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dc.contributor.authorKim, Chan-Hee
dc.contributor.authorPaik, Donggi
dc.contributor.authorRus, Florentina
dc.contributor.authorSilverman, Neal S.
dc.date2022-08-11T08:09:08.000
dc.date.accessioned2022-08-23T16:19:01Z
dc.date.available2022-08-23T16:19:01Z
dc.date.issued2014-07-18
dc.date.submitted2014-11-26
dc.identifier.citationJ Biol Chem. 2014 Jul 18;289(29):20092-101. doi: 10.1074/jbc.M113.544841. Epub 2014 Jun 2. <a href="http://dx.doi.org/10.1074/jbc.M113.544841">Link to article on publisher's site</a>
dc.identifier.issn0021-9258 (Linking)
dc.identifier.doi10.1074/jbc.M113.544841
dc.identifier.pmid24891502
dc.identifier.urihttp://hdl.handle.net/20.500.14038/34949
dc.description.abstractIn Drosophila, the Imd pathway is activated by diaminopimelic acid-type peptidoglycan and triggers the humoral innate immune response, including the robust induction of antimicrobial peptide gene expression. Imd and Relish, two essential components of this pathway, are both endoproteolytically cleaved upon immune stimulation. Genetic analyses have shown that these cleavage events are dependent on the caspase-8 like Dredd, suggesting that Imd and Relish are direct substrates of Dredd. Among the seven Drosophila caspases, we find that Dredd uniquely promotes Imd and Relish processing, and purified recombinant Dredd cleaves Imd and Relish in vitro. In addition, interdomain cleavage of Dredd is not required for Imd or Relish processing and is not observed during immune stimulation. Baculovirus p35, a suicide substrate of executioner caspases, is not cleaved by purified Dredd in vitro. Consistent with this biochemistry but contrary to earlier reports, p35 does not interfere with Imd signaling in S2* cells or in vivo.
dc.language.isoen_US
dc.relation<a href="http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?db=pubmed&cmd=Retrieve&list_uids=24891502&dopt=Abstract">Link to Article in PubMed</a>
dc.relation.urlhttp://dx.doi.org/10.1074/jbc.M113.544841
dc.subjectAmino Acid Sequence
dc.subjectAmino Acid Substitution
dc.subjectAnimals
dc.subjectAnimals, Genetically Modified
dc.subjectCaspase 8
dc.subjectCaspases
dc.subjectCell Line
dc.subjectDrosophila
dc.subjectDrosophila Proteins
dc.subjectFemale
dc.subjectMolecular Sequence Data
dc.subjectMutagenesis, Site-Directed
dc.subjectProtein Interaction Domains and Motifs
dc.subjectProtein Processing, Post-Translational
dc.subjectRecombinant Proteins
dc.subjectSignal Transduction
dc.subjectSubstrate Specificity
dc.subjectTranscription Factors
dc.subjectViral Proteins
dc.subjectBiochemistry
dc.subjectImmunity
dc.subjectImmunology and Infectious Disease
dc.titleThe caspase-8 homolog Dredd cleaves Imd and Relish but is not inhibited by p35
dc.typeJournal Article
dc.source.journaltitleThe Journal of biological chemistry
dc.source.volume289
dc.source.issue29
dc.identifier.legacycoverpagehttps://escholarship.umassmed.edu/infdis_pp/171
dc.identifier.contextkey6399368
html.description.abstract<p>In Drosophila, the Imd pathway is activated by diaminopimelic acid-type peptidoglycan and triggers the humoral innate immune response, including the robust induction of antimicrobial peptide gene expression. Imd and Relish, two essential components of this pathway, are both endoproteolytically cleaved upon immune stimulation. Genetic analyses have shown that these cleavage events are dependent on the caspase-8 like Dredd, suggesting that Imd and Relish are direct substrates of Dredd. Among the seven Drosophila caspases, we find that Dredd uniquely promotes Imd and Relish processing, and purified recombinant Dredd cleaves Imd and Relish in vitro. In addition, interdomain cleavage of Dredd is not required for Imd or Relish processing and is not observed during immune stimulation. Baculovirus p35, a suicide substrate of executioner caspases, is not cleaved by purified Dredd in vitro. Consistent with this biochemistry but contrary to earlier reports, p35 does not interfere with Imd signaling in S2* cells or in vivo.</p>
dc.identifier.submissionpathinfdis_pp/171
dc.contributor.departmentDepartment of Medicine, Division of Infectious Diseases and Immunology
dc.source.pages20092-101


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