Enzymatic Phosphorylation of Oxidized Tyrosine Residues
Post-translational modifications (PTMs) alter the function and fate of proteins and cells in almost every conceivable way. Protein modifications can occur as a result of specific regulating actions of enzymes, such as tyrosine kinases phosphorylating tyrosine residues or by nonenzymatic reactions, such as oxidation related to oxidative stress and diseases. While many studies have addressed the multisite, dynamic, and network-like properties of PTMs, only little is known of the interplay of the same site modifications. In this work, we studied the enzymatic phosphorylation of oxidized tyrosine (l-DOPA) residues using synthetic insulin receptor peptides, in which tyrosine residues were replaced with l-DOPA. The phosphorylated peptides were identified by liquid chromatography-high-resolution mass spectrometry and the site of phosphorylation by tandem mass spectrometry. The results clearly show that the oxidized tyrosine residues are phosphorylated, displaying a specific immonium ion peak in the MS2 spectra. Furthermore, we detected this modification in our reanalysis (MassIVE ID: MSV000090106) of published bottom-up phosphoproteomics data. The modification, where both oxidation and phosphorylation take place at the same amino acid, has not yet been published in PTM databases. Our data indicate that there can be multiple PTMs that do not exclude each other at the same modification site.
| Medienart: |
E-Artikel |
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| Erscheinungsjahr: |
2023 |
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| Erschienen: |
2023 |
| Enthalten in: |
Zur Gesamtaufnahme - volume:22 |
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| Enthalten in: |
Journal of proteome research - 22(2023), 6 vom: 02. Juni, Seite 1959-1968 |
| Sprache: |
Englisch |
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| Beteiligte Personen: |
Heininen, Juho [VerfasserIn] |
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| Links: |
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| Anmerkungen: |
Date Completed 05.06.2023 Date Revised 20.06.2023 published: Print-Electronic Citation Status MEDLINE |
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| doi: |
10.1021/acs.jproteome.3c00061 |
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| funding: |
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| Förderinstitution / Projekttitel: |
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NLM356492613 |
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| 245 | 1 | 0 | |a Enzymatic Phosphorylation of Oxidized Tyrosine Residues |
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| 520 | |a Post-translational modifications (PTMs) alter the function and fate of proteins and cells in almost every conceivable way. Protein modifications can occur as a result of specific regulating actions of enzymes, such as tyrosine kinases phosphorylating tyrosine residues or by nonenzymatic reactions, such as oxidation related to oxidative stress and diseases. While many studies have addressed the multisite, dynamic, and network-like properties of PTMs, only little is known of the interplay of the same site modifications. In this work, we studied the enzymatic phosphorylation of oxidized tyrosine (l-DOPA) residues using synthetic insulin receptor peptides, in which tyrosine residues were replaced with l-DOPA. The phosphorylated peptides were identified by liquid chromatography-high-resolution mass spectrometry and the site of phosphorylation by tandem mass spectrometry. The results clearly show that the oxidized tyrosine residues are phosphorylated, displaying a specific immonium ion peak in the MS2 spectra. Furthermore, we detected this modification in our reanalysis (MassIVE ID: MSV000090106) of published bottom-up phosphoproteomics data. The modification, where both oxidation and phosphorylation take place at the same amino acid, has not yet been published in PTM databases. Our data indicate that there can be multiple PTMs that do not exclude each other at the same modification site | ||
| 650 | 4 | |a Journal Article | |
| 650 | 4 | |a Research Support, Non-U.S. Gov't | |
| 650 | 4 | |a insulin receptor | |
| 650 | 4 | |a liquid chromatography-tandem mass spectrometry (LC-MS/MS) | |
| 650 | 4 | |a mass spectrometry (MS) | |
| 650 | 4 | |a oxidation−reduction (redox) | |
| 650 | 4 | |a phosphorylation | |
| 650 | 4 | |a post-translational modification (PTM) | |
| 650 | 4 | |a ultra-high-performance liquid chromatography (UHPLC) | |
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| 700 | 1 | |a Kotiaho, Tapio |e verfasserin |4 aut | |
| 700 | 1 | |a Kostiainen, Risto |e verfasserin |4 aut | |
| 700 | 1 | |a Teppo, Jaakko |e verfasserin |4 aut | |
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