The proteasome regulator PTRE1 contributes to the turnover of SNC1 immune receptor

Molecular Plant Pathology
Karen Thulasi DevendrakumarXin Li

Abstract

Plants have evolved a sophisticated immune system in order to recognize and respond to microbes in their environments. Nucleotide-binding leucine-rich repeat (NLR) proteins detect the presence of specific effector molecules delivered into host cells by pathogens and activate strong defence responses. However, as excessive accumulation of NLRs can result in inappropriate immune responses, their abundance must be tightly regulated. Targeted degradation of NLRs through the ubiquitin proteasome pathway is an important mechanism to limit NLR accumulation. Mutations that perturb NLR degradation can cause autoimmune phenotypes. In this study, we show that the proteasome regulator PTRE1 also contributes to NLR degradation. ptre1 mutant plants exhibit increased defence marker gene expression and enhanced disease resistance against virulent pathogens. The stability of the NLR, SUPPRESSOR OF npr1-1 CONSTITUTIVE 1 (SNC1) is also increased in the ptre1 mutant. Although the mouse homologue of PTRE1 was reported to interact with a Cell Division Control protein 48 (CDC48) homologue in vitro (Clemen et al., 2015), we only observed interaction between PTRE1 and AtCDC48A in a split luciferase assay, but not in co-immunoprecipitation. In addition,...Continue Reading

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Citations

Aug 17, 2020·The Journal of Biological Chemistry·Katrina J Linden, Judy Callis
Dec 18, 2019·Plant Communications·Solveig van WerschXin Li

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Methods Mentioned

BETA
transgenic
immunoprecipitation

Software Mentioned

BLAST
ImageJ

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