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The AMSH3 ESCRT-III-Associated Deubiquitinase Is Essential for Plant Immunity
Author(s) -
Torsten SchultzLarsen,
Andrea Lenk,
Kamila Kalinowska,
Lau K. Vestergaard,
Carsten Pedersen,
Erika Isono,
Hans ThordalChristensen
Publication year - 2018
Publication title -
cell reports
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 6.264
H-Index - 154
eISSN - 2639-1856
pISSN - 2211-1247
DOI - 10.1016/j.celrep.2018.11.011
Subject(s) - deubiquitinating enzyme , plant immunity , immunity , escrt , chemistry , biology , immune system , biochemistry , immunology , ubiquitin , gene , cell , endosome , arabidopsis , mutant
Plant "nucleotide-binding leucine-rich repeat" receptor proteins (NLRs) detect alterations in host targets of pathogen effectors and trigger immune responses. The Arabidopsis thaliana mutant pen1 syp122 displays autoimmunity, and a mutant screen identified the deubiquitinase "associated molecule with the SH3 domain of STAM3" (AMSH3) to be required for this phenotype. AMSH3 has previously been implicated in ESCRT-mediated vacuolar targeting. Pathology experiments show that AMSH3 activity is required for immunity mediated by the CC-NLRs, RPS2 and RPM1. Co-expressing the autoactive RPM1 D505V and the catalytically inactive ESCRT-III protein SKD1 E232Q in Nicotiana benthamiana supports the requirement of ESCRT-associated functions for this CC-NLR-activated immunity. Meanwhile, loss of ESCRT function in A. thaliana is lethal, and we find that AMSH3 knockout-triggered seedling lethality is "enhanced disease susceptibility 1" (EDS1) dependent. Future studies may reveal whether AMSH3 is monitored by a TIR-NLR immunity receptor.

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