TY - JOUR
T1 - The calcium-dependent protein kinase CPK28 buffers plant immunity and regulates BIK1 turnover
AU - Monaghan, Jacqueline
AU - Matschi, Susanne
AU - Shorinola, Oluwaseyi
AU - Rovenich, Hanna
AU - Matei, Alexandra
AU - Segonzac, Cécile
AU - Malinovsky, Frederikke Gro
AU - Rathjen, John P.
AU - MacLean, Dan
AU - Romeis, Tina
AU - Zipfel, Cyril
N1 - Copyright © 2014 Elsevier Inc. All rights reserved.
PY - 2014/11/12
Y1 - 2014/11/12
N2 - 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.
AB - 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.
U2 - 10.1016/j.chom.2014.10.007
DO - 10.1016/j.chom.2014.10.007
M3 - Journal article
C2 - 25525792
SN - 1931-3128
VL - 16
SP - 605
EP - 615
JO - Cell Host and Microbe
JF - Cell Host and Microbe
IS - 5
ER -