S-Nitrosation of Protein Tyrosine Phosphatase 1 Prevents Its Irreversible Oxidation by Hydrogen Peroxide
Overview
Authors
Affiliations
Tyrosine-specific protein tyrosine phosphatases (Tyr-specific PTPases) are key signaling enzymes catalyzing the removal of the phosphate group from phosphorylated tyrosine residues on target proteins. This post-translational modification notably allows the regulation of mitogen-activated protein kinase (MAPK) cascades during defense reactions. protein tyrosine phosphatase 1 (PTP1), the only Tyr-specific PTPase present in this plant, acts as a repressor of HO production and regulates the activity of MPK3/MPK6 MAPKs by direct dephosphorylation. Here, we report that recombinant histidine (His)-PTP1 protein activity is directly inhibited by HO and nitric oxide (NO) exogenous treatments. The effects of NO are exerted by S-nitrosation, i.e., the formation of a covalent bond between NO and a reduced cysteine residue. This post-translational modification targets the catalytic cysteine C265 and could protect the PTP1 protein from its irreversible oxidation by HO. This mechanism of protection could be a conserved mechanism in plant PTPases.
Emerging Functions of Protein Tyrosine Phosphatases in Plants.
Xin J, Li C, Liu X, Shi X, Sun Y, Shang J Int J Mol Sci. 2024; 25(22).
PMID: 39596119 PMC: 11593807. DOI: 10.3390/ijms252212050.
Mukherjee S, Corpas F Plant Cell Environ. 2022; 46(3):688-717.
PMID: 36583401 PMC: 10108057. DOI: 10.1111/pce.14531.
Redox post-translational modifications and their interplay in plant abiotic stress tolerance.
Marti-Guillen J, Pardo-Hernandez M, Martinez-Lorente S, Almagro L, Rivero R Front Plant Sci. 2022; 13:1027730.
PMID: 36388514 PMC: 9644032. DOI: 10.3389/fpls.2022.1027730.