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- Publisher
- Springer Journals
- Copyright
- Copyright © 1998 by Kluwer Academic Publishers
- Subject
- Life Sciences; Biochemistry, general; Plant Sciences; Plant Pathology
- ISSN
- 0167-4412
- eISSN
- 1573-5028
- DOI
- 10.1023/A:1006054607850
- Publisher site
- See Article on Publisher Site
Abstract
In the past few years, molecular cloning studies have revealed the primary structure of plant protein serine/threonine phosphatases. Two structurally distinct families, the PP1/PP2A family and the PP2C family, are present in plants as well as in animals. This review will focus on the plant PP2C family of protein phosphatases. Biochemical and molecular genetic studies in Arabidopsis have identified PP2C enzymes as key players in plant signal transduction processes. For instance, the ABI1/ABI2 PP2Cs are central components in abscisic acid (ABA) signal transduction. Arabidopsis mutants containing a single amino acid exchange in ABI1 or ABI2 show a reduced response to ABA. Another member of the PP2C family, kinase-associated protein phosphatase (KAPP), appears to be an important element in some receptor-like kinase (RLK) signalling pathways. Finally, an alfalfa PP2C acts as a negative regulator of a plant mitogen-activated protein kinase (MAPK) pathway. Thus, the plant PP2Cs function as regulators of various signal transduction pathways.
Journal
Plant Molecular Biology – Springer Journals
Published: Oct 6, 2004