Poster
Ruoqi Dou
Queen's University
Kingston, Ontario, Canada
Karima El Mahboubi
Laboratoire de Recherche en Sciences Végétales (LRSV), Université de Toulouse, CNRS, UPS
Toulouse, Midi-Pyrenees, France
Cailun A.S. Tanney
Queen's University
kingston, Ontario, Canada
Jiashu Chu
Institute of Plant and Microbial Biology and Zurich-Basel Plant Science Center, University of Zurich
Zurich, Zurich, Switzerland
Baptiste Castel
CNRS
Castanet Tolosan, Midi-Pyrenees, France
Melissa Bredow
Department of Plant Pathology, Entomology and Microbiology, Iowa State University
Ames, Iowa, United States
Maria Camila Rodriguez-Gallo
University of Alberta
Edmonton, Alberta, Canada
Virginia-Natali Miguel
Queen's University
Kingston, Ontario, Canada
Dominique Lauressergues
Laboratoire de Recherche en Sciences Végétales (LRSV), Université de Toulouse, CNRS
Toulouse, Midi-Pyrenees, France
Jean Keller
CNRS
Castanet-Tolosan, Midi-Pyrenees, France
Thomas A. DeFalco
Assistant professor
Department of Biology, Western University
London, Ontario, Canada
R. Glen Uhrig
Professor
University of Alberta
Edmonton, Alberta, Canada
Cyril Zipfel
Institute of Plant and Microbial Biology, University of Zurich / The Sainsbury Laboratory
Zurich, Zurich, Switzerland
Pierre-Marc Delaux
CNRS
Castanet-Tolosan, Midi-Pyrenees, France
Jacqueline Monaghan
Queen's University
Kingston, Ontario, Canada
Immune homeostasis is critical for plant survival, ensuring an optimal balance between pathogen defense and growth. In Arabidopsis thaliana, CALCIUM-DEPENDENT PROTEIN KINASE 28 (CPK28) regulates immune signaling by phosphorylating the E3 ubiquitin ligases PLANT U-BOX 25 (PUB25) and PUB26, which mediate turnover of BOTRYTIS-INDUCED KINASE 1 (BIK1), a key immune signaling hub. BIK1 stability is also redundantly controlled by PUB22, PUB23, and PUB24, forming a robust regulatory network that prevents excessive immune activation. However, whether this immune regulatory module is conserved across land plants remains unclear. Here, we identify and characterize a homologous CPK28-PUB-BIK1 module in the liverwort Marchantia polymorpha. We show that MpCPK28 phosphorylates and interacts with MpPUB20e, a putative ortholog of AtPUB25/26, and MpPBLa, a functional equivalent of AtBIK1. MpPBLa undergoes proteasomal degradation and is ubiquitinated by MpPUB20e in vitro, mirroring PUB25/26 function. Overexpression of MpCPK28 in Marchantia causes developmental abnormalities and reduced chitin-induced ROS, resembling AtCPK28 overexpression. Complementation assays confirm functional conservation, as MpCPK28 rescues the immune and developmental defects of Arabidopsis cpk28-1 mutants. These findings indicate that the CPK28-PUB-BIK1 module is an ancient mechanism of immune homeostasis in land plants. I will present ongoing work aimed at strengthening this hypothesis.