ArticleMolecular biology of the cell2019
Neuronal drebrin A directly interacts with mDia2 formin to inhibit actin assembly.
Article in Molecular biology of the cell, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
What it found
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Who cites it
6 citing papers in PubMed, 17 citations in OpenAlex.
- Structural mechanisms of drebrin-mediated F-actin network modulation.Nature communications · 2026Article
- Functional Differences Between Neuronal and Non-neuronal Isoforms of Drebrin.Journal of molecular biology · 2025Article
- ARHGEF5 binds Drebrin and affects α-tubulin acetylation to direct neuronal morphogenesis and migration during mouse brain development.Frontiers in molecular neuroscience · 2024Article
- A framework to validate fluorescently labeled DNA-binding proteins for single-molecule experiments.Cell reports methods · 2023Article
- Profilin and Mical combine to impair F-actin assembly and promote disassembly and remodeling.Nature communications · 2021Article
- Drebrin controls scar formation and astrocyte reactivity upon traumatic brain injury by regulating membrane trafficking.Nature communications · 2021Article
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Dendritic spines (DS) are actin-rich postsynaptic terminals of neurons that are critical for higher-order brain functions. Maturation of DS is accompanied by a change in actin architecture from linear to branched filamentous structures. Presumably, the underlying cause of this is a switch in a mode of actin assembly from formin-driven to Arp2/3-mediated via an undefined mechanism. Here we present data suggesting that neuron-specific actin-binding drebrin A may be a part of such a switch. It is well documented that DS are highly enriched in drebrin A, which is critical for their plasticity and function. At the same time, mDia2 is known to mediate the formation of filopodia-type (immature) spines. We found that neuronal drebrin A directly interacts with mDia2 formin. Drebrin inhibits formin-mediated nucleation of actin and abolishes mDia2-induced actin bundling. Using truncated protein constructs we identified the domain requirements for drebrin-mDia2 interaction. We hypothesize that accumulation of drebrin A in DS (that coincides with spine maturation) leads to inhibition of mDia2-driven actin polymerization and, therefore, may contribute to a change in actin architecture from linear to branched filaments.
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