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

Verena Henrichs, Lenka Grycova, Cyril Barinka, Zuzana Nahacka, Jiri Neuzil, Stefan Diez, Jakub Rohlena, Marcus Braun () and Zdenek Lansky ()
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Verena Henrichs: BIOCEV, Vestec
Lenka Grycova: BIOCEV, Vestec
Cyril Barinka: BIOCEV, Vestec
Zuzana Nahacka: BIOCEV, Vestec
Jiri Neuzil: BIOCEV, Vestec
Stefan Diez: Technische Universität Dresden
Jakub Rohlena: BIOCEV, Vestec
Marcus Braun: BIOCEV, Vestec
Zdenek Lansky: BIOCEV, Vestec

Nature Communications, 2020, vol. 11, issue 1, 1-13

Abstract: 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.

Date: 2020
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DOI: 10.1038/s41467-020-16972-5

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