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Plant MAP kinase phosphatases
González Besteiro, Marina A. Department of Botany and Plant Biology, University of Geneva, Geneva, Switzerland.
Ulm, Roman Department of Botany and Plant Biology, University of Geneva, Geneva, Switzerland.
- MAPK cascade principles
- Negative regulation of MAPKs by MAP kinase phosphatases
- Abiotic stress responses controlled by plant MKPs
- Biotic stress responses controlled by plant MKPs
- Developmental processes controlled by plant MKPs
- Regulation of MKPs
- Related Primary Literature
- Additional Reading
Cells are constantly monitoring their environment. If changes are perceived, a series of molecular events are triggered in order to adjust the cellular behavior according to the prevailing conditions. Within a cell, the information gathered by receptors is communicated, by a process called signal transduction, to molecules that directly control cellular functions. The addition or removal of a phosphate group (reversible phosphorylation) is a universal posttranslational protein modification that is used to pass on signals (Fig. 1a). It has often profound effects on the structure and thereby the properties of the target protein, including activity, localization, stability, and molecular interactions. Protein kinases phosphorylate their targets, and protein phosphatases remove phosphate groups. Mitogen-activated protein (MAP) kinase (MAPK) cascades constitute fundamental pillars of signal transduction mechanisms in all eukaryotes, including plants. They are activated in the presence of environmental stresses (for example, ultraviolet radiation, cold, heat, heavy metals, salinity, pathogens, and wounding) or in response to developmental cues (such as hormones and peptide signals). MAPK activity controls a broad range of cellular processes, including transcription, cell division, cell cycle, and metabolism. Importantly, MAPK activity needs to be tightly regulated because unbalanced MAPK signaling can lead to detrimental effects, including cell death.
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