Structure of the CED-4–CED-9 complex provides insights into programmed cell death in Caenorhabditis elegans View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

2005-10

AUTHORS

Nieng Yan, Jijie Chai, Eui Seung Lee, Lichuan Gu, Qun Liu, Jiaqing He, Jia-Wei Wu, David Kokel, Huilin Li, Quan Hao, Ding Xue, Yigong Shi

ABSTRACT

Interplay 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 A 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. More... »

PAGES

831

Identifiers

URI

http://scigraph.springernature.com/pub.10.1038/nature04002

DOI

http://dx.doi.org/10.1038/nature04002

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1016162000

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/16208361


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