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TitleCapsid transfer of the retrotransposon Copia controls structural synaptic plasticity in Drosophila.
Journal, issue, pagesPLoS Biol, Vol. 23, Issue 2, Page e3002983, Year 2025
Publish dateFeb 18, 2025
AuthorsP Githure M'Angale / Adrienne Lemieux / Yumeng Liu / Shuhao Wang / Max Zinter / Gimena Alegre / Alfred Simkin / Vivian Budnik / Brian A Kelch / Travis Thomson /
PubMed AbstractTransposons are parasitic genome elements that can also serve as raw material for the evolution of new cellular functions. However, how retrotransposons are selected and domesticated by host ...Transposons are parasitic genome elements that can also serve as raw material for the evolution of new cellular functions. However, how retrotransposons are selected and domesticated by host organisms to modulate synaptic plasticity remains largely unknown. Here, we show that the Ty1 retrotransposon Copia forms virus-like capsids in vivo and transfers between cells. Copia is enriched at the Drosophila neuromuscular junction (NMJ) and transported across synapses, and disrupting its expression promotes both synapse development and structural synaptic plasticity. We show that proper synaptic plasticity is maintained in Drosophila by the balance of Copia and the Arc1 (activity-regulated cytoskeleton-associated protein) homolog. High-resolution cryogenic-electron microscopy imaging shows that the structure of the Copia capsid has a large capacity and pores like retroviruses but is distinct from domesticated capsids such as dArc1. Our results suggest a fully functional transposon mediates synaptic plasticity, possibly representing an early stage of domestication of a retrotransposon.
External linksPLoS Biol / PubMed:39964983 / PubMed Central
MethodsEM (single particle)
Resolution3.29 - 4.17 Å
Structure data

EMDB-43571, PDB-8vvw:
Structure of the five-fold capsomer of the Drosophila retrotransposon Copia capsid
Method: EM (single particle) / Resolution: 3.29 Å

EMDB-43573, PDB-8vvz:
Structure of the three-fold capsomer of the Drosophila retrotransposon Copia capsid
Method: EM (single particle) / Resolution: 3.41 Å

EMDB-43575, PDB-8vw3:
Structure of the non-symmetric capsomer of the Drosophila retrotransposon Copia capsid
Method: EM (single particle) / Resolution: 3.47 Å

EMDB-43584, PDB-8vwg:
Structure of the Drosophila retrotransposon Copia capsid
Method: EM (single particle) / Resolution: 4.17 Å

Source
  • drosophila (fruit flies)
KeywordsVIRUS LIKE PARTICLE / Drosophila retrotransposon Copia / Gag protein

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