A novel strategy to visualize vesicle-bound kinesins reveals the diversity of kinesin-mediated transport

Rui Yang, Zoe Bostick, Alex Garbouchian, Julie Luisi, Gary Banker, Marvin Bentley

Research output: Contribution to journalArticle

2 Scopus citations

Abstract

In mammals, 15 to 20 kinesins are thought to mediate vesicle transport. Little is known about the identity of vesicles moved by each kinesin or the functional significance of such diversity. To characterize the transport mediated by different kinesins, we developed a novel strategy to visualize vesicle-bound kinesins in living cells. We applied this method to cultured neurons and systematically determined the localization and transport parameters of vesicles labeled by different members of the Kinesin-1, -2, and -3 families. We observed vesicle labeling with nearly all kinesins. Only six kinesins bound vesicles that undergo long-range transport in neurons. Of these, three had an axonal bias (KIF5B, KIF5C and KIF13B), two were unbiased (KIF1A and KIF1Bβ), and one transported only in dendrites (KIF13A). Overall, the trafficking of vesicle-bound kinesins to axons or dendrites did not correspond to their motor domain preference, suggesting that on-vesicle regulation is crucial for kinesin targeting. Surprisingly, several kinesins were associated with populations of somatodendritic vesicles that underwent little long-range transport. This assay should be broadly applicable for investigating kinesin function in many cell types.

Original languageEnglish (US)
Pages (from-to)851-866
Number of pages16
JournalTraffic
Volume20
Issue number11
DOIs
Publication statusPublished - Nov 1 2019

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Keywords

  • Kinesin
  • membrane trafficking
  • motor protein
  • neuron
  • polarity
  • transport
  • vesicle

ASJC Scopus subject areas

  • Structural Biology
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology

Cite this

Yang, R., Bostick, Z., Garbouchian, A., Luisi, J., Banker, G., & Bentley, M. (2019). A novel strategy to visualize vesicle-bound kinesins reveals the diversity of kinesin-mediated transport. Traffic, 20(11), 851-866. https://doi.org/10.1111/tra.12692