Journal
JOURNAL OF CELL SCIENCE
Volume 121, Issue 7, Pages 1085-1095Publisher
COMPANY BIOLOGISTS LTD
DOI: 10.1242/jcs.026492
Keywords
kinesin-1; microtubules; detyrosinated microtubules; trafficking
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Funding
- Biotechnology and Biological Sciences Research Council [BB/D524875/1] Funding Source: Medline
- Cancer Research UK Funding Source: Medline
- Medical Research Council Funding Source: Medline
- Wellcome Trust Funding Source: Medline
- BBSRC [BB/D524875/1] Funding Source: UKRI
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Kinesin-1 is a molecular transporter that trafficks along microtubules. There is some evidence that kinesin-1 targets specific cellular sites, but it is unclear how this spatial regulation is achieved. To investigate this process, we used a combination of in vivo imaging of kinesin heavy-chain Kif5c ( an isoform of kinesin-1) fused to GFP, in vitro analyses and mathematical modelling. GFP-Kif5c fluorescent puncta localised to a subset of microtubules in live cells. These puncta moved at speeds of up to 1 mu m second(-1) and exchanged into cortically labelled clusters at microtubule ends. This behaviour depended on the presence of a functional motor domain, because a rigor-mutant GFP-Kif5c bound to microtubules but did not move along them. Further analysis indicated that the microtubule subset decorated by GFP-Kif5c was highly stable and primarily composed of detyrosinated tubulin. In vitro motility assays showed that the motor domain of Kif5c moved detyrosinated microtubules at significantly lower velocities than tyrosinated ( unmodified) microtubules. Mathematical modelling predicted that a small increase in detyrosination would bias kinesin-1 occupancy towards detyrosinated microtubules. These data suggest that kinesin-1 preferentially binds to and trafficks on detyrosinated microtubules in vivo, providing a potential basis for the spatial targeting of kinesin-1-based cargo transport.
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