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-Structure paper
タイトル | Structural insight into TPX2-stimulated microtubule assembly. |
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ジャーナル・号・ページ | Elife, Vol. 6, Year 2017 |
掲載日 | 2017年11月9日 |
著者 | Rui Zhang / Johanna Roostalu / Thomas Surrey / Eva Nogales / |
PubMed 要旨 | During mitosis and meiosis, microtubule (MT) assembly is locally upregulated by the chromatin-dependent Ran-GTP pathway. One of its key targets is the MT-associated spindle assembly factor TPX2. The ...During mitosis and meiosis, microtubule (MT) assembly is locally upregulated by the chromatin-dependent Ran-GTP pathway. One of its key targets is the MT-associated spindle assembly factor TPX2. The molecular mechanism of how TPX2 stimulates MT assembly remains unknown because structural information about the interaction of TPX2 with MTs is lacking. Here, we determine the cryo-electron microscopy structure of a central region of TPX2 bound to the MT surface. TPX2 uses two flexibly linked elements ('ridge' and 'wedge') in a novel interaction mode to simultaneously bind across longitudinal and lateral tubulin interfaces. These MT-interacting elements overlap with the binding site of importins on TPX2. Fluorescence microscopy-based in vitro reconstitution assays reveal that this interaction mode is critical for MT binding and facilitates MT nucleation. Together, our results suggest a molecular mechanism of how the Ran-GTP gradient can regulate TPX2-dependent MT formation. |
リンク | Elife / PubMed:29120325 / PubMed Central |
手法 | EM (らせん対称) |
解像度 | 3.3 - 3.6 Å |
構造データ | EMDB-7102: |
化合物 | ChemComp-GTP: ChemComp-MG: ChemComp-G2P: |
由来 |
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キーワード | CELL CYCLE / mitosis / GanGTP / nucleation |