AI Article Synopsis

  • E3 ubiquitin ligases, specifically SCF-type ligases in plants, are crucial for regulating hormone signaling by targeting proteins for degradation, impacting various plant biological processes.
  • The specific F-box proteins TIR1 and COI1 interact with transcriptional repressors in response to auxin and jasmonates, facilitating hormone perception and gene activation.
  • Recent findings highlight the significance of S-nitrosation (a type of protein modification by nitric oxide) on E3 ligases like TIR1 and ASK1, enhancing their interactions and functions, particularly in stress responses and hormone signaling pathways.

Article Abstract

E3 ubiquitin ligases mediate the last step of the ubiquitination pathway in the ubiquitin-proteasome system (UPS). By targeting transcriptional regulators for their turnover, E3s play a crucial role in every aspect of plant biology. In plants, SKP1/CULLIN1/F-BOX PROTEIN (SCF)-type E3 ubiquitin ligases are essential for the perception and signaling of several key hormones including auxins and jasmonates (JAs). F-box proteins, TRANSPORT INHIBITOR RESPONSE 1 (TIR1) and CORONATINE INSENSITIVE 1 (COI1), bind directly transcriptional repressors AUXIN/INDOLE-3-ACETIC ACID (AUX/IAA) and JASMONATE ZIM-DOMAIN (JAZ) in auxin- and JAs-depending manner, respectively, which permits the perception of the hormones and transcriptional activation of signaling pathways. Redox modification of proteins mainly by S-nitrosation of cysteines (Cys) residues nitric oxide (NO) has emerged as a valued regulatory mechanism in physiological processes requiring its rapid and versatile integration. Previously, we demonstrated that TIR1 and SKP1 (ASK1) are targets of S-nitrosation, and these NO-dependent posttranslational modifications enhance protein-protein interactions and positively regulate SCF complex assembly and expression of auxin response genes. In this work, we confirmed S-nitrosation of Cys140 in TIR1, which was associated to auxin-dependent developmental and stress-associated responses. In addition, we provide evidence on the modulation of the SCF complex by different S-nitrosation events. We demonstrated that S-nitrosation of ASK1 Cys118 enhanced ASK1-COI1 protein-protein interaction. Overexpression of non-nitrosable ask1 mutant protein impaired the activation of JA-responsive genes mediated by SCF illustrating the functional relevance of this redox-mediated regulation . analysis positions COI1 as a promising S-nitrosation target, and demonstrated that plants treated with methyl JA (MeJA) or S-nitrosocysteine (NO-Cys, S-nitrosation agent) develop shared responses at a genome-wide level. The regulation of SCF components involved in hormonal perception by S-nitrosation may represent a key strategy to determine the precise time and site-dependent activation of each hormonal signaling pathway and highlights NO as a pivotal molecular player in these scenarios.

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Source
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC8854210PMC
http://dx.doi.org/10.3389/fpls.2021.794582DOI Listing

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