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Stress-induced protein disaggregation in the endoplasmic reticulum catalysed by BiP

2022Journal article Open access
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dc.contributor.authorMelo, Eduardo
dc.contributor.authorKonno, Tasuku
dc.contributor.authorFarace, Ilaria
dc.contributor.authorAwadelkareem, Mosab Ali
dc.contributor.authorSkov, Lise R.
dc.contributor.authorTeodoro, Fernando
dc.contributor.authorSancho, Teresa
dc.contributor.authorPaton, Adrienne W.
dc.contributor.authorPaton, James C.
dc.contributor.authorFares, Matthew
dc.contributor.authorPaulo, Pedro M. R.
dc.contributor.authorZhang, Xin
dc.contributor.authorAvezov, Edward
dc.date.accessioned2022-10-10T12:36:32Z
dc.date.available2022-10-10T12:36:32Z
dc.date.issued2022
dc.description.abstractProtein synthesis is supported by cellular machineries that ensure polypeptides fold to their native conformation, whilst eliminating misfolded, aggregation prone species. Protein aggregation underlies pathologies including neurodegeneration. Aggregates' formation is antagonised by molecular chaperones, with cytoplasmic machinery resolving insoluble protein aggregates. However, it is unknown whether an analogous disaggregation system exists in the Endoplasmic Reticulum (ER) where -30% of the proteome is synthesised. Here we show that the ER of a variety of mammalian cell types, including neurons, is endowed with the capability to resolve protein aggregates under stress. Utilising a purpose-developed protein aggregation probing system with a sub-organellar resolution, we observe steady-state aggregate accumulation in the ER. Pharmacological induction of ER stress does not augment aggregates, but rather stimulate their clearance within hours. We show that this dis-sagregation activity is catalysed by the stress-responsive ER molecular chaperone - BiP. This work reveals a hitherto unknow, non-redundant strand of the proteostasis-restorative ER stress response.pt_PT
dc.description.sponsorshipEMBRC.PT ALG-01-0145-FEDER-022121
dc.description.versioninfo:eu-repo/semantics/publishedVersionpt_PT
dc.identifier.doi10.1038/s41467-022-30238-2pt_PT
dc.identifier.issn2041-1723
dc.identifier.urihttp://hdl.handle.net/10400.1/18348
dc.language.isoengpt_PT
dc.peerreviewedyespt_PT
dc.publisherNature Portfoliopt_PT
dc.relationAlgarve Centre for Marine Sciences
dc.relationAlgarve Centre for Marine Sciences
dc.rights.urihttp://creativecommons.org/licenses/by/4.0/pt_PT
dc.titleStress-induced protein disaggregation in the endoplasmic reticulum catalysed by BiPpt_PT
dc.typejournal article
dspace.entity.typePublication
oaire.awardTitleAlgarve Centre for Marine Sciences
oaire.awardTitleAlgarve Centre for Marine Sciences
oaire.awardURIinfo:eu-repo/grantAgreement/FCT/6817 - DCRRNI ID/UIDB%2F04326%2F2020/PT
oaire.awardURIinfo:eu-repo/grantAgreement/FCT/6817 - DCRRNI ID/UIDP%2F04326%2F2020/PT
oaire.citation.issue1pt_PT
oaire.citation.titleNature Communicationspt_PT
oaire.citation.volume13pt_PT
oaire.fundingStream6817 - DCRRNI ID
oaire.fundingStream6817 - DCRRNI ID
person.familyNamePinho Melo
person.familyNameTeodoro Duarte Garcia Morais
person.givenNameEduardo
person.givenNameFernando Jorge
person.identifier1443188
person.identifier.ciencia-id3C1C-C10C-1510
person.identifier.ciencia-id2517-06F1-0746
person.identifier.orcid0000-0002-0974-8977
person.identifier.orcid0000-0001-5384-1469
person.identifier.scopus-author-id35566177900
project.funder.identifierhttp://doi.org/10.13039/501100001871
project.funder.identifierhttp://doi.org/10.13039/501100001871
project.funder.nameFundação para a Ciência e a Tecnologia
project.funder.nameFundação para a Ciência e a Tecnologia
rcaap.rightsopenAccesspt_PT
rcaap.typearticlept_PT
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relation.isAuthorOfPublicatione3e3d75b-fd58-4b79-9ae0-81d77994e748
relation.isAuthorOfPublication.latestForDiscovery5fa1895f-5577-4652-961a-886ec9bf41b1
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