CIDE domains form functionally important higher-order assemblies for DNA fragmentation
| Autor: | Jae-Hee Jeong, Chang Min Kim, Yeon-Gil Kim, Hao Wu, Se Hoon Hong, Yong-Keun Jung, Hyun Ho Park, Qi Qiao, Jae Young Choi |
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| Rok vydání: | 2017 |
| Předmět: |
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 |
| Zdroj: | Proceedings of the National Academy of Sciences. 114:7361-7366 |
| ISSN: | 1091-6490 0027-8424 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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