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

12.0K
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...
12.0K
Protein Kinases and Phosphatases02:54

Protein Kinases and Phosphatases

3.3K
3.3K
Phosphorylation01:02

Phosphorylation

44.6K
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...
44.6K
Covalently Linked Protein Regulators02:04

Covalently Linked Protein Regulators

8.2K
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....
8.2K
Amplifying Signals via Enzymatic Cascade01:22

Amplifying Signals via Enzymatic Cascade

14.9K
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...
14.9K

You might also read

Related Articles

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

Sort by
Same author

High-throughput sequencing reveals that microRNA-based regulation, cell wall remodeling and phytohormone signaling orchestrate wheat seminal root development.

Planta·2026
Same author

Gallic Acid-Responsive microRNAs Reprogram Lignification During Drought Acclimation Process in Spearmint.

Plant biotechnology journal·2026
Same author

Rare uniparental lineages reveal external ancestries in the gene pool of the Italian linguistic enclave of Grecìa Salentina.

Scientific reports·2025
Same author

Structural and functional impact of the POLD1 Ser605del variant in MDPL syndrome: insights from protein-protein interactions.

Human genomics·2025
Same author

Transcriptome profiling of human dermal MDPL fibroblasts reveals a characteristic molecular signature providing insights into pathogenic mechanisms.

Journal of molecular medicine (Berlin, Germany)·2025
Same author

The Integrated Cellular and Molecular Landscape of Autoimmunity.

bioRxiv : the preprint server for biology·2025

Related Experiment Video

Updated: Apr 22, 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

25.2K

Exploiting holistic approaches to model specificity in protein phosphorylation.

Antonio Palmeri1, Fabrizio Ferrè1, Manuela Helmer-Citterich1

  • 1Department of Biology, Centre for Molecular Bioinformatics, University of Rome Tor Vergata Rome, Italy.

Frontiers in Genetics
|October 18, 2014
PubMed
Summary

Protein phosphorylation is crucial for cellular signaling but predicting it remains challenging. Integrating diverse contextual information beyond sequence and structure is key for accurate site annotation and kinase identification.

Keywords:
cellular signalingkinase-peptide specificitykinase-substrate specificityphosphorylation contextphosphorylation predictionsignaling networkssubstrate recruitment

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

1.8K
Oligopeptide Competition Assay for Phosphorylation Site Determination
09:16

Oligopeptide Competition Assay for Phosphorylation Site Determination

Published on: May 18, 2017

7.8K

Related Experiment Videos

Last Updated: Apr 22, 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

25.2K
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

1.8K
Oligopeptide Competition Assay for Phosphorylation Site Determination
09:16

Oligopeptide Competition Assay for Phosphorylation Site Determination

Published on: May 18, 2017

7.8K

Area of Science:

  • Biochemistry
  • Cell Biology
  • Systems Biology

Background:

  • Phosphate's unique role in cellular signaling, particularly in eukaryotes.
  • Protein phosphorylation is a fundamental post-translational modification studied across multiple biological contexts.
  • Despite advances, accurately inferring phosphorylation sites and identifying cognate kinases remain significant challenges in kinome biology.

Purpose of the Study:

  • To provide an overview of the various contexts influencing protein phosphorylation.
  • To discuss the impact of these contexts on phosphorylation site annotation.
  • To explore the prediction of kinase-substrate specificity.

Main Methods:

  • Review of existing literature on protein phosphorylation.
  • Analysis of sequence and structural contexts near phosphorylation sites.
  • Consideration of cellular environment and systems-level factors.

Main Results:

  • Near-site sequence and structure alone are insufficient for modeling in vivo phosphorylation rules.
  • Orthogonal information must be integrated for accurate phosphorylation site prediction.
  • Understanding diverse contexts is essential for advancing kinome biology.

Conclusions:

  • Accurate phosphorylation site inference requires integrating multiple layers of biological information.
  • Predicting kinase-substrate specificity benefits from a holistic contextual approach.
  • Further research integrating sequence, structure, and cellular context is needed to fully understand phosphorylation dynamics.