Identification and Functional Analysis of in vitro/in vivo Phosphorylation Sites of the Arabidopsis BAK1 Interacting Receptor Kinase BIR2

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dc.contributor.advisor Kemmerling, Birgit (Dr.)
dc.contributor.author Schmidt, Nikola Julia
dc.date.accessioned 2017-09-25T07:33:26Z
dc.date.available 2017-09-25T07:33:26Z
dc.date.issued 2019-06-09
dc.identifier.other 1667510541 de_DE
dc.identifier.uri http://hdl.handle.net/10900/77945
dc.identifier.uri http://nbn-resolving.de/urn:nbn:de:bsz:21-dspace-779456 de_DE
dc.identifier.uri http://dx.doi.org/10.15496/publikation-19345
dc.description.abstract The recognition of plant pathogens by plants is primarily mediated by pattern recognition receptors (PRRs), acting as watchdogs at the plant surface. The leucine-rich repeat receptor-like kinase (LRR-RLK) BRI1-ASSOCIATED KINASE 1 (BAK1), and other SOMATIC EMBRYOGENESIS RECEPTOR KINASES (SERKs) play crucial roles as co-receptors of LRR-RLKs in diverse signaling pathways. Signaling has to be tightly controlled, thus the discovery of BAK1-INTERACTING RLK 2 (BIR2) as a negative regulator of BAK1, has added novel aspects to the understanding of regulatory processes in plant immunity. BIR2 can be transphosphorylated by BAK1 in vitro, and kinase complex formations are often mediated by phosphorylation-dependent mechanisms. Subject of this work is the identification of in vivo BIR2 phosphorylation sites (P-sites) by liquid chromatography-mass spectrometry/mass spectrometry (LC-MS/MS). Selected BIR2 P-sites have been mutated to alanine or aspartate to prevent or mimic phosphorylation. Functional and interaction studies with bir2 mutant lines, complemented with these constructs have revealed the potential action of these BIR2 P-sites. BIR2 transphosphorylation could have a dual function; strengthening and weakening the protein-protein interaction to regulate receptor complex formation and downstream signaling. Nevertheless, BAK1-unrelated BIR2 P-sites were detected, pointing to an involvement of other kinases in BIR2-BAK1 complex action. These findings underline the importance of phosphorylation as a key protein modification for the regulation of receptor complex dynamics. en
dc.language.iso en de_DE
dc.publisher Universität Tübingen de_DE
dc.rights ubt-podno de_DE
dc.rights.uri http://tobias-lib.uni-tuebingen.de/doku/lic_ohne_pod.php?la=de de_DE
dc.rights.uri http://tobias-lib.uni-tuebingen.de/doku/lic_ohne_pod.php?la=en en
dc.subject.classification Schmalwand <Arabidopsis> , Kinasen , Phosphorylierung , Massenspektrometrie de_DE
dc.subject.ddc 500 de_DE
dc.subject.ddc 570 de_DE
dc.subject.ddc 580 de_DE
dc.subject.other Plant innate immunity en
dc.subject.other Signaling pathway en
dc.subject.other Signalweg de_DE
dc.subject.other Immunität der Pflanzen de_DE
dc.subject.other BAK1 de_DE
dc.subject.other BIR2 de_DE
dc.title Identification and Functional Analysis of in vitro/in vivo Phosphorylation Sites of the Arabidopsis BAK1 Interacting Receptor Kinase BIR2 en
dc.type Dissertation de_DE
dcterms.dateAccepted 2017-06-09
utue.publikation.fachbereich Biologie de_DE
utue.publikation.fakultaet 7 Mathematisch-Naturwissenschaftliche Fakultät de_DE

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