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Negative control of BAK 1 by protein phosphatase 2A during plant innate immunity
Author(s) -
Segonzac Cécile,
Macho Alberto P,
Sanmartín Maite,
Ntoukakis Vardis,
SánchezSerrano José Juan,
Zipfel Cyril
Publication year - 2014
Publication title -
the embo journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 7.484
H-Index - 392
eISSN - 1460-2075
pISSN - 0261-4189
DOI - 10.15252/embj.201488698
Subject(s) - innate immune system , biology , phosphatase , immunity , microbiology and biotechnology , immune system , phosphorylation , pattern recognition receptor , receptor , pathogen associated molecular pattern , regulator , kinase , plant immunity , immunology , biochemistry , arabidopsis , gene , mutant
Recognition of pathogen‐associated molecular patterns ( PAMP s) by surface‐localized pattern‐recognition receptors ( PRR s) activates plant innate immunity, mainly through activation of numerous protein kinases. Appropriate induction of immune responses must be tightly regulated, as many of the kinases involved have an intrinsic high activity and are also regulated by other external and endogenous stimuli. Previous evidences suggest that PAMP ‐triggered immunity ( PTI ) is under constant negative regulation by protein phosphatases but the underlying molecular mechanisms remain unknown. Here, we show that protein Ser/Thr phosphatase type 2A ( PP 2A) controls the activation of PRR complexes by modulating the phosphostatus of the co‐receptor and positive regulator BAK 1. A potential PP 2A holoenzyme composed of the subunits A1, C4, and B’η/ζ inhibits immune responses triggered by several PAMP s and anti‐bacterial immunity. PP 2A constitutively associates with BAK 1 in planta . Impairment in this PP 2A‐based regulation leads to increased steady‐state BAK 1 phosphorylation, which can poise enhanced immune responses. This work identifies PP 2A as an important negative regulator of plant innate immunity that controls BAK 1 activation in surface‐localized immune receptor complexes.