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  Proteome dynamics during homeostatic scaling in cultured neurons

Dörrbaum, A. R., Alvarez-Castelao, B., Nassim-Assir, B., Langer, J. D., & Schuman, E. M. (2020). Proteome dynamics during homeostatic scaling in cultured neurons. eLife, 9: e52939. doi:10.7554/eLife.52939.

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Dörrbaum, Aline Ricarda1, 2, Autor
Alvarez-Castelao, Beatriz1, Autor
Nassim-Assir, Belquis1, Autor
Langer, Julian David1, 3, Autor                 
Schuman, Erin Margaret1, Autor
Affiliations:
1Synaptic Plasticity Department, Max Planck Institute for Brain Research, Max Planck Society, ou_2461710              
2Goethe University Frankfurt, Faculty of Biological Sciences, Frankfurt, Germany, ou_persistent22              
3Proteomics and Mass Spectrometry, Max Planck Institute of Biophysics, Max Planck Society, ou_3262216              

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Schlagwörter: homeostasis; neuroscience; protein degradation; protein synthesis; protein turnover; rat; synaptic scaling
 Zusammenfassung: Protein turnover, the net result of protein synthesis and degradation, enables cells to remodel their proteomes in response to internal and external cues. Previously, we analyzed protein turnover rates in cultured brain cells under basal neuronal activity and found that protein turnover is influenced by subcellular localization, protein function, complex association, cell type of origin, and by the cellular environment (Dörrbaum et al., 2018). Here, we advanced our experimental approach to quantify changes in protein synthesis and degradation, as well as the resulting changes in protein turnover or abundance in rat primary hippocampal cultures during homeostatic scaling. Our data demonstrate that a large fraction of the neuronal proteome shows changes in protein synthesis and/or degradation during homeostatic up- and down-scaling. More than half of the quantified synaptic proteins were regulated, including pre- as well as postsynaptic proteins with diverse molecular functions

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Sprache(n): eng - English
 Datum: 2019-10-252020-03-222020-04-02
 Publikationsstatus: Online veröffentlicht
 Seiten: 28
 Ort, Verlag, Ausgabe: -
 Inhaltsverzeichnis: -
 Art der Begutachtung: Expertenbegutachtung
 Identifikatoren: DOI: 10.7554/eLife.52939
 Art des Abschluß: -

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Titel: eLife
Genre der Quelle: Zeitschrift
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Ort, Verlag, Ausgabe: Cambridge : eLife Sciences Publications
Seiten: - Band / Heft: 9 Artikelnummer: e52939 Start- / Endseite: - Identifikator: ISSN: 2050-084X
CoNE: https://pure.mpg.de/cone/journals/resource/2050-084X