Protein phosphatases 1 and 2A and their naturally occurring inhibitors: current topics in smooth muscle physiology and chemical biology

• Published in: The journal of physiological sciences Vol. 68; no. 1; pp. 1 - 17
• Main Authors: Takai, Akira, Eto, Masumi, Hirano, Katsuya, Takeya, Kosuke, Wakimoto, Toshiyuki, Watanabe, Masaru
• Format: Journal Article
• Language: English
• Published: Japan Springer 01.01.2018; BioMed Central; Springer Japan
• Subjects: Animals; Calyculin A; Cellular signal transduction; Enzyme Inhibitors - pharmacology; Humans; Marine microorganisms; Muscle, Smooth - drug effects; Muscle, Smooth - metabolism; Phosphatase; Phosphatases; Physiological aspects; Physiology; Protein phosphatase; Protein Phosphatase 1 - antagonists & inhibitors; Protein Phosphatase 1 - metabolism; Protein Phosphatase 2 - antagonists & inhibitors; Protein Phosphatase 2 - metabolism; Protein phosphatase inhibitors; Proteins; Review; Serine; Smooth muscle; Threonine; Signal transduction; Phosphatase inhibitors; Smooth muscle; Protein phosphorylation; Protein phosphatase 1; Protein phosphatase 2A
• ISSN: 1880-6546; 1880-6562
• DOI: 10.1007/s12576-017-0556-6

Protein phosphatases 1 and 2A (PP1 and PP2A) are the most ubiquitous and abundant serine/threonine phosphatases in eukaryotic cells. They play fundamental roles in the regulation of various cellular functions. This review focuses on recent advances in the functional studies of these enzymes in the field of smooth muscle physiology. Many naturally occurring protein phosphatase inhibitors with different relative PP1/PP2A affinities have been discovered and are widely used as powerful research tools. Current topics in the chemical biology of PP1/PP2A inhibitors are introduced and discussed, highlighting the identification of the gene cluster responsible for the biosynthesis of calyculin A in a symbiont microorganism of a marine sponge.