David Biermann

@davidbiermann.bsky.social

PhD Student at TUM in group of @julien-gronnier.bsky.social Plant Evolution - Plasma Membrane - Cell Surface Innovations 🔬🧬

Latest work from our group on powdery mildew susceptibility is finally out! We show that host RALF signalling, cell wall organization, and apoplastic pH regulation are required for successful fungal colonization. Surprisingly, the function of RALFs is only partly dependent on FERONIA. #TRR356

New Phytologist@newphyt.bsky.social · 2mo ago

RALFs, likely combining cell wall and signalling functions, support powdery mildew infection of #Arabidopsis 📖 nph.onlinelibrary.wiley.com/doi/10.1111/... by Leicher et al. @WileyPlantSci #PlantScience

Model of RALF-FER-dependent effects on powdery mildew sporulation.

Born from the collaborative spirit of #TRR356, I’m excited to share my first first-author project! 🪴🦠 What started as a side project with @kbuhrman.bsky.social led us to discover that KAR/KL and SL signalling fine-tune the strength and timing of plant defense responses in a conserved manner!

bioRxiv Plant Bio@biorxiv-plants.bsky.social · 3mo ago

Karrikin and strigolactone signalling affect pattern-triggered immunity and resistance to specific pathogens https://www.biorxiv.org/content/10.64898/2026.05.05.722863v1

Thrilled to see my main PhD project finally online @MolCell !! 🥳🌱🧬 If you want to know how the plant proteasome activators are sorted in a proteasome-dependent manner and how they coordinate transcriptional response during proteotoxic stress, please have a read ! 🤓 www.cell.com/molecular-ce...

Proteotoxic stress response is governed by ER-associated sorting of proteasome transcriptional activators

Langin et al. find that ER-associated sorting (ERAS) directs NAC53/78 turnover and activation to couple proteasome induction with repression of photosynthesis genes, linking proteostasis to energy met...

cell.com

New Preprint: Plasma membrane nanoscale dynamics of Arabidopsis leucine-rich repeat receptor kinase complexes (2026) https://www.tsl.ac.uk/publications/164874

bioRxiv: Plasma membrane nanoscale dynamics of Arabidopsis leucine-rich repeat receptor kinase complexes (2026)

Plasma membrane-localized receptors operate as dynamic signaling complexes and integrative networks, yet the spatial and temporal regulation of these interactions remain largely unknown. Here, by analyzing the components of a minimal Arabidopsis leucine-rich repeat receptor kinase network, we describe the differential diffusion and organization of receptor complex components and unveil the nanoscale spatial and temporal logic underlying the formation of receptor kinase complexes. The ligand-binding receptors FLS2 and BRI1, and the accessory receptor BIR3, are organized in plasma membrane nanodomains, within which the co-receptor BAK1 diffuses and is spatially arrested upon ligand perception. BAK1 spatial arrest relies on extracellular domain (ECD)-ECD interactions but does not require receptor complex activation. Mathematical modelling, single molecule imaging and bio-assays infer that accessory receptors maintain a dynamic pool of co-receptors in the vicinity of ligand-binding receptors to promote ligand-induced complex formation and signaling. We propose that ligand-induced receptor kinase complex formation is a deterministic process defined by the relative nanoscale spatial positioning of individual signaling and regulatory components.

doi.org