Related Experiment Video
Updated: Jul 9, 2026
11:13
Identification of Kinase-substrate Pairs Using High Throughput Screening
Published on: August 29, 2015
Interaction networks explain holoenzyme allostery in Protein Kinase A
Colin L Welsh1, Abigail E Conklin1, Lalima K Madan1,2
1Department of Cell and Molecular Pharmacology & Experimental Therapeutics, College of Medicine, Medical University of South Carolina, Charleston, SC-29425, USA.
Kinases and Phosphatases
|July 8, 2026
Summary
Protein Kinase A (PKA) is key to cell signaling via phosphorylation. This review details PKA
Area of Science:
- Biochemistry and Molecular Biology
- Cellular Signaling Pathways
Background:
- Protein Kinase A (PKA) is a crucial mediator of cAMP-dependent cellular signaling.
- Its catalytic subunit was the first protein kinase catalytic domain to be structurally elucidated.
- PKA holoenzyme structure and function are central to understanding kinase mechanics.
Purpose of the Study:
- To provide an updated overview of Protein Kinase A (PKA) structure and function.
- To describe the structures of PKA's catalytic and regulatory subunits.
- To cover the structure, activation, and allosteric mechanisms of PKA holoenzymes.
Main Methods:
- Review of existing literature on PKA structure and function.
- Analysis of structural data for PKA catalytic and regulatory subunits.
- Examination of allosteric mechanisms governing PKA holoenzyme activation.
Main Results:
- Detailed structural insights into PKA catalytic and regulatory subunits.
- Elucidation of the PKA holoenzyme's role in cAMP-dependent signaling.
- Understanding of specialized protein allostery in PKA activation.
Conclusions:
- PKA structure and dynamics significantly advance kinase mechanics understanding.
- PKA holoenzymes highlight the importance of protein binding interfaces and dynamics in allostery.
- This review offers a comprehensive update on PKA structure, function, and allosteric regulation.
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