Homotypic FADD interactions through a conserved RXDLL motif are required for death receptor-induced apoptosis
DC Field | Value | Language |
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dc.contributor.author | Muppidi, J. R. | - |
dc.contributor.author | Lobito, A. A. | - |
dc.contributor.author | Ramaswamy, M. | - |
dc.contributor.author | Yang, J. K. | - |
dc.contributor.author | Wang, L. | - |
dc.contributor.author | Wu, H. | - |
dc.contributor.author | Siegel, R. M. | - |
dc.date.available | 2018-05-08T12:55:30Z | - |
dc.date.created | 2018-04-18 | - |
dc.date.issued | 2006-10 | - |
dc.identifier.issn | 1350-9047 | - |
dc.identifier.uri | http://scholarworks.bwise.kr/ssu/handle/2018.sw.ssu/6140 | - |
dc.description.abstract | Death receptors in the TNF receptor superfamily signal for apoptosis via the ordered recruitment of FADD and caspase-8 to a death-inducing signaling complex ( DISC). However, the nature of the protein-protein interactions in the signaling complex is not well defined. Here we show that FADD self-associates through a conserved RXDLL motif in the death effector domain (DED). Despite exhibiting similar binding to both Fas and caspase-8 and preserved overall secondary structure, FADD RDXLL motif mutants cannot reconstitute FasL- or TRAIL-induced apoptosis and fail to recruit caspase-8 into the DISC of reconstituted FADD-deficient cells. Abolishing self-association can transform FADD into a dominant-negative mutant that interferes with Fas-induced apoptosis and formation of microscopically visible receptor oligomers. These findings suggest that lateral interactions among adapter molecules are required for death receptor apoptosis signaling and implicate self-association into oligomeric assemblies as a key function of death receptor adapter proteins in initiating apoptosis. | - |
dc.language | 영어 | - |
dc.language.iso | en | - |
dc.publisher | NATURE PUBLISHING GROUP | - |
dc.relation.isPartOf | CELL DEATH AND DIFFERENTIATION | - |
dc.title | Homotypic FADD interactions through a conserved RXDLL motif are required for death receptor-induced apoptosis | - |
dc.type | Article | - |
dc.identifier.doi | 10.1038/sj.cdd.4401855 | - |
dc.type.rims | ART | - |
dc.identifier.bibliographicCitation | CELL DEATH AND DIFFERENTIATION, v.13, no.10, pp.1641 - 1650 | - |
dc.description.journalClass | 1 | - |
dc.identifier.wosid | 000241301400003 | - |
dc.identifier.scopusid | 2-s2.0-33744517489 | - |
dc.citation.endPage | 1650 | - |
dc.citation.number | 10 | - |
dc.citation.startPage | 1641 | - |
dc.citation.title | CELL DEATH AND DIFFERENTIATION | - |
dc.citation.volume | 13 | - |
dc.contributor.affiliatedAuthor | Yang, J. K. | - |
dc.type.docType | Article | - |
dc.description.isOpenAccess | N | - |
dc.description.journalRegisteredClass | scopus | - |
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