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CIDE domains form functionally important higher-order assemblies for DNA fragmentation.

Jae Young Choi1, Qi Qiao2,3, Se-Hoon Hong4

  • 1School of Chemistry and Biochemistry and Graduate School of Biochemistry, Yeungnam University, Gyeongsan 712-749, South Korea.

Proceedings of the National Academy of Sciences of the United States of America
|June 28, 2017
PubMed
Summary
This summary is machine-generated.

Cell death-inducing DFF45-like effector (CIDE) domains form helical filaments crucial for DNA fragmentation and lipid homeostasis. These structures are mediated by charged interfaces, impacting nuclease activity and lipid droplet fusion.

Keywords:
CIDE familyDNA fragmentationapoptosishigher-order structurelipid homeostasis

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Area of Science:

  • Molecular Biology
  • Cell Biology
  • Biochemistry

Background:

  • Cell death-inducing DFF45-like effector (CIDE) domains are implicated in diverse cellular processes.
  • Initially identified in apoptotic nucleases, CIDE domains have functions extending to lipid homeostasis.

Purpose of the Study:

  • To investigate the structural organization of CIDE domains in apoptotic nucleases.
  • To elucidate the role of CIDE domain assembly in nuclease activation and lipid homeostasis.

Main Methods:

  • Structural analysis of CIDE domains from Drosophila and human apoptotic nucleases (Drep2, Drep4, DFF40).
  • Site-directed mutagenesis to probe the function of charged interfaces.
  • Assays for nuclease activity and lipid droplet fusion.

Main Results:

  • CIDE domains of Drep2, Drep4, and DFF40 self-assemble into head-to-tail helical filaments.
  • Opposing charged interfaces mediate filament formation; mutations disrupt nuclease activation for DNA fragmentation.
  • Conserved filamentous structures and charged interfaces are found in CIDE proteins involved in lipid homeostasis, where mutations impair lipid droplet fusion.

Conclusions:

  • CIDE domains serve as scaffolds for higher-order assembly, essential for both DNA fragmentation during apoptosis and lipid homeostasis.
  • The conserved mechanism of filament formation via charged interfaces highlights a fundamental role for CIDE domain assembly in diverse biological functions.