Publication:
Redox-dependent and redox-independent functions of Caenorhabditis elegans thioredoxin 1.

dc.contributor.authorSanzo-Machuca, Ángela
dc.contributor.authorMonje Moreno, José Manuel
dc.contributor.authorCasado-Navarro, Rafael
dc.contributor.authorKarakuzu, Ozgur
dc.contributor.authorGuerrero-Gómez, David
dc.contributor.authorFierro-González, Juan Carlos
dc.contributor.authorSwoboda, Peter
dc.contributor.authorMuñoz, Manuel J
dc.contributor.authorGarsin, Danielle A
dc.contributor.authorPedrajas, José Rafael
dc.contributor.authorBarrios, Arantza
dc.contributor.authorMiranda-Vizuete, Antonio
dc.date.accessioned2023-01-25T13:32:31Z
dc.date.available2023-01-25T13:32:31Z
dc.date.issued2019-03-27
dc.description.abstractThioredoxins (TRX) are traditionally considered as enzymes catalyzing redox reactions. However, redox-independent functions of thioredoxins have been described in different organisms, although the underlying molecular mechanisms are yet unknown. We report here the characterization of the first generated endogenous redox-inactive thioredoxin in an animal model, the TRX-1 in the nematode Caenorhabditis elegans. We find that TRX-1 dually regulates the formation of an endurance larval stage (dauer) by interacting with the insulin pathway in a redox-independent manner and the cGMP pathway in a redox-dependent manner. Moreover, the requirement of TRX-1 for the extended longevity of worms with compromised insulin signalling or under calorie restriction relies on TRX-1 redox activity. In contrast, the nuclear translocation of the SKN-1 transcription factor and increased LIPS-6 protein levels in the intestine upon trx-1 deficiency are strictly redox-independent. Finally, we identify a novel function of C. elegans TRX-1 in male food-leaving behaviour that is redox-dependent. Taken together, our results position C. elegans as an ideal model to gain mechanistic insight into the redox-independent functions of metazoan thioredoxins, overcoming the limitations imposed by the embryonic lethal phenotypes of thioredoxin mutants in higher organisms.
dc.identifier.doi10.1016/j.redox.2019.101178
dc.identifier.essn2213-2317
dc.identifier.pmcPMC6449771
dc.identifier.pmid30953965
dc.identifier.pubmedURLhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC6449771/pdf
dc.identifier.unpaywallURLhttps://doi.org/10.1016/j.redox.2019.101178
dc.identifier.urihttp://hdl.handle.net/10668/13795
dc.journal.titleRedox biology
dc.journal.titleabbreviationRedox Biol
dc.language.isoen
dc.organizationInstituto de Biomedicina de Sevilla-IBIS
dc.organizationHospital Universitario Virgen del Rocío
dc.page.number101178
dc.pubmedtypeJournal Article
dc.pubmedtypeResearch Support, N.I.H., Extramural
dc.pubmedtypeResearch Support, Non-U.S. Gov't
dc.rightsAttribution-NonCommercial-NoDerivatives 4.0 International
dc.rights.accessRightsopen access
dc.rights.urihttp://creativecommons.org/licenses/by-nc-nd/4.0/
dc.subjectCaenorhabditis elegans
dc.subjectDauer
dc.subjectFood-leaving
dc.subjectLips-6
dc.subjectLongevity
dc.subjectMale
dc.subjectRedox
dc.subjectSkn-1
dc.subjectThioredoxin
dc.subject.meshAmino Acid Substitution
dc.subject.meshAnimals
dc.subject.meshBiomarkers
dc.subject.meshCaenorhabditis elegans
dc.subject.meshCaenorhabditis elegans Proteins
dc.subject.meshCysteine
dc.subject.meshDNA Mutational Analysis
dc.subject.meshDNA-Binding Proteins
dc.subject.meshGene Expression
dc.subject.meshMale
dc.subject.meshMutation
dc.subject.meshOxidation-Reduction
dc.subject.meshProtein Transport
dc.subject.meshThioredoxins
dc.subject.meshTranscription Factors
dc.titleRedox-dependent and redox-independent functions of Caenorhabditis elegans thioredoxin 1.
dc.typeresearch article
dc.type.hasVersionVoR
dc.volume.number24
dspace.entity.typePublication
Files
Original bundle
Now showing 1 - 1 of 1
Loading...
Thumbnail Image
Name:
PMC6449771.pdf
Size:
2.16 MB
Format:
Adobe Portable Document Format