Journal
TRAFFIC
Volume 9, Issue 6, Pages 882-892Publisher
WILEY-BLACKWELL
DOI: 10.1111/j.1600-0854.2008.00741.x
Keywords
dynein; kinesin; regulation; tau; transport
Categories
Funding
- NATIONAL INSTITUTE OF GENERAL MEDICAL SCIENCES [R01GM070676] Funding Source: NIH RePORTER
- NATIONAL INSTITUTE OF NEUROLOGICAL DISORDERS AND STROKE [R01NS048501] Funding Source: NIH RePORTER
- NIGMS NIH HHS [R01 GM070676-04, R01 GM070676, 1R01GM070676] Funding Source: Medline
- NINDS NIH HHS [R01 NS048501, 1R01NS048501] Funding Source: Medline
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We recently proposed that regulating the single-to-multiple motor transition was a likely strategy for regulating kinesin-based transport in vivo. In this study, we use an in vitro bead assay coupled with an optical trap to investigate how this proposed regulatory mechanism affects dynein-based transport. We show that tau's regulation of kinesin function can proceed without interfering with dynein-based transport. Surprisingly, at extremely high tau levels - where kinesin cannot bind microtubules (MTs) - dynein can still contact MTs. The difference between tau's effects on kinesin- and dynein-based motility suggests that tau can be used to tune relative amounts of plus-end and minus-end-directed transport. As in the case of kinesin, we find that the 3RS isoform of tau is a more potent inhibitor of dynein binding to MTs. We show that this isoform-specific effect is not because of steric interference of tau's projection domains but rather because of tau's interactions with the motor at the MT surface. Nonetheless, we do observe a modest steric interference effect of tau away from the MT and discuss the potential implications of this for molecular motor structure.
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