Abstract
The crystal structure of Drebrin-HBM1/Homer-EVH1 reveals an extended Homer EVH1 binding motif. Homer tetramer promotes actin bundling activity of Drebrin and stimulates Drebrin-induced filopodia formation in cells, suggesting a potential role of Homer1 in modulating synaptic spine homeostatic scaling via binding to Drebrin.
| Original language | English |
|---|---|
| Pages (from-to) | 27-38.e4 |
| Journal | Structure |
| Volume | 27 |
| Issue number | 1 |
| DOIs | |
| Publication status | Published - 2 Jan 2019 |
Bibliographical note
Publisher Copyright:© 2018 Elsevier Ltd
Keywords
- Drebrin
- EVH1 domain
- Homer1
- actin bundle
- postsynaptic density
- proline rich motif
- scaffold proteins
- synaptic plasticity
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