Arabidopsis ubiquitin ligase PUB12 interacts with and negatively regulates Chitin Elicitor Receptor Kinase 1 (CERK1).

ABSTRACT: In Arabidopsis, fungal chitin is recognized as a pathogen-associated molecular pattern (PAMP) by the chitin receptor complex containing the lysin-motif (LysM) receptor-like kinases CERK1 and LYK5. Upon the perception of chitin, CERK1 phosphorylates the receptor-like cytoplasmic kinase, PBL27, which activates the intracellular mitogen-activated protein kinase (MAPK) cascade. However, the mechanisms by which the CERK1-PBL27 complex is regulated remain largely unknown. We identified ubiquitin ligase PUB12 as a component of the PBL27 complex using co-immunoprecipitation and mass spectrometry. However, PUB12 did not interact directly with PBL27. Instead, the ARM domains of PUB12 and its paralog PUB13 interacted with the intracellular domain of CERK1 in a manner that was dependent on its autopho

SUBMITTER: Yamaguchi K 

PROVIDER: S-EPMC5705137 | biostudies-literature | 2017

REPOSITORIES: biostudies-literature