A role for S-nitrosylation of the SUMO-conjugating enzyme SCE1 in plant immunity.

Proceedings of the National Academy of Sciences of the United States of America
Michael J SkellyGary J Loake

Abstract

SUMOylation, the covalent attachment of the small ubiquitin-like modifier (SUMO) to target proteins, is emerging as a key modulator of eukaryotic immune function. In plants, a SUMO1/2-dependent process has been proposed to control the deployment of host defense responses. The molecular mechanism underpinning this activity remains to be determined, however. Here we show that increasing nitric oxide levels following pathogen recognition promote S-nitrosylation of the Arabidopsis SUMO E2 enzyme, SCE1, at Cys139. The SUMO-conjugating activities of both SCE1 and its human homolog, UBC9, were inhibited following this modification. Accordingly, mutation of Cys139 resulted in increased levels of SUMO1/2 conjugates, disabled immune responses, and enhanced pathogen susceptibility. Our findings imply that S-nitrosylation of SCE1 at Cys139 enables NO bioactivity to drive immune activation by relieving SUMO1/2-mediated suppression. The control of global SUMOylation is thought to occur predominantly at the level of each substrate via complex local machineries. Our findings uncover a parallel and complementary mechanism by suggesting that total SUMO conjugation may also be regulated directly by SNO formation at SCE1 Cys139. This Cys is evolut...Continue Reading

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Citations

Apr 28, 2020·The New Phytologist·Kapuganti Jagadis GuptaGary J Loake
Sep 11, 2020·Journal of Experimental Botany·Jeremy AstierDavid Wendehenne
Oct 3, 2020·Journal of Experimental Botany·Jibril LubegaGary J Loake
Oct 15, 2020·Journal of Experimental Botany·Zsuzsanna KolbertAndrea Rónavári
Mar 2, 2021·Frontiers in Plant Science·Zhen-Chao LiJian-Zhong Liu
Jun 3, 2021·Plants·Catherine M Doorly, Emmanuelle Graciet
Jun 20, 2021·Journal of Experimental Botany·Kishor D IngoleSaikat Bhattacharjee

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