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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

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

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....

Amplifying Signals via Enzymatic Cascade

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...

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Related Experiment Video

Updated: Mar 28, 2026

Oligopeptide Competition Assay for Phosphorylation Site Determination

Oligopeptide Competition Assay for Phosphorylation Site Determination

Published on: May 18, 2017

Induced proximity for dephosphorylation.

Kwang-Su Park¹, Taeg Kyu Kwon²

¹College of Pharmacy, Keimyung University, Daegu 42601, South Korea.

Trends in Pharmacological Sciences

|March 26, 2026

Summary

Induced-proximity dephosphorylation precisely removes phosphate groups from target proteins. This targeted approach offers specific reprogramming of pathological phosphorylation for potential therapeutic applications.

Keywords:

dephosphorylation induced proximity phosphatase recruitment phosphorylation modulation

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Last Updated: Mar 28, 2026

Oligopeptide Competition Assay for Phosphorylation Site Determination

Oligopeptide Competition Assay for Phosphorylation Site Determination

Published on: May 18, 2017

Detection of Heterodimerization of Protein Isoforms Using an in Situ Proximity Ligation Assay

Detection of Heterodimerization of Protein Isoforms Using an in Situ Proximity Ligation Assay

Published on: October 20, 2018

Characterization at the Molecular Level using Robust Biochemical Approaches of a New Kinase Protein

Characterization at the Molecular Level using Robust Biochemical Approaches of a New Kinase Protein

Published on: June 30, 2019

Area of Science:

Biochemistry
Molecular Biology
Chemical Biology

Background:

Dephosphorylation is a critical cellular process regulating protein function.
Pathological phosphorylation contributes to various diseases.
Current dephosphorylation methods lack specificity.

Purpose of the Study:

To introduce induced-proximity dephosphorylation as a novel strategy.
To explain its mechanistic basis and advantages.
To discuss its therapeutic potential.

Main Methods:

Recruiting phosphatases to target proteins via induced proximity.
Utilizing reversible chemical or biological modifications.
Analyzing specificity and pathway engagement.

Main Results:

Demonstrated selective and reversible phosphate removal.
Achieved context-dependent reprogramming of phosphorylation.
Highlighted improved mechanistic and pathway specificity.

Conclusions:

Induced-proximity dephosphorylation offers precise control over protein phosphorylation.
This strategy holds significant promise for therapeutic interventions.
Further research is warranted to explore its full clinical potential.