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Mitochondria-adaptor TRAK1 promotes kinesin-1 driven transport in crowded environments.

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Diez,  Stefan
Max Planck Institute for Molecular Cell Biology and Genetics, Max Planck Society;

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Braun,  Marcus
Max Planck Institute for Molecular Cell Biology and Genetics, Max Planck Society;

/persons/resource/persons219371

Lansky,  Zdenek
Max Planck Institute for Molecular Cell Biology and Genetics, Max Planck Society;

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Citation

Henrichs, V., Grycova, L., Barinka, C., Nahacka, Z., Neuzil, J., Diez, S., et al. (2020). Mitochondria-adaptor TRAK1 promotes kinesin-1 driven transport in crowded environments. Nature communications, 11(1): 3123. doi:10.1038/s41467-020-16972-5.


Cite as: https://hdl.handle.net/21.11116/0000-0008-A2FA-7
Abstract
Intracellular trafficking of organelles, driven by kinesin-1 stepping along microtubules, underpins essential cellular processes. In absence of other proteins on the microtubule surface, kinesin-1 performs micron-long runs. Under crowding conditions, however, kinesin-1 motility is drastically impeded. It is thus unclear how kinesin-1 acts as an efficient transporter in intracellular environments. Here, we demonstrate that TRAK1 (Milton), an adaptor protein essential for mitochondrial trafficking, activates kinesin-1 and increases robustness of kinesin-1 stepping on crowded microtubule surfaces. Interaction with TRAK1 i) facilitates kinesin-1 navigation around obstacles, ii) increases the probability of kinesin-1 passing through cohesive islands of tau and iii) increases the run length of kinesin-1 in cell lysate. We explain the enhanced motility by the observed direct interaction of TRAK1 with microtubules, providing an additional anchor for the kinesin-1-TRAK1 complex. Furthermore, TRAK1 enables mitochondrial transport in vitro. We propose adaptor-mediated tethering as a mechanism regulating kinesin-1 motility in various cellular environments.