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26 April 2024 |
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Structure of the CED-4-CED-9 complex provides insights into programmed cell death in Caenorhabditis elegans | | 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
; | | Date: |
6 Oct 2005 | | Journal: | Nature, 437 (7060), 831-7 | | 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. | | Source: | PubMed, pmid16208361 doi: 10.1038/nature04002 | | Services: | Forum | Review | Favorites | |
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