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Phosphorylation of iRhom2 Controls Stimulated Proteolytic Shedding by the Metalloprotease ADAM17/TACE

2017-10-17Journal article Open access
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dc.contributor.authorCavadas, Miguel
dc.contributor.authorOikonomidi, Ioanna
dc.contributor.authorGaspar, Catarina J.
dc.contributor.authorBurbridge, Emma
dc.contributor.authorBadenes, Marina
dc.contributor.authorFélix, Inês
dc.contributor.authorBolado, Alfonso
dc.contributor.authorHu, Tianyi
dc.contributor.authorBileck, Andrea
dc.contributor.authorGerner, Christopher
dc.contributor.authorDomingos, Pedro M.
dc.contributor.authorvon Kriegsheim, Alex
dc.contributor.authorAdrain, Colin
dc.date.accessioned2017-10-30T17:09:36Z
dc.date.available2017-10-30T17:09:36Z
dc.date.issued2017-10-17
dc.descriptionThis deposit is composed by the main article plus the supplementary materials of the publication.pt_PT
dc.description.abstractCell surface metalloproteases coordinate signaling during development, tissue homeostasis, and disease. TACE (TNF-α-converting enzyme), is responsible for cleavage ("shedding") of membrane-tethered signaling molecules, including the cytokine TNF, and activating ligands of the EGFR. The trafficking of TACE within the secretory pathway requires its binding to iRhom2, which mediates the exit of TACE from the endoplasmic reticulum. An important, but mechanistically unclear, feature of TACE biology is its ability to be stimulated rapidly on the cell surface by numerous inflammatory and growth-promoting agents. Here, we report a role for iRhom2 in TACE stimulation on the cell surface. TACE shedding stimuli trigger MAP kinase-dependent phosphorylation of iRhom2 N-terminal cytoplasmic tail. This recruits 14-3-3 proteins, enforcing the dissociation of TACE from complexes with iRhom2, promoting the cleavage of TACE substrates. Our data reveal that iRhom2 controls multiple aspects of TACE biology, including stimulated shedding on the cell surface.pt_PT
dc.description.sponsorshipFundação Calouste Gulbenkian; Worldwide Cancer Research grant: (14-1289); Marie Curie Career Integration Grant: (project no. 618769); Fundação para a Ciência e Tecnologia grants:( SFRH/BCC/52507/2014, PTDC/BEX-BCM/3015/2014, LISBOA-01-0145-FEDER-007660, FCT-ANR/NEU-NMC/0006/2013, PTDC/NEU-NMC/2459/2014, IF/00697/2014, SFRH/BPD/117216/2016); European Crohn’s and Colitis Organization, and COST grant: (BM1406).pt_PT
dc.description.versioninfo:eu-repo/semantics/publishedVersionpt_PT
dc.identifier.citationMiguel Cavadas, Ioanna Oikonomidi, Catarina J. Gaspar, Emma Burbridge, Marina Badenes, Inês Félix, Alfonso Bolado, Tianyi Hu, Andrea Bileck, Christopher Gerner, Pedro M. Domingos, Alex von Kriegsheim, Colin Adrain, Phosphorylation of iRhom2 Controls Stimulated Proteolytic Shedding by the Metalloprotease ADAM17/TACE, In Cell Reports, Volume 21, Issue 3, 2017, Pages 745-757, ISSN 2211-1247, https://doi.org/10.1016/j.celrep.2017.09.074. (http://www.sciencedirect.com/science/article/pii/S2211124717313797) Keywords: ADAM metalloproteases; ADAM17/TACE; iRhom2; 14-3-3; MAP kinases; TNF; EGFR; ectodomain sheddingpt_PT
dc.identifier.doi10.1016/j.celrep.2017.09.074pt_PT
dc.identifier.urihttp://hdl.handle.net/10400.7/794
dc.language.isoengpt_PT
dc.peerreviewedyespt_PT
dc.publisherElsevierpt_PT
dc.relation14-1289pt_PT
dc.relationIntramembrane Proteases, their Inactive cognates, and Disease
dc.relationINTRAMEMBRANE PROTEASES THEIR INACTIVE COGNATES AND DISEASE
dc.relationBM1406pt_PT
dc.relation0145 LISBOA-01-0145-FEDER-007660pt_PT
dc.relationModulating Ire1 to prevent Parkinson' Disease
dc.relationIF/00697/2014pt_PT
dc.relationCell signaling control: mechanisms of TACE regulation during EGFR transactivation
dc.relation.publisherversionhttp://www.sciencedirect.com/science/article/pii/S2211124717313797?via%3Dihubpt_PT
dc.rights.urihttp://creativecommons.org/licenses/by/4.0/pt_PT
dc.subjectADAM metalloproteasespt_PT
dc.subjectADAM17/TACEpt_PT
dc.subjectiRhom2pt_PT
dc.subject14-3-3pt_PT
dc.subjectMAP kinasespt_PT
dc.subjectTNFpt_PT
dc.subjectEGFRpt_PT
dc.subjectectodomain sheddingpt_PT
dc.titlePhosphorylation of iRhom2 Controls Stimulated Proteolytic Shedding by the Metalloprotease ADAM17/TACEpt_PT
dc.typejournal article
dspace.entity.typePublication
oaire.awardTitleIntramembrane Proteases, their Inactive cognates, and Disease
oaire.awardTitleINTRAMEMBRANE PROTEASES THEIR INACTIVE COGNATES AND DISEASE
oaire.awardTitleModulating Ire1 to prevent Parkinson' Disease
oaire.awardTitleCell signaling control: mechanisms of TACE regulation during EGFR transactivation
oaire.awardURIinfo:eu-repo/grantAgreement/EC/FP7/618769/EU
oaire.awardURIinfo:eu-repo/grantAgreement/FCT//SFRH%2FBCC%2F52507%2F2014/PT
oaire.awardURIinfo:eu-repo/grantAgreement/FCT/3599-PPCDT/PTDC%2FBEX-BCM%2F3015%2F2014/PT
oaire.awardURIinfo:eu-repo/grantAgreement/FCT/3599-PPCDT/FCT-ANR%2FNEU-NMC%2F0006%2F2013/PT
oaire.awardURIinfo:eu-repo/grantAgreement/FCT/3599-PPCDT/PTDC%2FNEU-NMC%2F2459%2F2014/PT
oaire.awardURIinfo:eu-repo/grantAgreement/FCT/OE/SFRH%2FBPD%2F117216%2F2016/PT
oaire.citation.endPage757pt_PT
oaire.citation.issue3pt_PT
oaire.citation.startPage745pt_PT
oaire.citation.titleCell Reportspt_PT
oaire.citation.volume21pt_PT
oaire.fundingStreamFP7
oaire.fundingStream3599-PPCDT
oaire.fundingStream3599-PPCDT
oaire.fundingStream3599-PPCDT
oaire.fundingStreamOE
project.funder.identifierhttp://doi.org/10.13039/501100008530
project.funder.identifierhttp://doi.org/10.13039/501100001871
project.funder.identifierhttp://doi.org/10.13039/501100001871
project.funder.identifierhttp://doi.org/10.13039/501100001871
project.funder.identifierhttp://doi.org/10.13039/501100001871
project.funder.identifierhttp://doi.org/10.13039/501100001871
project.funder.nameEuropean Commission
project.funder.nameFundação para a Ciência e a Tecnologia
project.funder.nameFundação para a Ciência e a Tecnologia
project.funder.nameFundação para a Ciência e a Tecnologia
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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