Journal
TRENDS IN PLANT SCIENCE
Volume 20, Issue 1, Pages 49-55Publisher
ELSEVIER SCIENCE LONDON
DOI: 10.1016/j.tplants.2014.09.006
Keywords
MAPK; phosphorylation; stress signalling; peptide motifs
Categories
Funding
- Austrian Science Foundation (FWF Elise-Richter-Project) [V167-B09]
- Austrian Science Fund (FWF) [V167] Funding Source: Austrian Science Fund (FWF)
- Austrian Science Fund (FWF) [V 167] Funding Source: researchfish
Ask authors/readers for more resources
Mitogen-activated protein kinase (MARK) cascades are universal, evolutionary conserved signalling modules, which translate environmental information into appropriate responses via phosphorylation of their substrate proteins. In Arabidopsis, the MARK MPK3 regulates numerous cellular processes, including the adaptation to abiotic and biotic stresses. The molecular steps immediately downstream of MPK3 induction have, therefore, received abundant attention, and a respectable number of MPK3 targets are known by now. These proteins illustrate the substrate promiscuity of MPK3. They also are evidence for how manifold phosphorylation-regulated functions can be. This review presents the current knowledge about the function and regulation of MPK3-targeted proteins, takes a close look at their primary protein sequences, and proposes a model of how MPK3 recognises, binds, and phosphorylates its targets.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available