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Plant Physiol, April 2000, Vol. 122, pp. 1301-1310
ATMPK4, an Arabidopsis Homolog of
Mitogen-Activated Protein Kinase, Is Activated in Vitro
by AtMEK1 through Threonine Phosphorylation1
Yafan
Huang,2
Hui
Li,
Rajeev
Gupta,
Peter C.
Morris,
Sheng
Luan, and
Joseph J.
Kieber3*
Department of Biological Sciences, Laboratory for Molecular
Biology, University of Illinois at Chicago, Chicago, Illinois 60607 (Y.H., H.L., J.J.K.); Department of Plant and Microbial Biology,
University of California, Berkeley, California 94720 (R.G., S.L.); and
Department of Biological Sciences, Heriot-Watt University,
Riccarton, Edinburgh, EH14 4AS, United Kingdom (P.C.M.)
The
modulation of mitogen-activated protein kinase (MAPK) activity
regulates many intracellular signaling processes. In animal and yeast
cells, MAP kinases are activated via phosphorylation by the
dual-specificity kinase MEK (MAP kinase kinase). Several plant homologs
of MEK and MAPK have been identified, but the biochemical events
underlying the activation of plant MAPKs remain unknown. We describe
the in vitro activation of an Arabidopsis homolog of MAP kinase,
ATMPK4. ATMPK4 was phosphorylated in vitro by an Arabidopsis MEK
homolog, AtMEK1. This phosphorylation occurred principally on threonine
(Thr) residues and resulted in elevated ATMPK4 kinase activity. A
second Arabidopsis MEK isoform, ATMAP2K , failed to phosphorylate
ATMPK4 in vitro. Tyr dephosphorylation by the Arabidopsis Tyr-specific
phosphatase AtPTP1 resulted in an almost complete loss of ATMPK4
activity. Immunoprecipitates of Arabidopsis extracts with anti-ATMPK4
antibodies displayed myelin basic protein kinase activity that was
sensitive to treatment with AtPTP1. These results demonstrate that a
plant MEK can phosphorylate and activate MAPK, and that Tyr
phosphorylation is critical for the catalytic activity of MAPK in
plants. Surprisingly, in contrast to the animal enzymes, AtMEK1 may not
be a dual-specificity kinase but, rather, the required Tyr
phosphorylation on ATMPK4 may result from autophosphorylation.
1
This work was supported by the National Science
Foundation (grant nos. MCB-9816914 and IBN-9416017 to J.J.K.).
2
Present address: Performance Plants, Inc.,
Bioscience Complex, Queen's University Kingston, Ontario, Canada K7L 3N6.
3
Present address: University of North Carolina,
Biology Department, CB#3280, Chapel Hill, NC 27599-3280.
*
Corresponding author; e-mail jkieber{at}unc.edu; fax 919-962-1625.
© 2000 American Society of Plant Physiologists
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