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- Title
Preferential binding of a kinesin-1 motor to GTP-tubulin--rich microtubules underlies polarized vesicle transport.
- Authors
Nakata, Takao; Niwa, Shinsuke; Okada, Yasushi; Perez, Franck; Hirokawa, Nobutaka
- Abstract
Polarized transport in neurons is fundamental for the formation of neuronal circuitry. A motor domain--containing truncated KIF5 (a kinesin-1) recognizes axonal microtubules, which are enriched in EB1 binding sites, and selectively accumulates at the tips of axons. However , it remains unknown what cue KIF5 recognizes to result in this selective accumulation. We found that axonal microtubules were preferentially stained by the anti--GTP-tubulin antibody hMB11. Super-resolution microscopy combined with EM immunocytochemistry revealed that hMB11 was localized at KIF5 attachment sites. In addition, EB1, which binds preferentially to guanylyl-methylene-diphosphate (GMPCPP) microtubules in vitro, recognized hMB11 binding sites on axonal microtubules. Further , expression of hMB11 antibody in neurons disrupted the selective accumulation of truncated KIF5 in the axon tips. In vitro studies revealed approximately three-fold stronger binding of KIF5 motor head to GMPCPP microtubules than to GDP microtubules. Collectively, these data suggest that the abundance of GTP-tubulin in axonal microtubules may underlie selective KIF5 localization and polarized axonal vesicular transport.
- Subjects
NEURAL circuitry; NEURONS; KINESIN; MICROTUBULES; AXONS; IMMUNOCYTOCHEMISTRY
- Publication
Journal of Cell Biology, 2011, Vol 194, Issue 2, p245
- ISSN
0021-9525
- Publication type
Article
- DOI
10.1083/jcb.201104034