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-Structure paper
タイトル | Structural insight into microtubule stabilization and kinesin inhibition by Tau family MAPs. |
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ジャーナル・号・ページ | J Cell Biol, Vol. 217, Issue 12, Page 4155-4163, Year 2018 |
掲載日 | 2018年12月3日 |
著者 | Hideki Shigematsu / Tsuyoshi Imasaki / Chihiro Doki / Takuya Sumi / Mari Aoki / Tomomi Uchikubo-Kamo / Ayako Sakamoto / Kiyotaka Tokuraku / Mikako Shirouzu / Ryo Nitta / |
PubMed 要旨 | The Tau family microtubule-associated proteins (MAPs) promote microtubule stabilization and regulate microtubule-based motility. They share the C-terminal microtubule-binding domain, which includes ...The Tau family microtubule-associated proteins (MAPs) promote microtubule stabilization and regulate microtubule-based motility. They share the C-terminal microtubule-binding domain, which includes three to five tubulin-binding repeats. Different numbers of repeats formed by alternative splicing have distinct effects on the activities of these proteins, and the distribution of these variants regulates fundamental physiological phenomena in cells. In this study, using cryo-EM, we visualized the MAP4 microtubule complex with the molecular motor kinesin-1. MAP4 bound to the C-terminal domains of tubulins along the protofilaments stabilizes the longitudinal contacts of the microtubule. The strongest bond of MAP4 was found around the intertubulin-dimer interface such that MAP4 coexists on the microtubule with kinesin-1 bound to the intratubulin-dimer interface as well. MAP4, consisting of five repeats, further folds and accumulates above the intertubulin-dimer interface, interfering with kinesin-1 movement. Therefore, these cryo-EM studies reveal new insight into the structural basis of microtubule stabilization and inhibition of kinesin motility by the Tau family MAPs. |
リンク | J Cell Biol / PubMed:30275105 / PubMed Central |
手法 | EM (らせん対称) |
解像度 | 7.29 - 7.35 Å |
構造データ | EMDB-9637: EMDB-9638: |
由来 |
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