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The AMSH3 ESCRT-III-Associated Deubiquitinase Is Essential for Plant Immunity

The AMSH3 ESCRT-III-Associated Deubiquitinase Is Essential for Plant Immunity

Type of Publication: Journal article
Publication status: Published
URI (citable link): http://nbn-resolving.de/urn:nbn:de:bsz:352-2-1rc1n0gy5n04i0
Author: Schultz-Larsen, Torsten; Lenk, Andrea; Kalinowska, Kamila; Vestergaard, Lau Kræsing; Pedersen, Carsten; Isono, Erika; Thordal-Christensen, Hans
Year of publication: 2018
Published in: Cell Reports ; 25 (2018), 9. - pp. 2329-2338. - eISSN 2211-1247
Pubmed ID: 30485803
DOI (citable link): https://dx.doi.org/10.1016/j.celrep.2018.11.011
Summary:
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 RPM1D505V and the catalytically inactive ESCRT-III protein SKD1E232Q 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.
Subject (DDC): 570 Biosciences, Biology
Keywords: plant immunity autoimmunity, AMSH3 deubiquitinase, ESCRT, nucleotide-binding leucine-rich repeat receptors
Link to License: Attribution-NonCommercial-NoDerivatives 4.0 International
Bibliography of Konstanz: Yes
Refereed: Yes

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SCHULTZ-LARSEN, Torsten, Andrea LENK, Kamila KALINOWSKA, Lau Kræsing VESTERGAARD, Carsten PEDERSEN, Erika ISONO, Hans THORDAL-CHRISTENSEN, 2018. The AMSH3 ESCRT-III-Associated Deubiquitinase Is Essential for Plant Immunity. In: Cell Reports. 25(9), pp. 2329-2338. eISSN 2211-1247. Available under: doi: 10.1016/j.celrep.2018.11.011

@article{SchultzLarsen2018-11-27AMSH3-45320, title={The AMSH3 ESCRT-III-Associated Deubiquitinase Is Essential for Plant Immunity}, year={2018}, doi={10.1016/j.celrep.2018.11.011}, number={9}, volume={25}, journal={Cell Reports}, pages={2329--2338}, author={Schultz-Larsen, Torsten and Lenk, Andrea and Kalinowska, Kamila and Vestergaard, Lau Kræsing and Pedersen, Carsten and Isono, Erika and Thordal-Christensen, Hans} }

Pedersen, Carsten 2018-11-27 The AMSH3 ESCRT-III-Associated Deubiquitinase Is Essential for Plant Immunity Kalinowska, Kamila Schultz-Larsen, Torsten 2019-03-05T14:46:59Z Isono, Erika 2019-03-05T14:46:59Z Vestergaard, Lau Kræsing Attribution-NonCommercial-NoDerivatives 4.0 International Lenk, Andrea Pedersen, Carsten Lenk, Andrea Schultz-Larsen, Torsten Isono, Erika Kalinowska, Kamila 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<sup>D505V</sup> and the catalytically inactive ESCRT-III protein SKD1<sup>E232Q</sup> 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. eng Thordal-Christensen, Hans Thordal-Christensen, Hans Vestergaard, Lau Kræsing

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