identification of key regulatory enzymes (kinases and phosphatases) and their functions.
Comprehensive description of methods used to detect and analyze protein phosphorylation.

Conclusions:

Protein phosphorylation is a critical regulatory mechanism in cell biology.
Labeling studies and advanced detection methods are essential for its investigation.
This overview serves as a foundational resource for researchers in the field.