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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...

Yeast Signaling

Yeast Signaling

Yeasts are single-celled organisms, but unlike bacteria, they are eukaryotes (cells with a nucleus). Cell signaling in yeast is similar to signaling in other eukaryotic cells. A ligand, such as a protein or a small molecule released from a yeast cell, attaches to a receptor on the cell surface. The binding stimulates second-messenger kinases to activate or inactivate transcription factors that further regulate gene expression. Many of the yeast intracellular signaling cascades have similar...

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.

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Related Experiment Video

Updated: May 27, 2026

Identification of Kinase-substrate Pairs Using High Throughput Screening

Identification of Kinase-substrate Pairs Using High Throughput Screening

Published on: August 29, 2015

Dissecting phosphorylation networks: lessons learned from yeast.

Janine Mok¹, Xiaowei Zhu, Michael Snyder

¹Stanford Genome Technology Center, Department of Biochemistry, Stanford School of Medicine, 855 S. California Avenue, Palo Alto, CA 94304, USA.

Expert Review of Proteomics

|November 18, 2011

Summary

This summary is machine-generated.

Researchers reviewed technologies for mapping protein phosphorylation in yeast. These methods illuminate kinase signaling pathways and eukaryotic proteomic networks, aiding disease research.

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Last Updated: May 27, 2026

Identification of Kinase-substrate Pairs Using High Throughput Screening

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Quantitative Phosphoproteomics in Fatty Acid Stimulated Saccharomyces cerevisiae

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Enzymatic Modification and Flow Cytometry Assessment of Yeast Surface Displayed Proteins

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Area of Science:

Biochemistry
Molecular Biology
Cell Biology

Background:

Protein phosphorylation is a critical post-translational modification in eukaryotes.
Dysregulated phosphorylation is linked to various human diseases.
The budding yeast Saccharomyces cerevisiae is a valuable model for studying kinases.

Purpose of the Study:

To review emerging technologies for global phosphorylation mapping in yeast.
To discuss the insights gained from these mapping efforts into kinase signaling and proteomic networks.

Main Methods:

Review of recent technological advancements in yeast phosphoproteomics.
Analysis of data generated by global phosphorylation mapping studies.

Main Results:

Emerging technologies enable comprehensive mapping of phosphorylation sites in yeast.
Phosphorylation mapping provides insights into kinase function and signaling networks.
These studies enhance understanding of eukaryotic proteomic networks.

Conclusions:

Global phosphorylation mapping in yeast is a powerful approach.
Understanding yeast phosphorylation networks aids in deciphering human disease mechanisms.
Technological advancements continue to drive discoveries in this field.