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Structure of the two-fold capsomer of the dArc1 capsidStructure of the two-fold capsomer of the dArc1 capsid
Structural highlights
FunctionARC1_DROME Master regulator of synaptic plasticity that self-assembles into virion-like capsids that encapsulate RNAs and mediate intercellular RNA transfer from motorneurons to muscles (PubMed:29328915). Arc1 protein is released from motorneurons in extracellular vesicles that mediate the transfer of Arc1 mRNA into muscle cells, where Arc1 mRNA can undergo activity-dependent translation (PubMed:29328915). Intercellular transfer od Arc1 mRNA is required for synaptic plasticity at the neuromuscular junction (PubMed:29328915). May play a role in energy balance: required for regulation of body fat by a specific population of brain neurons, named E347, that are necessary and sufficient for proper body fat storage (PubMed:26209258).[1] [2] Publication Abstract from PubMedArc, a neuronal gene that is critical for synaptic plasticity, originated through the domestication of retrotransposon Gag genes and mediates intercellular messenger RNA transfer. We report high-resolution structures of retrovirus-like capsids formed by Drosophila dArc1 and dArc2 that have surface spikes and putative internal RNA-binding domains. These data demonstrate that virus-like capsid-forming properties of Arc are evolutionarily conserved and provide a structural basis for understanding their function in intercellular communication. Structures of virus-like capsids formed by the Drosophila neuronal Arc proteins.,Erlendsson S, Morado DR, Cullen HB, Feschotte C, Shepherd JD, Briggs JAG Nat Neurosci. 2020 Feb;23(2):172-175. doi: 10.1038/s41593-019-0569-y. Epub 2020, Jan 6. PMID:31907439[3] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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