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Unsaturated fatty acids inhibit MP2C, a protein phosphatase 2C involved in the wound‐induced MAP kinase pathway regulation
Author(s) -
Baudouin Emmanuel,
Meskiene Irute,
Hirt Heribert
Publication year - 1999
Publication title -
the plant journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.058
H-Index - 269
eISSN - 1365-313X
pISSN - 0960-7412
DOI - 10.1046/j.1365-313x.1999.00608.x
Subject(s) - phosphatase , polyunsaturated fatty acid , biochemistry , kinase , protein kinase a , mapk/erk pathway , fatty acid , chemistry , threonine , serine , microbiology and biotechnology , biology , phosphorylation
Summary When mechanically injured, plants develop multiple defense systems including the activation of specific genes. These responses are triggered by a complex network of signalling events that include Ca 2+ fluxes, the production of free fatty acids from membrane lipids, as well as the activation of mitogen‐activated protein kinases (MAPK). In the present paper, we address the question of the regulation of the MAPK pathway by wound‐induced Ca 2+ and fatty acid signals. We report that MP2C, a serine/threonine protein phosphatase 2C from alfalfa involved in MAPK pathway inactivation, is inhibited specifically in vitro by long‐carbon‐chain polyunsaturated fatty acids, and α‐linolenic acid, the primary product of the octadecanoid pathway, was found to be the most potent inhibitor. Ca 2+ also inhibits MP2C, but only at high concentrations, and other divalent cations show similar inhibitory effect, making it unlikely that Ca 2+ is involved in the regulation of MP2C in vivo . Overall, our data suggest that cross‐talk between wound‐induced MAPK and octadecanoid pathways may occur at the level of protein phosphatase 2C and linolenic acid.