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-Structure paper
タイトル | Kinesin-binding-triggered conformation switching of microtubules contributes to polarized transport. |
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ジャーナル・号・ページ | J Cell Biol, Vol. 217, Issue 12, Page 4164-4183, Year 2018 |
掲載日 | 2018年12月3日 |
著者 | 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 / |
PubMed 要旨 | 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 ...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. |
リンク | J Cell Biol / PubMed:30297389 / PubMed Central |
手法 | EM (らせん対称) |
解像度 | 5.35 - 6.46 Å |
構造データ | EMDB-6779, PDB-5xxt: EMDB-6781, PDB-5xxv: |
化合物 | ChemComp-GTP: ChemComp-MG: ChemComp-GDP: ChemComp-HOH: ChemComp-G2P: |
由来 |
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キーワード | STRUCTURAL PROTEIN / Microtubule / KIF5C / Kinesin |