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

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...

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...

Protein Networks

Protein Networks

An organism can have thousands of different proteins, and these proteins must cooperate to ensure the health of an organism. Proteins bind to other proteins and form complexes to carry out their functions. Many proteins interact with multiple other proteins creating a complex network of protein interactions.
These interactions can be represented through maps depicting protein-protein interaction networks, represented as nodes and edges. Nodes are circles that are representative of a protein,...

Protein Networks

Protein Networks

An organism can have thousands of different proteins, and these proteins must cooperate to ensure the health of an organism. Proteins bind to other proteins and form complexes to carry out their functions. Many proteins interact with multiple other proteins creating a complex network of protein interactions.
These interactions can be represented through maps depicting protein-protein interaction networks, represented as nodes and edges. Nodes are circles that are representative of a protein,...

You might also read

Related Articles

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

Sort by

Same author

PP2A catalytic subunit alpha is critically required for CD8<sup>+</sup> T-cell homeostasis and antibacterial responses.

European journal of immunology·2024

Same author

Diversity of post-translational modifications and cell signaling revealed by single cell and single organelle mass spectrometry.

Communications biology·2024

Same author

Culture-Free Whole Genome Sequencing of <i>Mycobacterium tuberculosis</i> Using Ligand-Mediated Bead Enrichment Method.

Open forum infectious diseases·2024

Same author

Multicolumn Nanoflow Liquid Chromatography with Accelerated Offline Gradient Generation for Robust and Sensitive Single-Cell Proteome Profiling.

Analytical chemistry·2024

Same author

Metabolome-wide association identifies altered metabolites and metabolic pathways in the serum of patients with cholangiocarcinoma.

JHEP reports : innovation in hepatology·2024

Same author

Dysregulated Cerebrospinal Fluid Proteome of Spinocerebellar Ataxia Type 2 and its Clinical Implications.

Movement disorders : official journal of the Movement Disorder Society·2024

Search research articles

Related Experiment Video

Updated: May 12, 2026

Identification of Kinase-substrate Pairs Using High Throughput Screening

Identification of Kinase-substrate Pairs Using High Throughput Screening

Published on: August 29, 2015

Construction of human activity-based phosphorylation networks.

Robert H Newman¹, Jianfei Hu, Hee-Sool Rho

¹Department of Pharmacology and Molecular Sciences, Johns Hopkins School of Medicine, Baltimore, MD 21205, USA.

Molecular Systems Biology

|April 4, 2013

Summary

Researchers mapped human phosphorylation networks by identifying kinase-substrate relationships (KSRs) using functional protein microarrays. This study reveals new insights into cellular signaling pathways and kinase functions.

More Related Videos

Identification of Cyclin-dependent Kinase 1 Specific Phosphorylation Sites by an In Vitro Kinase Assay

Identification of Cyclin-dependent Kinase 1 Specific Phosphorylation Sites by an In Vitro Kinase Assay

Published on: May 3, 2018

Related Experiment Videos

Last Updated: May 12, 2026

Identification of Kinase-substrate Pairs Using High Throughput Screening

Identification of Kinase-substrate Pairs Using High Throughput Screening

Published on: August 29, 2015

Identification of Cyclin-dependent Kinase 1 Specific Phosphorylation Sites by an In Vitro Kinase Assay

Identification of Cyclin-dependent Kinase 1 Specific Phosphorylation Sites by an In Vitro Kinase Assay

Published on: May 3, 2018

Area of Science:

Cellular signaling
Molecular biology
Proteomics

Background:

Human phosphorylation networks are largely unexplored, limiting understanding of cellular signaling.
Identifying upstream kinases for in vivo phosphorylated residues requires biochemical kinase-substrate relationship (KSR) analysis.

Purpose of the Study:

To systematically explore human phosphorylation networks.
To experimentally identify kinase substrates and construct a high-resolution map of phosphorylation networks.

Main Methods:

Developed the CEASAR strategy combining functional protein microarrays and bioinformatics.
Experimentally identified substrates for 289 kinases, yielding 3656 high-quality KSRs.
Integrated KSRs and in vivo phosphorylation sites to map kinase-mediated signaling.

Main Results:

Constructed a high-resolution map connecting 230 kinases to 2591 in vivo phosphorylation sites in 652 substrates.
Generated consensus phosphorylation motifs for identified kinases.
Discovered a novel role for Protein Kinase A (PKA) downstream of Bruton's tyrosine kinase (Btk) in B-cell receptor signaling.

Conclusions:

Provides global insights into kinase-mediated signaling pathways.
Advances the understanding of human cellular signaling processes.
Establishes a valuable dataset for future research in cell signaling and disease.