Abstract
Mitogen-activated protein kinase (MAPK) modules play key roles in the transduction of environmental and developmental signals through phosphorylation of downstream signaling targets, including other kinases, enzymes, cytoskeletal proteins or transcription factors, in all eukaryotic cells. A typical MAPK cascade consists of at least three sequentially acting serine/threonine kinases, a MAP kinase kinase kinase (MAPKKK), a MAP kinase kinase (MAPKK) and finally, the MAP kinase (MAPK) itself, with each phosphorylating, and hence activating, the next kinase in the cascade. Recent advances in our understanding of hormone signaling pathways have led to the discovery of new regulatory systems. In particular, this research has revealed the emerging role of crosstalk between the protein components of various signaling pathways and the involvement of this crosstalk in multiple cellular processes. Here we provide an overview of current models and mechanisms of hormone signaling with a special emphasis on the role of MAPKs in cell signaling networks.One-sentence summary: In this review we highlight the mechanisms of crosstalk between MAPK cascades and plant hormone signaling pathways and summarize recent findings on MAPK regulation and function in various cellular processes.
Highlights
Mitogen-activated protein kinases (MAPKs) are one of the largest group of transferases, catalyzing phosphorylation of appropriate protein substrates on serine or threonine residues
To summarize, when the BR level is high, BR signal transduction through plasma-membrane receptor brassinosteroid-insensitive 1 (AtBRI1), BR-signaling kinase 1 (AtBSK1) and phosphatase AtBRI1 suppressor 1 (AtBSU1) inactivates the glycogen synthase kinase 3 (GSK3)-like kinase BR insensitive 2 (AtBIN2), making AtBES1 (BRI1-EMS-suppressor 1; called brassinazole-resistant 2 – BZR2)/AtBZR1, and the MAPK cascade active, which in turn leads to promotion of plant growth and inhibition of cell division and stomatal formation in cotyledons, respectively (Kim T.W. et al, 2012; Le et al, 2014; Zhang et al, 2014a)
(2015) demonstrated that the germination of mkkk18 knockout plant lines is inhibited in medium supplied with abscisic acid (ABA). These results suggest that the MAPKKK18-MKK3 module mediates ABA signaling during germination and root elongation
Summary
Mitogen-activated protein kinases (MAPKs) are one of the largest group of transferases, catalyzing phosphorylation of appropriate protein substrates on serine or threonine residues. To summarize, when the BR level is high, BR signal transduction through plasma-membrane receptor brassinosteroid-insensitive 1 (AtBRI1), BR-signaling kinase 1 (AtBSK1) and phosphatase AtBRI1 suppressor 1 (AtBSU1) inactivates the glycogen synthase kinase 3 (GSK3)-like kinase BR insensitive 2 (AtBIN2), making AtBES1 (BRI1-EMS-suppressor 1; called brassinazole-resistant 2 – BZR2)/AtBZR1, and the MAPK cascade (repressing AtSPCH) active, which in turn leads to promotion of plant growth and inhibition of cell division and stomatal formation in cotyledons, respectively (Kim T.W. et al, 2012; Le et al, 2014; Zhang et al, 2014a).
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