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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...
Proteomics01:33

Proteomics

A proteome is the entire set of proteins that a cell type produces. We can study proteomes using the knowledge of genomes because genes code for mRNAs, and the mRNAs encode proteins. Although mRNA analysis is a step in the right direction, not all mRNAs are translated into proteins.
Proteomics is the study of proteomes' function. It involves the large-scale systematic study of the proteome to denote the protein complement expressed by a genome. Scientist Mark Wilkins coined the term proteomics...
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...

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Related Experiment Video

Updated: Jun 9, 2026

Oligopeptide Competition Assay for Phosphorylation Site Determination
09:16

Oligopeptide Competition Assay for Phosphorylation Site Determination

Published on: May 18, 2017

Focus issue: systems analysis of protein phosphorylation.

Nancy R Gough, John F Foley

    Science Signaling
    |September 3, 2010
    PubMed
    Summary

    Protein kinases and phosphatases regulate cell signaling. Advanced phosphoproteomic analyses reveal cellular behavior, disease mechanisms, and the active roles of phosphatases in signal transduction.

    Area of Science:

    • Cellular Biology
    • Molecular Biology
    • Biochemistry

    Background:

    • Kinases and phosphatases are crucial regulators in cellular signaling pathways.
    • Phosphorylation is a central mechanism in biological regulation.

    Discussion:

    • Systems-level analyses and phosphoproteomics offer deep insights into phosphorylation sites and kinase specificity.
    • These analyses illuminate cellular behavior, environmental responses, and disease mechanisms.
    • Phosphatases actively participate in signal transduction, particularly in redox signaling, and are not just signal terminators.

    Key Insights:

    • Protein phosphorylation is a fundamental process in cell signaling.
    • Phosphoproteomic data provides a wealth of information on cellular functions and disease.

    More Related Videos

    Identification of Cyclin-dependent Kinase 1 Specific Phosphorylation Sites by an In Vitro Kinase Assay
    12:26

    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: Jun 9, 2026

    Oligopeptide Competition Assay for Phosphorylation Site Determination
    09:16

    Oligopeptide Competition Assay for Phosphorylation Site Determination

    Published on: May 18, 2017

    Identification of Cyclin-dependent Kinase 1 Specific Phosphorylation Sites by an In Vitro Kinase Assay
    12:26

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

    Published on: May 3, 2018

  • The dynamic roles of phosphatases in signaling are increasingly recognized.

    • Outlook:

    • Future research will continue to leverage phosphoproteomics for understanding complex biological systems.
    • Further exploration of phosphatase functions will uncover new therapeutic targets.
    • Integrating systems-level data will advance our comprehension of signaling networks.