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Updated: Jan 10, 2026

Identification of Post-translational Modifications of Plant Protein Complexes
Published on: February 22, 2014
Regulation of plant NLRs by post-translational modifications
Chenchen Zhong1, Xinchen Wang1, Yi Li1
1State Key Laboratory of Plant Environmental Resilience, College of Biological Sciences, China Agricultural University, Beijing 100193, China.
Abstract:
The discovery of resistosomes has revolutionized our understanding of plant immunity by elucidating the structural and mechanistic basis of nucleotide-binding leucine-rich repeat receptor (NLR)-mediated defense. Recent structural insights and mechanistic studies highlight the pivotal role of post-translational modifications (PTMs), including phosphorylation, ubiquitination, lipidation, acetylation, and SUMOylation in regulating NLR function. Kinases, E3 ubiquitin ligases, and other PTM-modifying enzymes have emerged as key regulators that control NLR conformational dynamics, stability, and immune signaling. These findings underscore the importance of spatiotemporal regulation in balancing growth-defense trade-off during NLR-mediated immunity and provide new insights for engineering NLRs to enhance crop disease resistance.
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