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

Jacqueline Monaghan, Susanne Matschi, Oluwaseyi Shorinola, Hanna Rovenich, Alexandra Matei, Cécile Segonzac, Frederikke Gro Malinovsky, John P. Rathjen, Dan Maclean, Tina Romeis, Cyril Zipfel*

*Corresponding author for this work

Research output: Contribution to journalArticleAcademicpeer-review

119 Citations (Scopus)

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.

Original languageEnglish
Pages (from-to)605-615
Number of pages11
JournalCell Host and Microbe
Volume16
Issue number5
DOIs
Publication statusPublished - 12 Nov 2014

Fingerprint Dive into the research topics of 'The calcium-dependent protein kinase CPK28 buffers plant immunity and regulates BIK1 turnover'. Together they form a unique fingerprint.

Cite this