Journal
PLANTA
Volume 223, Issue 4, Pages 708-713Publisher
SPRINGER
DOI: 10.1007/s00425-005-0126-7
Keywords
mitogen-activated protein kinase kinase kinase; mitogen-activated protein kinase kinase; mitogen-activated protein kinase; plant signal transduction; stress response; wounding
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We have constructed a series of deletion mutants of Arabidopsis MAPK kinase kinase (AtMEKK1) and obtained a constitutively active mutant, At-MEKK1 Delta 166, which lacks in self-inhibitory sequence of N-terminal 166 amino acids but still has substrate specificity. AtMEKK1 Delta 166 predominantly phosphorylates AtMEK1, an Arabidopsis MAPKK, but not its double mutant (AtMEKIT218A/S224E), suggesting that Thr-218 and Ser-224 are the phosphorylation sites. In wounded seedlings, AtMEKK1 was activated and phosphorylated its downstream AtMEK1. Furthermore, analysis using anti-AtMEKK1 and anti-AtMEK1 antibodies revealed that the interaction between the two proteins was signal dependent. These results suggest the presence of AtMEKK1-AtMEK1 pathway induced by wounding.
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