[Seminar] Targeting Post Translational Modifications in Plant Immunity Signaling

Title: Targeting Post Translational Modifications in Plant Immunity Signaling

Speaker: Frank L.H. Menke

Affiliation: The Sainsbury Laboratory, Norwich Research Park, Norwich, United Kingdom

Abstract:

Innate immune systems in animals and plants have to recognize pathogens in the extracellular space. For this they rely on plasma membrane localized pattern recognition receptors (PRRs) that bind pathogen derived molecular patterns (PAMPs). Upon binding of PAMPs to PRRs signaling networks are triggered that ultimately results in PAMP triggered immunity (PTI). How activated PRR are connected to downstream defense activation has largely remained an open question, but it is evident that changes in phosphorylation play a major role and changes in ubiquitination play an emergent role. We have used quantitative phosphoproteomics approaches (Benschop et al., 2007; Mithoe et al., 2012) to identify key players in PRR signaling. Some of the earliest changes in phosphorylation, immediately downstream of activated PRRs, were identified on BIK1, RBOHD and MKKK7 (Kadota et al 2014; Mithoe et al 2016). Our initial analysis using a ubiquitin-remnant enrichment approach suggests that key components of PRR signaling also rapidly become ubiquitinated. Using targeted proteomics we are now measuring temporal changes in both phosphorylation and ubiquitination on components required in the PRR signaling network.