The calcium-dependent protein kinase CPK28 buffers plant immunity and regulates BIK1 turnover

Monaghan, Jacqueline, Matschi, Susanne, Shorinola, Oluwaseyi, Rovenich, Hanna, Matei, Alexandra, Segonzac, Cécile, Malinovsky, Frederikke Gro, Rathjen, John P, MacLean, Dan, Romeis, Tina and Zipfel, Cyril (2014) The calcium-dependent protein kinase CPK28 buffers plant immunity and regulates BIK1 turnover. Cell Host & Microbe, 16 (5). pp. 605-15. ISSN 1931-3128

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Abstract

Plant perception of pathogen-associated molecular patterns (PAMPs) triggers a phosphorylation relay leading to PAMP-triggered immunity (PTI). Despite increasing knowledge of PTI signaling, how immune homeostasis is maintained remains largely unknown. Here we describe a forward-genetic screen to identify loci involved in PTI and characterize the Arabidopsis calcium-dependent protein kinase CPK28 as a negative regulator of immune signaling. Genetic analyses demonstrate that CPK28 attenuates PAMP-triggered immune responses and antibacterial immunity. CPK28 interacts with and phosphorylates the plasma-membrane-associated cytoplasmic kinase BIK1, an important convergent substrate of multiple pattern recognition receptor (PRR) complexes. We find that BIK1 is rate limiting in PTI signaling and that it is continuously turned over to maintain cellular homeostasis. We further show that CPK28 contributes to BIK1 turnover. Our results suggest a negative regulatory mechanism that continually buffers immune signaling by controlling the turnover of this key signaling kinase.

Item Type: Article
Additional Information: Copyright © 2014 Elsevier Inc. All rights reserved.
Uncontrolled Keywords: amino acid sequence,arabidopsis,arabidopsis proteins,gene expression regulation, plant,genetic loci,molecular sequence data,phosphorylation,plant diseases,plant immunity,protein kinases,protein-serine-threonine kinases
Faculty \ School: Faculty of Science > School of Biological Sciences
Depositing User: Pure Connector
Date Deposited: 09 Mar 2016 14:00
Last Modified: 24 Jul 2019 22:03
URI: https://ueaeprints.uea.ac.uk/id/eprint/57392
DOI: 10.1016/j.chom.2014.10.007

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