Transport of a kinesin-cargo pair along microtubules into dendritic spines undergoing synaptic plasticity

Derrick P. McVicker, Adam M. Awe, Karl E. Richters, Rebecca L. Wilson, Diana A. Cowdrey, Xindao Hu, Edwin R. Chapman and Erik W. Dent ()
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Derrick P. McVicker: University of Wisconsin, School of Medicine and Public Health
Adam M. Awe: University of Wisconsin, School of Medicine and Public Health
Karl E. Richters: University of Wisconsin, School of Medicine and Public Health
Rebecca L. Wilson: University of Wisconsin, School of Medicine and Public Health
Diana A. Cowdrey: University of Wisconsin, School of Medicine and Public Health
Xindao Hu: University of Wisconsin, School of Medicine and Public Health
Edwin R. Chapman: University of Wisconsin, School of Medicine and Public Health
Erik W. Dent: University of Wisconsin, School of Medicine and Public Health

Nature Communications, 2016, vol. 7, issue 1, 1-13

Abstract: Abstract Synaptic plasticity often involves changes in the structure and composition of dendritic spines. Vesicular cargos and organelles enter spines either by exocytosing in the dendrite shaft and diffusing into spines or through a kinesin to myosin hand-off at the base of spines. Here we present evidence for microtubule (MT)-based targeting of a specific motor/cargo pair directly into hippocampal dendritic spines. During transient MT polymerization into spines, the kinesin KIF1A and an associated cargo, synaptotagmin-IV (syt-IV), are trafficked in unison along MTs into spines. This trafficking into selected spines is activity-dependent and results in exocytosis of syt-IV-containing vesicles in the spine head. Surprisingly, knockdown of KIF1A causes frequent fusion of syt-IV-containing vesicles throughout the dendritic shaft and diffusion into spines. Taken together, these findings suggest a mechanism for targeting dendritic cargo directly into spines during synaptic plasticity and indicate that MT-bound kinesins prevent unregulated fusion by sequestering vesicular cargo to MTs.

Date: 2016
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DOI: 10.1038/ncomms12741

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