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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

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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.
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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.
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Related Experiment Video

Updated: Jun 28, 2026

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

Structural basis of protein kinase C isoform function.

Susan F Steinberg¹

¹Department of Pharmacology, College of Physicians and Surgeons, Columbia University, New York, New York 10032, USA. sfs1@columbia.edu

Physiological Reviews

|October 17, 2008

Summary

This summary is machine-generated.

Protein kinase C (PKC) isoforms are lipid-activated enzymes with diverse cellular roles. Understanding their unique structural features and regulation is key to developing targeted therapies for PKC-related diseases.

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

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Identification of Kinase-substrate Pairs Using High Throughput Screening

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Identification of Novel CK2 Kinase Substrates Using a Versatile Biochemical Approach

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Published on: February 21, 2019

Area of Science:

Biochemistry
Cell Biology
Molecular Pharmacology

Background:

Protein kinase C (PKC) isoforms are lipid-activated enzymes crucial for numerous cellular functions.
PKCs possess modular structures with regulatory and catalytic domains, responding to lipid cofactors and calcium.
Despite shared characteristics, individual PKC isoforms exhibit distinct functions due to specific localization, interactions, and modifications.

Purpose of the Study:

To review the structural basis for differential lipid cofactor responsiveness among PKC isoforms.
To discuss regulatory phosphorylations controlling PKC maturation, activation, and signaling.
To explore intra- and intermolecular interactions governing PKC activation and subcellular targeting.

Main Methods:

Literature review focusing on structural biology and molecular mechanisms.
Analysis of studies on PKC isoform-specific regulation and function.
Synthesis of data on posttranslational modifications and protein-protein interactions.

Main Results:

PKC isoforms display unique structural features influencing their interaction with lipid cofactors.
Regulatory phosphorylations are critical for PKC enzyme lifecycle, from maturation to downregulation.
Isoform-specific interactions and subcellular localization dictate distinct PKC signaling pathways.

Conclusions:

Understanding the molecular underpinnings of PKC isoform specificity is essential.
Targeted modulation of PKC isoform activity holds therapeutic potential.
Developing isoform-specific activators or inhibitors can lead to effective treatments for diseases involving aberrant PKC signaling.