Journal
PLANT JOURNAL
Volume 79, Issue 3, Pages 427-439Publisher
WILEY-BLACKWELL
DOI: 10.1111/tpj.12573
Keywords
HSP90; NLR; resistance protein turnover; SKP1-Cullin 1-F-Box; SNC1; RPS2; RPS4; SGT1; plant immunity; Arabidopsis
Categories
Funding
- Natural Sciences and Engineering Research Council of Canada (NSERC)
- China Scholarship Council (CSC)
- NSERC
Ask authors/readers for more resources
Heat shock proteins (HSPs) serve as molecular chaperones for diverse client proteins in many biological processes. In plant immunity, cytosolic HSP90s participate in the assembly, stability control and/or activation of immune receptor complexes. In this paper we report that in addition to the well-established positive roles that HSP90 isoforms play in plant immunity, they are also involved in the negative regulation of immune receptor accumulation. Point mutations in two HSP90 genes, HSP90.2 and HSP90.3, were identified from a forward genetic screen designed to isolate mutants with enhanced disease resistance. We found that specific mutations in HSP90.2 and HSP90.3 lead to heightened accumulation of immune receptors, including SNC1, RPS2 and RPS4. HSP90s may assist SGT1 in the formation of SCF E3 ubiquitin ligase complexes that target immune receptors for degradation. Such regulation is critical for maintaining appropriate levels of immune receptor proteins to avoid autoimmunity.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available