RAIDD is a new 'death' adaptor molecule
dc.contributor.author | Duan, H. | en_US |
dc.contributor.author | Dixit, Vishva M. | en_US |
dc.date.accessioned | 2009-06-01T17:34:43Z | |
dc.date.available | 2009-06-01T17:34:43Z | |
dc.date.issued | 1997-01-02 | en_US |
dc.identifier.citation | Duan, H; Dixit, VM. (1997) "RAIDD is a new 'death' adaptor molecule." Nature 385(6611): 86-89. <http://hdl.handle.net/2027.42/62739> | en_US |
dc.identifier.issn | 0028-0836 | en_US |
dc.identifier.uri | https://hdl.handle.net/2027.42/62739 | |
dc.identifier.uri | http://www.ncbi.nlm.nih.gov/sites/entrez?cmd=retrieve&db=pubmed&list_uids=8985253&dopt=citation | en_US |
dc.description.abstract | THE effector arm of the the cell-death pathway is composed of cysteine proteases belonging to the ICE/CED-3 family(1,2). In metazoan cells these exist as inactive polypeptide precursors (zymogens), each composed of a prodomain, which is cleaved to activate the protease, and a large and small catalytic subunit. The coupling of these 'death' proteases to signalling pathways is probably mediated by adaptor molecules that contain protein-protein interaction motifs such as the death domain(1). Were we describe such an adaptor molecule, RAIDD, which has an unusual bipartite architecture comprising a carboxy-terminal death domain that binds to the homologous domain in RIP, a serine/threonine kinase component of the death pathway(3,4). The amino-terminal domain is surprisingly homologous with the sequence of the prodomain of two ICE/CED-3 family members, human ICH-1 (ref. 5) and Caenorhabditis elegans CED-3 (ref. 6). This similar region mediates the binding of RAIDD to ICH-1 and CED-3, serving as a direct link to the death proteases, indicating that the prodomain may, through homophilic interactions, determine the specificity of binding of ICE/CED-3 zymogens to regulatory adaptor molecules. Finally, alternations in the sequence of the N-terminal domain that are equivalent to inactivating mutations in the C. elegans ced-3 gene(7,8) prevent homophilic binding, highlighting the potentially primordial nature of this interaction. | en_US |
dc.format.extent | 1367369 bytes | |
dc.format.extent | 2489 bytes | |
dc.format.mimetype | application/octet-stream | |
dc.format.mimetype | text/plain | |
dc.publisher | Macmillan Magazines Ltd. | en_US |
dc.source | Nature | en_US |
dc.title | RAIDD is a new 'death' adaptor molecule | en_US |
dc.type | Article | en_US |
dc.subject.hlbtoplevel | Science | en_US |
dc.description.peerreviewed | Peer Reviewed | en_US |
dc.contributor.affiliationum | UNIV MICHIGAN, SCH MED, DEPT PATHOL, ANN ARBOR, MI 48109 USA | en_US |
dc.identifier.pmid | 8985253 | en_US |
dc.description.bitstreamurl | http://deepblue.lib.umich.edu/bitstream/2027.42/62739/1/385086a0.pdf | |
dc.identifier.doi | http://dx.doi.org/10.1038/385086a0 | en_US |
dc.identifier.source | Nature | en_US |
dc.owningcollname | Interdisciplinary and Peer-Reviewed |
Files in this item
Remediation of Harmful Language
The University of Michigan Library aims to describe library materials in a way that respects the people and communities who create, use, and are represented in our collections. Report harmful or offensive language in catalog records, finding aids, or elsewhere in our collections anonymously through our metadata feedback form. More information at Remediation of Harmful Language.
Accessibility
If you are unable to use this file in its current format, please select the Contact Us link and we can modify it to make it more accessible to you.