| Autor: |
María José Iglesias, María Cecilia Terrile, Natalia Correa-Aragunde, Silvana Lorena Colman, Alicia Izquierdo-Álvarez, Diego Fernando Fiol, Ramiro París, Nuria Sánchez-López, Anabel Marina, Luz Irina A. Calderón Villalobos, Mark Estelle, Lorenzo Lamattina, Antonio Martínez-Ruiz, Claudia Anahí Casalongué |
| Jazyk: |
angličtina |
| Rok vydání: |
2018 |
| Předmět: |
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| Zdroj: |
Redox Biology, Vol 18, Iss , Pp 200-210 (2018) |
| Druh dokumentu: |
article |
| ISSN: |
2213-2317 |
| DOI: |
10.1016/j.redox.2018.07.003 |
| Popis: |
The F-box proteins (FBPs) TIR1/AFBs are the substrate recognition subunits of SKP1–cullin–F-box (SCF) ubiquitin ligase complexes and together with Aux/IAAs form the auxin co-receptor. Although tremendous knowledge on auxin perception and signaling has been gained in the last years, SCFTIR1/AFBs complex assembly and stabilization are emerging as new layers of regulation. Here, we investigated how nitric oxide (NO), through S-nitrosylation of ASK1 is involved in SCFTIR1/AFBs assembly. We demonstrate that ASK1 is S-nitrosylated and S-glutathionylated in cysteine (Cys) 37 and Cys118 residues in vitro. Both, in vitro and in vivo protein-protein interaction assays show that NO enhances ASK1 binding to CUL1 and TIR1/AFB2, required for SCFTIR1/AFB2 assembly. In addition, we demonstrate that Cys37 and Cys118 are essential residues for proper activation of auxin signaling pathway in planta. Phylogenetic analysis revealed that Cys37 residue is only conserved in SKP proteins in Angiosperms, suggesting that S-nitrosylation on Cys37 could represent an evolutionary adaption for SKP1 function in flowering plants. Collectively, these findings indicate that multiple events of redox modifications might be part of a fine-tuning regulation of SCFTIR1/AFBs for proper auxin signal transduction. Keywords: Arabidopsis thaliana, ASK1, Nitric oxide, Auxin signaling, SCF E3 ligase complex |
| Databáze: |
Directory of Open Access Journals |
| Externí odkaz: |
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