期刊
JOURNAL OF PHYSIOLOGICAL SCIENCES
卷 68, 期 1, 页码 1-17出版社
SPRINGER JAPAN KK
DOI: 10.1007/s12576-017-0556-6
关键词
Protein phosphorylation; Protein phosphatase 1; Protein phosphatase 2A; Smooth muscle; Phosphatase inhibitors; Signal transduction
类别
资金
- Grants-in-Aid for Scientific Research [16H06448, 16K09518] Funding Source: KAKEN
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.
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