A novel receptor kinase involved in jasmonate-mediated wound and phytochrome signaling in maize coleoptiles
Related Experiment Video
Updated: Aug 18, 2026

Wide-Field, Real-Time Imaging of Local and Systemic Wound Signals in Arabidopsis
Published on: June 4, 2021
Guozhen He1, Yutaka Tarui, Moritoshi Iino
1Botanical Gardens, Graduate School of Science, Osaka City University, Kisaichi, Katano-shi, Osaka, 576-0004 Japan.
Abstract:
We identified a gene of maize (Zea mays L.) that is transcriptionally activated in decapitated coleoptiles. The amino acid sequence deduced from its full-length cDNA indicated that the identified gene encodes a novel leucine-rich-repeat receptor-like kinase. The gene is named WOUND-RESPONSIVE AND PHYTOCHROME-REGULATED KINASE1 (WPK1) based on the findings of this study. Database searches revealed two and three homologs of WPK1 for Arabidopsis thaliana and rice, respectively. These homologs occurred along with WPK1 on a phylogenetic branch separated from all reported receptor kinases. We uncovered that the level of WPK1 transcripts is up-regulated rapidly and transiently in response to wounding and red light. The response to red light was reversible by far-red light, indicating that it is mediated by phytochrome. Applied jasmonic acid activated the expression of WPK1, while ethylene, salicylic acid and abscisic acid had no such effect. These results strongly suggested that WPK1 is a component of the jasmonate-mediated signaling that participates in both wound-induced defensive and phytochrome-mediated photomorphogenetic responses. Furthermore, it was found that both wounding and red light up-regulate the transcript level of ZmAOS, a gene for the jasmonate biosynthesis enzyme allene oxide synthase, and that auxin inhibits the expression of WPK1 but not of ZmAOS. We present a model of jasmonate-mediated signaling to explain the results obtained.
Related Concept Videos
Cell Signaling in Plants
MAPK Signaling Cascades
The JAK-STAT Signaling Pathway
Photoreceptors and Plant Responses to Light
Calmodulin-dependent Signaling
The Ca2+-CaM complex does not have enzymatic activity by itself. Instead, the complex binds downstream target proteins, including membrane proteins or enzymes,...
cAMP-dependent Protein Kinase Pathways

