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Cited by 249Ubiquitin and proteasome pathwaysAdvanced Proteomics Techniques and ApplicationsGenetics, Aging, and Longevity in Model Organisms

Local and global influences on protein turnover in neurons and glia

Open access
Dörrbaum, Aline R, Kochen, Lisa, Langer, Julian D, Schuman, Erin M·2018·eLife
DOI 10.7554/elife.34202PMC PMC6008053
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Abstract

Regulation of protein turnover allows cells to react to their environment and maintain homeostasis. Proteins can show different turnover rates in different tissue, but little is known about protein turnover in different brain cell types. We used dynamic SILAC to determine half-lives of over 5100 proteins in rat primary hippocampal cultures as well as in neuron-enriched and glia-enriched cultures ranging from <1 to >20 days. In contrast to synaptic proteins, membrane proteins were relatively shorter-lived and mitochondrial proteins were longer-lived compared to the population. Half-lives also correlate with protein functions and the dynamics of the complexes they are incorporated in. Proteins in glia possessed shorter half-lives than the same proteins in neurons. The presence of glia sped up or slowed down the turnover of neuronal proteins. Our results demonstrate that both the cell-type of origin as well as the nature of the extracellular environment have potent influences on protein turnover.

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  • CaMKII is known to turn over rapidly, with a half-life of 2-4 days.

    “In particular, CaMKII is known to turn over rapidly, with a half-life of 2–4 days (403–405).”

    From Synaptic memory and CaMKII (2023) · cites this paper as [405]

    The Results section on protein localization and function reports that CaMK2 subunits have different half-lives. It does not give a 2–4-day range for CaMKII or establish that all its subunits turn over rapidly; the numerical half-lives quoted elsewhere in the Results concern other proteins. No page number is available in our copy. (LLM, conf=0.78)

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Cited by

Sorted by citations

Authors
Dörrbaum, A. R., Kochen, L., Langer, J. D., & Schuman, E. M.
Affiliations
  • Goethe University Frankfurt (DE)
  • Max Planck Institute for Brain Research (DE)
  • Max Planck Institute of Biophysics (DE)
Corresponding author
  • Langer, Julian D
  • Schuman, Erin M
ORCID
Venue
eLife
Publisher
eLife Sciences Publications, Ltd
Published
2018-06-19
Volume
7
ISSN
2050-084X (ISSN-L)
DOI
10.7554/elife.34202
PMC
PMC6008053
OpenAlex
W2808848024
Cited by
249
References
7
Citations by year
2026: 14 · 2025: 28 · 2024: 38 · 2023: 32 · 2022: 35 · 2021: 55 · 2020: 27 · 2019: 19 · 2018: 1
FWCI
9.07
Type
journal article
Language
en
Open access
Licence
Locations
  • eLife (publishedVersion, cc-by)
  • Europe PMC (PubMed Central) (publishedVersion, cc-by)
  • PubMed Central (publishedVersion, cc-by)
  • PubMed (publishedVersion)
  • DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
  • Publication Server of Goethe University Frankfurt am Main (Goethe University Frankfurt) (submittedVersion, cc-by)
  • MPG.PuRe (Max Planck Society) (submittedVersion)
Funders
  • Horizon 2020 Framework Programme (743216)
  • Max-Planck-Gesellschaft (Open-access funding)
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Ubiquitin and proteasome pathways
  • Physical Sciences › Chemistry › Spectroscopy › Advanced Proteomics Techniques and Applications
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Aging › Genetics, Aging, and Longevity in Model Organisms
Keywords
protein turnover, protein half-life, neurons, glia, hippocampus, membrane proteins, mitochondrial proteins, synaptic proteins, extracellular environment, brain homeostasis
MeSH terms
Animals, Animals, Newborn, Cell Communication, Cerebral Cortex, Half-Life, Hippocampus, Membrane Proteins, Nerve Tissue Proteins, Neuroglia, Neurons, Culture Media, Conditioned, Rats, Sprague-Dawley, Coculture Techniques, Computational Biology, Proteome, Mitochondrial Proteins, Rats, Protein Stability, Proteolysis, Primary Cell Culture

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