Redox proteomics and structural analyses provide insightful implications for additional non-catalytic thiol-disulfide motifs in PDIs
Protein disulfide isomerases (PDIs) catalyze redox reactions that reduce, oxidize, or isomerize disulfide bonds and act as chaperones of proteins as they fold. The characteristic features of PDIs are the presence of one or more catalytic thioredoxin (TRX)-like domains harboring typical CXXC catalyti...
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| Format: | Article |
| Language: | English |
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Elsevier
2023-02-01
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| Series: | Redox Biology |
| Subjects: | |
| Online Access: | http://www.sciencedirect.com/science/article/pii/S221323172200355X |
| _version_ | 1828065336652464128 |
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| author | Natalia Zamorano Cuervo Nathalie Grandvaux |
| author_facet | Natalia Zamorano Cuervo Nathalie Grandvaux |
| author_sort | Natalia Zamorano Cuervo |
| collection | DOAJ |
| description | Protein disulfide isomerases (PDIs) catalyze redox reactions that reduce, oxidize, or isomerize disulfide bonds and act as chaperones of proteins as they fold. The characteristic features of PDIs are the presence of one or more catalytic thioredoxin (TRX)-like domains harboring typical CXXC catalytic motifs responsible for redox reactions, as well as non-catalytic TRX-like domain. As increasing attention is paid to oxidative post-translational modifications of cysteines (Cys ox-PTMs) with the recognition that they control cellular signaling, strategies to identify sites of Cys ox-PTM by redox proteomics have been optimized. Exploration of an available Cys redoxome dataset supported by modeled structure provided arguments for the existence of an additional non-catalytic thiol-disulfide motif, distinct from those contained in the TRX type patterns, typical of PDIAs. Further structural analysis of PDIA3 and 6 allows us to consider the possibility that this hypothesis could be extended to other members of PDI. These elements invite future studies to decipher the exact role of these non-catalytic thiol-disulfide motifs in the functions of PDIs. Strategies that would allow to validate this hypothesis are discussed. |
| first_indexed | 2024-04-10T23:13:22Z |
| format | Article |
| id | doaj.art-6649072aa5dd4794a7d1a9d9bf5a520e |
| institution | Directory Open Access Journal |
| issn | 2213-2317 |
| language | English |
| last_indexed | 2024-04-10T23:13:22Z |
| publishDate | 2023-02-01 |
| publisher | Elsevier |
| record_format | Article |
| series | Redox Biology |
| spelling | doaj.art-6649072aa5dd4794a7d1a9d9bf5a520e2023-01-13T04:16:19ZengElsevierRedox Biology2213-23172023-02-0159102583Redox proteomics and structural analyses provide insightful implications for additional non-catalytic thiol-disulfide motifs in PDIsNatalia Zamorano Cuervo0Nathalie Grandvaux1CRCHUM – Centre de Recherche du Centre Hospitalier de l’Université de Montréal, 900 rue Saint Denis, Montréal, H2X 0A9, Québec, CanadaCRCHUM – Centre de Recherche du Centre Hospitalier de l’Université de Montréal, 900 rue Saint Denis, Montréal, H2X 0A9, Québec, Canada; Department of Biochemistry and Molecular Medicine, Faculty of Medicine, Université de Montréal, Montréal, H3C 3J7, Québec, Canada; Corresponding author. CRCHUM – Centre de Recherche du Centre Hospitalier de l’Université de Montréal, 900 rue Saint Denis, Montréal, H2X 0A9, Québec, Canada.Protein disulfide isomerases (PDIs) catalyze redox reactions that reduce, oxidize, or isomerize disulfide bonds and act as chaperones of proteins as they fold. The characteristic features of PDIs are the presence of one or more catalytic thioredoxin (TRX)-like domains harboring typical CXXC catalytic motifs responsible for redox reactions, as well as non-catalytic TRX-like domain. As increasing attention is paid to oxidative post-translational modifications of cysteines (Cys ox-PTMs) with the recognition that they control cellular signaling, strategies to identify sites of Cys ox-PTM by redox proteomics have been optimized. Exploration of an available Cys redoxome dataset supported by modeled structure provided arguments for the existence of an additional non-catalytic thiol-disulfide motif, distinct from those contained in the TRX type patterns, typical of PDIAs. Further structural analysis of PDIA3 and 6 allows us to consider the possibility that this hypothesis could be extended to other members of PDI. These elements invite future studies to decipher the exact role of these non-catalytic thiol-disulfide motifs in the functions of PDIs. Strategies that would allow to validate this hypothesis are discussed.http://www.sciencedirect.com/science/article/pii/S221323172200355XProtein disulfide isomerasePDIA5PDIA3PDIA6CysteineRedox |
| spellingShingle | Natalia Zamorano Cuervo Nathalie Grandvaux Redox proteomics and structural analyses provide insightful implications for additional non-catalytic thiol-disulfide motifs in PDIs Redox Biology Protein disulfide isomerase PDIA5 PDIA3 PDIA6 Cysteine Redox |
| title | Redox proteomics and structural analyses provide insightful implications for additional non-catalytic thiol-disulfide motifs in PDIs |
| title_full | Redox proteomics and structural analyses provide insightful implications for additional non-catalytic thiol-disulfide motifs in PDIs |
| title_fullStr | Redox proteomics and structural analyses provide insightful implications for additional non-catalytic thiol-disulfide motifs in PDIs |
| title_full_unstemmed | Redox proteomics and structural analyses provide insightful implications for additional non-catalytic thiol-disulfide motifs in PDIs |
| title_short | Redox proteomics and structural analyses provide insightful implications for additional non-catalytic thiol-disulfide motifs in PDIs |
| title_sort | redox proteomics and structural analyses provide insightful implications for additional non catalytic thiol disulfide motifs in pdis |
| topic | Protein disulfide isomerase PDIA5 PDIA3 PDIA6 Cysteine Redox |
| url | http://www.sciencedirect.com/science/article/pii/S221323172200355X |
| work_keys_str_mv | AT nataliazamoranocuervo redoxproteomicsandstructuralanalysesprovideinsightfulimplicationsforadditionalnoncatalyticthioldisulfidemotifsinpdis AT nathaliegrandvaux redoxproteomicsandstructuralanalysesprovideinsightfulimplicationsforadditionalnoncatalyticthioldisulfidemotifsinpdis |