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Negative control of BAK1 by protein phosphatase 2A during plant innate immunity

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Segonzac, C., Macho, A. P., Sanmartin, M., Ntoukakis, Vardis, Sanchez-Serrano, J. J. and Zipfel, C. (2014) Negative control of BAK1 by protein phosphatase 2A during plant innate immunity. The EMBO Journal, 33 . pp. 2069-2079. doi:10.15252/embj.201488698 ISSN 0261-4189.

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Official URL: http://dx.doi.org/10.15252/embj.201488698

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Abstract

Recognition of pathogen-associated molecular patterns (PAMPs) by surface-localized pattern-recognition receptors (PRRs) 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 (PP2A) controls the activation of PRR complexes by modulating the phosphostatus of the co-receptor and positive regulator BAK1. A potential PP2A holoenzyme composed of the subunits A1, C4, and B’η/ζ inhibits immune responses triggered by several PAMPs and anti-bacterial immunity. PP2A constitutively associates with BAK1 in planta. Impairment in this PP2A-based regulation leads to increased steady-state BAK1 phosphorylation, which can poise enhanced immune responses. This work identifies PP2A as an important negative regulator of plant innate immunity that controls BAK1 activation in surface-localized immune receptor complexes.

Item Type: Journal Article
Divisions: Faculty of Science, Engineering and Medicine > Science > Life Sciences (2010- )
Journal or Publication Title: The EMBO Journal
Publisher: Nature Publishing Group
ISSN: 0261-4189
Official Date: 1 August 2014
Dates:
DateEvent
1 August 2014Published
1 August 2014Available
8 July 2014Accepted
10 April 2014Submitted
Volume: 33
Page Range: pp. 2069-2079
DOI: 10.15252/embj.201488698
Status: Peer Reviewed
Publication Status: Published
Access rights to Published version: Restricted or Subscription Access

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