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Inactive rhomboid proteins: New mechanisms with implications in health and disease

2016-12Journal article Open access
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dc.contributor.authorLemberg, Marius K
dc.contributor.authorAdrain, Colin
dc.date.accessioned2017-05-25T11:46:27Z
dc.date.available2017-12-01T01:30:09Z
dc.date.issued2016-12
dc.descriptionThis deposit is composed by the main article, and hasn't not associated any supplementary materials of the publication. This publication hasn't any creative commons license associated.pt_PT
dc.description.abstractRhomboids, proteases containing an unusual membrane-integral serine protease active site, were first identified in Drosophila, where they fulfill an essential role in epidermal growth factor receptor signaling, by cleaving membrane-tethered growth factor precursors. It has recently become apparent that eukaryotic genomes harbor conserved catalytically inactive rhomboid protease homologs, including derlins and iRhoms. Here we highlight how loss of proteolytic activity was followed in evolution by impressive functional diversification, enabling these pseudoproteases to fulfill crucial roles within the secretory pathway, including protein degradation, trafficking regulation, and inflammatory signaling. We distil the current understanding of the roles of rhomboid pseudoproteases in development and disease. Finally, we address mechanistically how versatile features of proteolytically active rhomboids have been elaborated to serve the sophisticated functions of their pseudoprotease cousins. By comparing functional and structural clues, we highlight common principles shared by the rhomboid superfamily, and make mechanistic predictions.pt_PT
dc.description.sponsorshipDeutsche Forschungsgemeinschaft grant: (SFB 1036, TP 12); Marie Curie Career Integration Grant: (PCIG13-GA-2013-618769); Worldwide Cancer Research grant: (14-1289); Fundação Calouste Gulbenkian.pt_PT
dc.description.versioninfo:eu-repo/semantics/publishedVersionpt_PT
dc.identifier.citationMarius K. Lemberg, Colin Adrain, Inactive rhomboid proteins: New mechanisms with implications in health and disease, Seminars in Cell & Developmental Biology, Volume 60, December 2016, Pages 29-37, ISSN 1084-9521, https://doi.org/10.1016/j.semcdb.2016.06.022. (http://www.sciencedirect.com/science/article/pii/S1084952116301847) Keywords: Rhomboid pseudoproteases; Endoplasmic reticulum-associated protein degradation; Vesicular trafficking control; Innate immunity; Cancer; Catalytically inactive enzyme homologspt_PT
dc.identifier.doi10.1016/j.semcdb.2016.06.022pt_PT
dc.identifier.urihttp://hdl.handle.net/10400.7/759
dc.language.isoengpt_PT
dc.peerreviewedyespt_PT
dc.publisherElsevierpt_PT
dc.relationIntramembrane Proteases, their Inactive cognates, and Disease
dc.relation.publisherversionhttp://www.sciencedirect.com/science/article/pii/S1084952116301847pt_PT
dc.subjectRhomboid pseudoproteasespt_PT
dc.subjectEndoplasmic reticulum-associated protein degradationpt_PT
dc.subjectVesicular trafficking controlpt_PT
dc.subjectVesicular trafficking controlpt_PT
dc.subjectCancerpt_PT
dc.subjectCatalytically inactive enzyme homologspt_PT
dc.titleInactive rhomboid proteins: New mechanisms with implications in health and diseasept_PT
dc.typejournal article
dspace.entity.typePublication
oaire.awardTitleIntramembrane Proteases, their Inactive cognates, and Disease
oaire.awardURIinfo:eu-repo/grantAgreement/EC/FP7/618769/EU
oaire.citation.endPage37pt_PT
oaire.citation.startPage29pt_PT
oaire.citation.titleSeminars in Cell and Developmental Biologypt_PT
oaire.citation.volume60pt_PT
oaire.fundingStreamFP7
project.funder.identifierhttp://doi.org/10.13039/501100008530
project.funder.nameEuropean Commission
rcaap.rightsembargoedAccesspt_PT
rcaap.typearticlept_PT
relation.isProjectOfPublicationd0670159-bb7c-4928-8332-8f581a65aac6
relation.isProjectOfPublication.latestForDiscoveryd0670159-bb7c-4928-8332-8f581a65aac6

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