SSBD - Singularity biology paper - Shima T et. al. (2018), J Cell Biol 217(12), 4164-4183

Paper information

Tomohiro Shima, Manatsu Morikawa, Junichi Kaneshiro, Taketoshi Kambara, Shinji Kamimura, Toshiki Yagi, Hiroyuki Iwamoto, Sotaro Uemura, Hideki Shigematsu, Mikako Shirouzu, Taro Ichimura, Tomonobu M Watanabe, Ryo Nitta, Yasushi Okada, Nobutaka Hirokawa (2018) Kinesin-binding-triggered conformation switching of microtubules contributes to polarized transport., The Journal of cell biology, Volume 217, Number 12, pp. 4164-4183

Electronic Published Date

Oct. 8, 2018, midnight

Published Date

2018 Dec 3

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.

MeSH Terms

DOI

doi: 10.1083/jcb.201711178

PubMed Central ID

PMC6279379

SSBD:database

Singularity Biology: Shima T et. al. (2018), J Cell Biol 217(12), 4164-4183