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.
journal_name
Nat Communjournal_title
Nature communicationsauthors
Henrichs V,Grycova L,Barinka C,Nahacka Z,Neuzil J,Diez S,Rohlena J,Braun M,Lansky Zdoi
10.1038/s41467-020-16972-5subject
Has Abstractpub_date
2020-06-19 00:00:00pages
3123issue
1issn
2041-1723pii
10.1038/s41467-020-16972-5journal_volume
11pub_type
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