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The long noncoding RNA mimi scaffolds neuronal granules to maintain nervous system maturity

MPG-Autoren

Grzejda,  Dominika
Max Planck Institute of Immunobiology and Epigenetics, Max Planck Society;

Mach,  Jana
Max Planck Institute of Immunobiology and Epigenetics, Max Planck Society;

Hummel,  Barbara
Max Planck Institute of Immunobiology and Epigenetics, Max Planck Society;

Rezansoff,  Andrew Mischa
Max Planck Institute of Immunobiology and Epigenetics, Max Planck Society;

Panhale,  Amol
Max Planck Institute of Immunobiology and Epigenetics, Max Planck Society;

Lalioti,  Maria-Eleni
Department of Cellular and Molecular Immunology, Max Planck Institute of Immunobiology and Epigenetics, Max Planck Society;

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Cabezas-Wallscheid,  Nina
Department of Cellular and Molecular Immunology, Max Planck Institute of Immunobiology and Epigenetics, Max Planck Society;

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Hilgers,  Valérie
Max Planck Institute of Immunobiology and Epigenetics, Max Planck Society;

Externe Ressourcen

https://www.science.org/doi/10.1126/sciadv.abo5578
(Verlagsversion)

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10.1126_sciadv.abo5578.pdf
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Zitation

Grzejda, D., Mach, J., Schweizer, J. A., Hummel, B., Rezansoff, A. M., Eggenhofer, F., et al. (2022). The long noncoding RNA mimi scaffolds neuronal granules to maintain nervous system maturity. Science Advances, 8: eabo5578. doi:10.1126/sciadv.abo5578.


Zitierlink: https://hdl.handle.net/21.11116/0000-000B-313B-C
Zusammenfassung
RNA binding proteins and messenger RNAs (mRNAs) assemble into ribonucleoprotein granules that regulate mRNA trafficking, local translation, and turnover. The dysregulation of RNA-protein condensation disturbs synaptic plas-ticity and neuron survival and has been widely associated with human neurological disease. Neuronal granules are thought to condense around particular proteins that dictate the identity and composition of each granule type. Here, we show in Drosophila that a previously uncharacterized long noncoding RNA, mimi, is required to scaffold large neuronal granules in the adult nervous system. Neuronal ELAV-like proteins directly bind mimi and mediate granule assembly, while Staufen maintains condensate integrity. mimi granules contain mRNAs and proteins involved in synaptic processes; granule loss in mimi mutant flies impairs nervous system maturity and neuropeptide-mediated signaling and causes phenotypes of neurodegeneration. Our work reports an architectural RNA for a neuronal granule and provides a handle to interrogate functions of a condensate independently of those of its constituent proteins.