PUBLICATION
Structure and Function of an Actin-Based Filter in the Proximal Axon
- Authors
- Balasanyan, V., Watanabe, K., Dempsey, W.P., Lewis, T.L., Trinh, L.A., Arnold, D.B.
- ID
- ZDB-PUB-171207-11
- Date
- 2017
- Source
- Cell Reports 21: 2696-2705 (Journal)
- Registered Authors
- Dempsey, William, Trinh, Le
- Keywords
- none
- MeSH Terms
-
- Actin Cytoskeleton/metabolism
- Actin-Related Protein 2-3 Complex/metabolism
- Actins/metabolism*
- Animals
- Axons/metabolism
- Cell Survival/physiology
- Dendrites/metabolism
- Microtubules/metabolism
- Myosins/metabolism
- Neurons/metabolism*
- Rats
- PubMed
- 29212018 Full text @ Cell Rep.
Citation
Balasanyan, V., Watanabe, K., Dempsey, W.P., Lewis, T.L., Trinh, L.A., Arnold, D.B. (2017) Structure and Function of an Actin-Based Filter in the Proximal Axon. Cell Reports. 21:2696-2705.
Abstract
The essential organization of microtubules within neurons has been described; however, less is known about how neuronal actin is arranged and the functional implications of its arrangement. Here, we describe, in live cells, an actin-based structure in the proximal axon that selectively prevents some proteins from entering the axon while allowing the passage of others. Concentrated patches of actin in proximal axons are present shortly after axonal specification in rat and zebrafish neurons imaged live, and they mark positions where anterogradely traveling vesicles carrying dendritic proteins halt and reverse. Patches colocalize with the ARP2/3 complex, and when ARP2/3-mediated nucleation is blocked, a dendritic protein mislocalizes to the axon. Patches are highly dynamic, with few persisting longer than 30 min. In neurons in culture and in vivo, actin appears to form a contiguous, semipermeable barrier, despite its apparently sparse distribution, preventing axonal localization of constitutively active myosin Va but not myosin VI.
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