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Article: Structure of the CED-4-CED-9 complex provides insights into programmed cell death in Caenorhabditis elegans

TitleStructure of the CED-4-CED-9 complex provides insights into programmed cell death in Caenorhabditis elegans
Authors
Issue Date2005
PublisherNature Publishing Group. The Journal's web site is located at http://www.nature.com/nature
Citation
Nature, 2005, v. 437 n. 7060, p. 831-837 How to Cite?
AbstractInterplay among four genes-egl-1, ced-9, ced-4 and ced-3-controls the onset of programmed cell death in the nematode Caenorhabditis elegans. Activation of the cell-killing protease CED-3 requires CED-4. However, CED-4 is constitutively inhibited by CED-9 until its release by EGL-1. Here we report the crystal structure of the CED-4-CED-9 complex at 2.6 Å resolution, and a complete reconstitution of the CED-3 activation pathway using homogeneous proteins of CED-4, CED-9 and EGL-1. One molecule of CED-9 binds to an asymmetric dimer of CED-4, but specifically recognizes only one of the two CED-4 molecules. This specific interaction prevents CED-4 from activating CED-3. EGL-1 binding induces pronounced conformational changes in CED-9 that result in the dissociation of the CED-4 dimer from CED-9. The released CED-4 dimer further dimerizes to form a tetramer, which facilitates the autoactivation of CED-3. Together, our studies provide important insights into the regulation of cell death activation in C. elegans. © 2005 Nature Publishing Group.
Persistent Identifierhttp://hdl.handle.net/10722/91935
ISSN
2015 Impact Factor: 38.138
2015 SCImago Journal Rankings: 21.936
ISI Accession Number ID
References

 

DC FieldValueLanguage
dc.contributor.authorYan, Nen_HK
dc.contributor.authorChai, Jen_HK
dc.contributor.authorEui, SLen_HK
dc.contributor.authorGu, Len_HK
dc.contributor.authorLiu, Qen_HK
dc.contributor.authorHe, Jen_HK
dc.contributor.authorWu, JWen_HK
dc.contributor.authorKokel, Den_HK
dc.contributor.authorLi, Hen_HK
dc.contributor.authorHao, Qen_HK
dc.contributor.authorXue, Den_HK
dc.contributor.authorShi, Yen_HK
dc.date.accessioned2010-09-17T10:31:00Z-
dc.date.available2010-09-17T10:31:00Z-
dc.date.issued2005en_HK
dc.identifier.citationNature, 2005, v. 437 n. 7060, p. 831-837en_HK
dc.identifier.issn0028-0836en_HK
dc.identifier.urihttp://hdl.handle.net/10722/91935-
dc.description.abstractInterplay among four genes-egl-1, ced-9, ced-4 and ced-3-controls the onset of programmed cell death in the nematode Caenorhabditis elegans. Activation of the cell-killing protease CED-3 requires CED-4. However, CED-4 is constitutively inhibited by CED-9 until its release by EGL-1. Here we report the crystal structure of the CED-4-CED-9 complex at 2.6 Å resolution, and a complete reconstitution of the CED-3 activation pathway using homogeneous proteins of CED-4, CED-9 and EGL-1. One molecule of CED-9 binds to an asymmetric dimer of CED-4, but specifically recognizes only one of the two CED-4 molecules. This specific interaction prevents CED-4 from activating CED-3. EGL-1 binding induces pronounced conformational changes in CED-9 that result in the dissociation of the CED-4 dimer from CED-9. The released CED-4 dimer further dimerizes to form a tetramer, which facilitates the autoactivation of CED-3. Together, our studies provide important insights into the regulation of cell death activation in C. elegans. © 2005 Nature Publishing Group.en_HK
dc.languageengen_HK
dc.publisherNature Publishing Group. The Journal's web site is located at http://www.nature.com/natureen_HK
dc.relation.ispartofNatureen_HK
dc.titleStructure of the CED-4-CED-9 complex provides insights into programmed cell death in Caenorhabditis elegansen_HK
dc.typeArticleen_HK
dc.identifier.emailHao, Q: qhao@hku.hken_HK
dc.identifier.authorityHao, Q=rp01332en_HK
dc.description.naturelink_to_subscribed_fulltext-
dc.identifier.doi10.1038/nature04002en_HK
dc.identifier.pmid16208361-
dc.identifier.scopuseid_2-s2.0-26844485563en_HK
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-26844485563&selection=ref&src=s&origin=recordpageen_HK
dc.identifier.volume437en_HK
dc.identifier.issue7060en_HK
dc.identifier.spage831en_HK
dc.identifier.epage837en_HK
dc.identifier.isiWOS:000232338600035-
dc.publisher.placeUnited Kingdomen_HK
dc.identifier.scopusauthoridYan, N=7102919452en_HK
dc.identifier.scopusauthoridChai, J=7202678942en_HK
dc.identifier.scopusauthoridEui, SL=8942151400en_HK
dc.identifier.scopusauthoridGu, L=7202674877en_HK
dc.identifier.scopusauthoridLiu, Q=35215401600en_HK
dc.identifier.scopusauthoridHe, J=35210288600en_HK
dc.identifier.scopusauthoridWu, JW=7409250712en_HK
dc.identifier.scopusauthoridKokel, D=8912968000en_HK
dc.identifier.scopusauthoridLi, H=15034755600en_HK
dc.identifier.scopusauthoridHao, Q=7102508868en_HK
dc.identifier.scopusauthoridXue, D=35739333200en_HK
dc.identifier.scopusauthoridShi, Y=7404964958en_HK
dc.identifier.citeulike341582-

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