Kinesin expands and stabilizes the GDP-microtubule lattice.

ABSTRACT: Kinesin-1 is a nanoscale molecular motor that walks towards the fast-growing (plus) ends of microtubules, hauling molecular cargo to specific reaction sites in cells. Kinesin-driven transport is central to the self-organization of eukaryotic cells and shows great promise as a tool for nano-engineering ¹ . Recent work hints that kinesin may also play a role in modulating the stability of its microtubule track, both in vitro^2,3 and in vivo ⁴ , but the results are conflicting^5-7 and the mechanisms are unclear. Here, we report a new dimension to the kinesin-microtubule interaction, whereby strong-binding state (adenosine triphosphate (ATP)-bound and apo) kinesin-1 motor domains inhibit the shrinkage of guanosine diphosphate (GDP) microtubules by up t

SUBMITTER: Peet DR 

PROVIDER: S-EPMC5937683 | biostudies-literature | 2018 May

REPOSITORIES: biostudies-literature