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CIDE domains form functionally important higher-order assemblies for DNA fragmentation
- Source :
- Proceedings of the National Academy of Sciences. 114:7361-7366
- Publication Year :
- 2017
- Publisher :
- Proceedings of the National Academy of Sciences, 2017.
-
Abstract
- Significance Cell death-inducing DFF45-like effector (CIDE) domains, initially identified in apoptotic nucleases, form a highly conserved family with diverse functions ranging from cell death to lipid homeostasis and synaptic regulation. Through structural determination of two CIDE family proteins, Drep2 and Drep4, we found that CIDE domains can form helical oligomers. Our results reveal that such higher-order structures not only are conserved in the CIDE family, but also are critically important for both DNA fragmentation and lipid droplet fusion. Therefore, our findings identify the CIDE domain as a scaffolding component for higher-order structure assembly. Our results expand the importance of higher-order structures from the established field of immune signaling to broader biological functions.
- Subjects :
- 0301 basic medicine
Programmed cell death
Cell
Molecular Conformation
Apoptosis
DNA Fragmentation
Crystallography, X-Ray
Mice
03 medical and health sciences
Microscopy, Electron, Transmission
Protein Domains
Lipid droplet
medicine
Animals
Drosophila Proteins
Homeostasis
Poly-ADP-Ribose Binding Proteins
Nuclease
Binding Sites
Deoxyribonucleases
Multidisciplinary
Cell Death
biology
Effector
Apoptotic DNA fragmentation
Proteins
Biological Sciences
Lipids
Cell biology
Drosophila melanogaster
030104 developmental biology
medicine.anatomical_structure
Mutation
biology.protein
DNA fragmentation
Protein Multimerization
Apoptosis Regulatory Proteins
Subjects
Details
- ISSN :
- 10916490 and 00278424
- Volume :
- 114
- Database :
- OpenAIRE
- Journal :
- Proceedings of the National Academy of Sciences
- Accession number :
- edsair.doi.dedup.....58d09572c905816da26897af8b8d7809
- Full Text :
- https://doi.org/10.1073/pnas.1705949114