Volker Lipka & Cara Haney

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Plants monitor the presence of potentially harmful pathogens by plasma-membrane localized receptor complexes, which detect conserved microbe associated molecular patterns (MAMPs) such as non-self cell wall components (Petutschnig et al.., 2010; Antolín-Llovera et al., 2014; Erwig et al., 2017; Barghahn et al., 2021). We recently identified a lineage-specific structural component of bacterial cell walls (Pierdzig et al., unpublished) that triggers programmed cell death responses in Arabidopsis thaliana.

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This project will focus on the underlying molecular mechanisms. To this end, the selected PhD student will characterize available Arabidopsis suppressor mutants, identify the underlying mutated genes via a mapping-by-sequencing approach and will functionally characterize the respective gene products using cell biology, molecular biology and biochemical experimental strategies. Effects on plant microbiome assemblies will be studied in collaboration with Prof. Dr. Cara Haney (University of Vancouver).

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References

Antolín-Llovera M., Petutsching E.K., Ried M.K., Lipka V., Nürnberger T., Robatzek S., Parniske M.:Knowing your friends and foes--plant receptor-like kinases as initiators of symbiosis or defence. New Phytologist 204(4): 791-802. (2014)

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Barghahn S., Arnal G., Jain N., Petutschnig E.K., Brumer H. and Lipka V.:Mixed Linkage β-1,3/1,4-Glucan Oligosaccharides Induce Defense Responses in Hordeum vulgare and Arabidopsis thaliana. Frontiers in Plant Science doi:10.3389/fpls.2021.682439 (2021)

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Erwig J., Ghareeb H., Kopischke M., Hacke R., Matei A., Petutschnig E.K., Lipka V.: Chitin-induced and CHITIN ELICITOR RECEPTOR KINASE1 (CERK1) phosphorylation-dependent endocytosis of Arabidopsis thaliana LYSIN MOTIF-CONTAINING RECEPTOR-LIKE KINASE5 (LYK5). New Phytologist 215(1): 382-396. (2017)

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Petutschnig E.K., Jones A.M., Serazetdinova L., Lipka U. and Lipka V.: The Lysin Motif Receptor-like Kinase (LysM-RLK) CERK1 Is a Major Chitin-binding Protein in Arabidopsis thaliana and Subject to Chitin-induced Phosphorylation. Journal of Biological Chemistry 285(37): 28902-28911. (2010)

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