Department of Neurobiology
Animals; Animals, Genetically Modified; Dendrites; Drosophila; Drosophila Proteins; Dynein ATPase; Membrane Proteins; Microtubule-Associated Proteins; Models, Biological; Mosaicism; Multiprotein Complexes; Organ Specificity; Protein Binding; Protein Isoforms; Protein Structure, Tertiary; Protein Transport
Life Sciences | Medicine and Health Sciences | Neuroscience and Neurobiology
BACKGROUND: Many membrane proteins, including Drosophila Dscam, are enriched in dendrites or axons within neurons. However, little is known about how the differential distribution is established and maintained.
METHODOLOGY/PRINCIPAL FINDINGS: Here we investigated the mechanisms underlying the dendritic targeting of Dscam[TM1]. Through forward genetic mosaic screens and by silencing specific genes via targeted RNAi, we found that several genes, encoding various components of the dynein-dynactin complex, are required for restricting Dscam[TM1] to the mushroom body dendrites. In contrast, compromising dynein/dynactin function did not affect dendritic targeting of two other dendritic markers, Nod and Rdl. Tracing newly synthesized Dscam[TM1] further revealed that compromising dynein/dynactin function did not affect the initial dendritic targeting of Dscam[TM1], but disrupted the maintenance of its restriction to dendrites.
CONCLUSIONS/SIGNIFICANCE: The results of this study suggest multiple mechanisms of dendritic protein targeting. Notably, dynein-dynactin plays a role in excluding dendritic Dscam, but not Rdl, from axons by retrograde transport.
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Citation: PLoS One. 2008;3(10):e3504. Epub 2008 Oct 23. Link to article on publisher's site