Help Privacy Policy Disclaimer
  Advanced SearchBrowse




Journal Article

Proteome dynamics during homeostatic scaling in cultured neurons


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

External Resource
Fulltext (restricted access)
There are currently no full texts shared for your IP range.
Fulltext (public)

(Publisher version), 5MB

Supplementary Material (public)
There is no public supplementary material available

Dorrbaum, 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.

Cite as: https://hdl.handle.net/21.11116/0000-0007-EEE7-9
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 (Dorrbaum 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.