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

Autor: Anja Staab, Veronica Villeri, Kristina Desch, Erin M. Schuman, Claudia M Fusco, Julian David Langer, Ivy C. W. Chan, Aline Ricarda Dörrbaum, Mantian Wang, Eleanor Vail
Jazyk: angličtina
Rok vydání: 2021
Předmět:
Male
metabolism [Ribosomal Proteins]
Neuropil
General Physics and Astronomy
Ribosome biogenesis
metabolism [Axons]
Ribosome
Rats
Sprague-Dawley

0302 clinical medicine
Protein biosynthesis
Ribosome profiling
Cells
Cultured

Neurons
0303 health sciences
Multidisciplinary
Chemistry
Translation (biology)
metabolism [Neurites]
genetics [Ribosomes]
Cell biology
medicine.anatomical_structure
metabolism [Neurons]
Cell polarity
Female
genetics [Ribosomal Proteins]
ddc:500
Ribosomal Proteins
Science
metabolism [Neuropil]
Molecular neuroscience
metabolism [RNA
Messenger]

Article
General Biochemistry
Genetics and Molecular Biology

03 medical and health sciences
genetics [RNA
Messenger]

Ribosomal protein
Neurites
medicine
Animals
RNA
Messenger

030304 developmental biology
General Chemistry
metabolism [Ribosomes]
Axons
Rats
nervous system
Cytoplasm
Protein Biosynthesis
Ribosomes
030217 neurology & neurosurgery
Zdroj: Nature Communications 12(1), 6127 (2021). doi:10.1038/s41467-021-26365-x
Nat. Commun.
Nature Communications, Vol 12, Iss 1, Pp 1-14 (2021)
Nature Communications
Nature Communications (Nat Commun)
Popis: 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.
Ribosomes, assembled in the nucleus and perinuclear region, are thought to remain invariant throughout their lifetime. Here the authors document the dynamic association or exchange of ribosomal proteins within mature ribosomes of neuronal cells.
Databáze: OpenAIRE