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Scientific article
English

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

Published inThe Journal of biological chemistry, vol. 288, no. 1, p. 480-486
Publication date2013
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.

Keywords
  • Amino Acid Sequence
  • Arabidopsis/enzymology
  • Arabidopsis Proteins/genetics/metabolism
  • Dual Specificity Phosphatase 1/chemistry/metabolism
  • Gene Expression Regulation
  • Plant/radiation effects
  • MAP Kinase Signaling System
  • Mitogen-Activated Protein Kinases/genetics/metabolism
  • Molecular Sequence Data
  • Mutagenesis
  • Site-Directed
  • Phenotype
  • Phosphorylation
  • Plant Proteins/metabolism
  • Plants
  • Genetically Modified
  • Protein Processing
  • Post-Translational
  • Signal Transduction
  • Ultraviolet Rays
Citation (ISO format)
GONZALEZ BESTEIRO, Marina, ULM, Roman. Phosphorylation and stabilization of Arabidopsis MAP kinase phosphatase 1 in response to UV-B stress. In: The Journal of biological chemistry, 2013, vol. 288, n° 1, p. 480–486. doi: 10.1074/jbc.M112.434654
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Article (Published version)
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Identifiers
ISSN of the journal0021-9258
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