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J Biol Chem. 2013 Jan 4;288(1):480-6. doi: 10.1074/jbc.M112.434654. Epub 2012 Nov 27.

Phosphorylation and stabilization of Arabidopsis MAP kinase phosphatase 1 in response to UV-B stress.

Author information

1
Department of Botany and Plant Biology, University of Geneva, Sciences III, CH-1211 Geneva 4, Switzerland.

Abstract

MAP kinase phosphatases (MKPs) are important regulators of the activation levels and kinetics of MAP kinases. This is crucial for a large number of physiological processes during development and growth, as well as interactions with the environment, including the response to ultraviolet-B (UV-B) stress. Arabidopsis MKP1 is a key regulator of MAP kinases MPK3 and MPK6 in response to UV-B stress. However, virtually nothing is presently known about the post-translational regulation of plant MKPs in vivo. Here, we provide evidence that MKP1 is a phosphoprotein in vivo and that MKP1 accumulates in response to UV-B stress. Moreover, proteasome inhibitor experiments suggest that MKP1 is constantly turned-over under non-stress conditions and that MKP1 is stabilized upon stress treatment. Stress-responsive phosphorylation and stabilization of MKP1 demonstrate the post-translational regulation of a plant MKP in vivo, adding an additional regulatory layer to MAP kinase signaling in plants.

PMID:
23188831
PMCID:
PMC3537045
DOI:
10.1074/jbc.M112.434654
[Indexed for MEDLINE]
Free PMC Article

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