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Proc Natl Acad Sci U S A

Title:		"MP2C, a plant protein phosphatase 2C, functions as a negative regulator of mitogen-activated protein kinase pathways in yeast and plants"
Author(s):		Meskiene I; Bogre L; Glaser W; Balog J; Brandstotter M; Zwerger K; Ammerer G; Hirt H;
Address:		"Institute of Microbiology and Genetics, Vienna Biocenter, Dr. Bohrgasse 9, A-1030 Vienna, Austria"
Journal Title:		Proc Natl Acad Sci U S A
Year:		1998
Volume:		95
Issue:		4
Page Number:		1938 - 1943
DOI:		10.1073/pnas.95.4.1938
ISSN/ISBN:		0027-8424 (Print) 1091-6490 (Electronic) 0027-8424 (Linking)
Abstract:		"By interference of the yeast pheromone mitogen-activated protein kinase (MAPK) pathway with an alfalfa cDNA expression library, we have isolated the MP2C gene encoding a functional protein phosphatase type 2C. Epistasis analysis in yeast indicated that the molecular target of the MP2C phosphatase is Ste11, a MAPK kinase kinase that is a central regulator of the pheromone and osmosensing pathways. In plants, MP2C functions as a negative regulator of the stress-activated MAPK (SAMK) pathway that is activated by cold, drought, touch, and wounding. Although activation of the SAMK pathway occurs by a posttranslational mechanism, de novo transcription and translation of protein factor(s) are necessary for its inactivation. MP2C is likely to be this or one of these factors, because wound-induced activation of SAMK is followed by MP2C gene expression and recombinant glutathione S-transferase-MP2C is able to inactivate extracts containing wound-induced SAMK. Wound-induced MP2C expression is a transient event and correlates with the refractory period, i.e., the time when restimulation of the SAMK pathway is not possible by a second stimulation. These data suggest that MP2C is part of a negative feedback mechanism that is responsible for resetting the SAMK cascade in plants"
Keywords:		Amino Acid Sequence Arabidopsis Calcium-Calmodulin-Dependent Protein Kinases/*metabolism Fungal Proteins/metabolism/*physiology Humans MAP Kinase Kinase Kinases/*physiology Molecular Sequence Data Phosphoprotein Phosphatases/*metabolism Plant Proteins/met;
Notes:		"MedlineMeskiene, I Bogre, L Glaser, W Balog, J Brandstotter, M Zwerger, K Ammerer, G Hirt, H eng Research Support, Non-U.S. Gov't 1998/03/21 Proc Natl Acad Sci U S A. 1998 Feb 17; 95(4):1938-43. doi: 10.1073/pnas.95.4.1938"