FB2026_03 , released September 17, 2026
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Citation
Choi, J.Y., Qiao, Q., Hong, S.H., Kim, C.M., Jeong, J.H., Kim, Y.G., Jung, Y.K., Wu, H., Park, H.H. (2017). CIDE domains form functionally important higher-order assemblies for DNA fragmentation.  Proc. Natl. Acad. Sci. U.S.A. 114(28): 7361--7366.
FlyBase ID
FBrf0236098
Publication Type
Research paper
Abstract
Cell death-inducing DFF45-like effector (CIDE) domains, initially identified in apoptotic nucleases, form a family with diverse functions ranging from cell death to lipid homeostasis. Here we show that the CIDE domains of Drosophila and human apoptotic nucleases Drep2, Drep4, and DFF40 all form head-to-tail helical filaments. Opposing positively and negatively charged interfaces mediate the helical structures, and mutations on these surfaces abolish nuclease activation for apoptotic DNA fragmentation. Conserved filamentous structures are observed in CIDE family members involved in lipid homeostasis, and mutations on the charged interfaces compromise lipid droplet fusion, suggesting that CIDE domains represent a scaffold for higher-order assembly in DNA fragmentation and other biological processes such as lipid homeostasis.
PubMed ID
PubMed Central ID
PMC5514754 (PMC) (EuropePMC)
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Secondary IDs
    Language of Publication
    English
    Additional Languages of Abstract
    Parent Publication
    Publication Type
    Journal
    Abbreviation
    Proc. Natl. Acad. Sci. U.S.A.
    Title
    Proceedings of the National Academy of Sciences of the United States of America
    Publication Year
    1915-
    ISBN/ISSN
    0027-8424
    Data From Reference
    Genes (2)