![[feed]](/style/images/feed-icon-14x14.png){kind=icon}
Tools
Tools
Preview |
PDF (Original Article)
- Requires a PDF viewer such as GSview, Xpdf or Adobe Acrobat Reader
1MB |
![[thumbnail of Supplementary Material]](https://edoc.mdc-berlin.de/style/images/fileicons/other.png) |
Other (Supplementary Material)
340kB |
| Item Type: | Article |
|---|---|
| Title: | Phosphoprofile reorganization of the actin binding protein Drebrin during long term depression |
| Creators Name: | Silva, Rafaela Pedro, Mack, Till G.A., Kirchner, Marieluise, Mertins, Philipp, Eickholt, Britta J. and Kreis, Patricia |
| Abstract: | Drebrin (DBN), an actin-binding protein critical for the structural integrity and function of dendritic spines, is highly phosphorylated at steady state in neurons. Here, we investigate the phosphorylation dynamics of DBN in the context of chemically induced long-term depression (cLTD), a synaptic plasticity model mimicking activity-dependent weakening of synapses. Using biochemical analyses and mass spectrometry analyses, we show that DBN undergoes rapid and robust changes in phosphorylation following cLTD induction. Notably, cLTD triggers a marked decrease in many DBN phosphorylation sites, accompanied by proteolytic cleavage of the protein, suggesting a tightly regulated mechanism linking post-translational modification to structural remodelling of the synapse. Our findings highlight the dynamic regulation of DBN by phosphorylation during synaptic depression and support its potential role as a modulator of activity-dependent synaptic plasticity. |
| Keywords: | Drebrin, Actin, Synaptic Plasticity, Long-Term Depression, Phosphorylation, Calpain |
| Source: | Frontiers in Molecular Neuroscience |
| ISSN: | 1662-5099 |
| Publisher: | Frontiers Media SA |
| Volume: | 18 |
| Page Range: | 1697642 |
| Date: | 5 November 2025 |
| Official Publication: | https://doi.org/10.3389/fnmol.2025.1697642 |
| PubMed: | View item in PubMed |
| Related to: |
Repository Staff Only: item control page
