Kinesin-binding-triggered conformation switching of microtubules contributes to polarized transport.
J Cell Biol
; 217(12): 4164-4183, 2018 12 03.
Article
in En
| MEDLINE
| ID: mdl-30297389
ABSTRACT
Kinesin-1, the founding member of the kinesin superfamily of proteins, is known to use only a subset of microtubules for transport in living cells. This biased use of microtubules is proposed as the guidance cue for polarized transport in neurons, but the underlying mechanisms are still poorly understood. Here, we report that kinesin-1 binding changes the microtubule lattice and promotes further kinesin-1 binding. This high-affinity state requires the binding of kinesin-1 in the nucleotide-free state. Microtubules return to the initial low-affinity state by washing out the binding kinesin-1 or by the binding of non-hydrolyzable ATP analogue AMPPNP to kinesin-1. X-ray fiber diffraction, fluorescence speckle microscopy, and second-harmonic generation microscopy, as well as cryo-EM, collectively demonstrated that the binding of nucleotide-free kinesin-1 to GDP microtubules changes the conformation of the GDP microtubule to a conformation resembling the GTP microtubule.
Full text:
1
Collection:
01-internacional
Database:
MEDLINE
Main subject:
Kinesins
/
Microtubules
Limits:
Animals
/
Humans
Language:
En
Journal:
J Cell Biol
Year:
2018
Document type:
Article
Affiliation country:
Japan