Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Concept Videos

Protein Kinases and Phosphatases02:54

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 Phosphatases02:54

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...
Phosphorylation01:02

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...
Phosphorylation01:02

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...
The Proteasome Structure01:17

The Proteasome Structure

The ubiquitin-proteasome pathway is a well-known mechanism utilized by eukaryotic cells to remove cytoplasmic proteins that are misfolded, damaged, or no longer needed. In this pathway, the protein that needs to be eliminated undergoes a process called ubiquitination, where a chain of ubiquitin molecules is attached to the 48th lysine residue of the target protein. This ubiquitin modification helps the proteasome distinguish between a target protein and a healthy protein.
The proteasome is an...
Amplifying Signals via Enzymatic Cascade01:22

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...

You might also read

Related Articles

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

Sort by
Same author

Overview of protein phosphorylation.

Current protocols in protein science·2008
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

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

Current protocols in molecular biology·2008

Related Experiment Video

Updated: Jul 7, 2026

Identification of Post-translational Modifications of Plant Protein Complexes
10:07

Identification of Post-translational Modifications of Plant Protein Complexes

Published on: February 22, 2014

Overview of protein phosphorylation.

B M Sefton1, S Shenolikar

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

Current Protocols in Molecular Biology
|February 12, 2008
PubMed
Summary

Protein phosphorylation is crucial for regulating protein function. This overview details phosphorylation sites, detection methods, and the roles of protein kinases and phosphatases.

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Cell Signaling

Background:

  • Protein phosphorylation is a key post-translational modification.
  • It plays a vital role in cellular signaling pathways and protein function regulation.
  • Dysregulation of phosphorylation is implicated in various diseases.

Purpose of the Study:

  • To provide a comprehensive overview of protein phosphorylation.
  • To discuss the significance and regulatory roles of phosphorylation in proteins.
  • To describe methods for detecting phosphoamino acids and key regulatory enzymes.

Main Methods:

  • Literature review and synthesis of existing research on protein phosphorylation.
  • Description of techniques for identifying phosphorylation sites.

More Related Videos

A Mass Spectrometry-Based Approach to Identify Phosphoprotein Phosphatases and their Interactors
10:17

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

Published on: April 29, 2022

Related Experiment Videos

Last Updated: Jul 7, 2026

Identification of Post-translational Modifications of Plant Protein Complexes
10:07

Identification of Post-translational Modifications of Plant Protein Complexes

Published on: February 22, 2014

A Mass Spectrometry-Based Approach to Identify Phosphoprotein Phosphatases and their Interactors
10:17

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

Published on: April 29, 2022

  • Explanation of methods for detecting phosphoamino acids (radiolabeled and unlabeled).

    • Main Results:

    • Phosphorylation significantly impacts protein function and cellular processes.
    • Specific sites of phosphorylation dictate protein activity and interactions.
    • Protein kinases and phosphatases are critical regulators of the phosphorylation state.

    Conclusions:

    • Protein phosphorylation is a fundamental regulatory mechanism in biology.
    • Understanding phosphorylation is essential for deciphering cellular functions and disease mechanisms.
    • Further research into kinases and phosphatases can yield therapeutic targets.