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Neuronal ribosomes exhibit dynamic and context-dependent exchange of ribosomal proteins

MPG-Autoren

Fusco,  Claudia M.
Synaptic Plasticity Department, Max Planck Institute for Brain Research, Max Planck Society;

Desch,  Kristina
Synaptic Plasticity Department, Max Planck Institute for Brain Research, Max Planck Society;

Dörrbaum,  Aline R.
Synaptic Plasticity Department, Max Planck Institute for Brain Research, Max Planck Society;

Wang,  Mantian
Synaptic Plasticity Department, Max Planck Institute for Brain Research, Max Planck Society;

Staab,  Anja
Synaptic Plasticity Department, Max Planck Institute for Brain Research, Max Planck Society;

Chan,  Ivy C. W.
Synaptic Plasticity Department, Max Planck Institute for Brain Research, Max Planck Society;

Vail,  Eleanor
Synaptic Plasticity Department, Max Planck Institute for Brain Research, Max Planck Society;

Villeri,  Veronica
Synaptic Plasticity Department, Max Planck Institute for Brain Research, Max Planck Society;

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Langer,  Julian D.       
Synaptic Plasticity Department, Max Planck Institute for Brain Research, Max Planck Society;
Proteomics and Mass Spectrometry, Max Planck Institute of Biophysics, Max Planck Society;

Schuman,  Erin M.
Synaptic Plasticity Department, Max Planck Institute for Brain Research, Max Planck Society;

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Zitation

Fusco, C. M., Desch, K., Dörrbaum, A. R., Wang, M., Staab, A., Chan, I. C. W., et al. (2021). Neuronal ribosomes exhibit dynamic and context-dependent exchange of ribosomal proteins. Nature Communications, 12(1): 6127. doi:10.1038/s41467-021-26365-x.


Zitierlink: https://hdl.handle.net/21.11116/0000-0009-671E-3
Zusammenfassung
Owing to their morphological complexity and dense network connections, neurons modify their proteomes locally, using mRNAs and ribosomes present in the neuropil (tissue enriched for dendrites and axons). Although ribosome biogenesis largely takes place in the nucleus and perinuclear region, neuronal ribosomal protein (RP) mRNAs have been frequently detected remotely, in dendrites and axons. Here, using imaging and ribosome profiling, we directly detected the RP mRNAs and their translation in the neuropil. Combining brief metabolic labeling with mass spectrometry, we found that a group of RPs rapidly associated with translating ribosomes in the cytoplasm and that this incorporation was independent of canonical ribosome biogenesis. Moreover, the incorporation probability of some RPs was regulated by location (neurites vs. cell bodies) and changes in the cellular environment (following oxidative stress). Our results suggest new mechanisms for the local activation, repair and/or specialization of the translational machinery within neuronal processes, potentially allowing neuronal synapses a rapid means to regulate local protein synthesis.