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The Msd1–Wdr8–Pkl1 complex anchors microtubule minus ends to fission yeast spindle pole bodies

https://hiroshima.repo.nii.ac.jp/records/2007248
https://hiroshima.repo.nii.ac.jp/records/2007248
4beea12e-fafa-4630-be11-e65dbde26d54
名前 / ファイル ライセンス アクション
JCB_209_549.pdf JCB_209_549.pdf (3.4 MB)
Item type デフォルトアイテムタイプ_(フル)(1)
公開日 2023-03-18
タイトル
タイトル The Msd1–Wdr8–Pkl1 complex anchors microtubule minus ends to fission yeast spindle pole bodies
言語 en
作成者 Yukawa, Masashi

× Yukawa, Masashi

en Yukawa, Masashi

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Ikebe, Chiho

× Ikebe, Chiho

en Ikebe, Chiho

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Toda, Takashi

× Toda, Takashi

en Toda, Takashi

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アクセス権
アクセス権 open access
アクセス権URI http://purl.org/coar/access_right/c_abf2
権利情報
権利情報 © 2015 Yukawa et al. This article is distributed under the terms of an Attribution–Noncommercial– Share Alike–No Mirror Sites license for the first six months after the publication date (see http://www.rupress.org/terms). After six months it is available under a Creative Commons License (Attribution–Noncommercial–Share Alike 3.0 Unported license, as described at http:// creativecommons.org/licenses/by-nc-sa/3.0/).
内容記述
内容記述 The minus ends of spindle microtubules are anchored to a microtubule-organizing center. The conserved Msd1/SSX2IP proteins are localized to the spindle pole body (SPB) and the centrosome in fission yeast and humans, respectively, and play a critical role in microtubule anchoring. In this paper, we show that fission yeast Msd1 forms a ternary complex with another conserved protein, Wdr8, and the minus end–directed Pkl1/kinesin-14. Individual deletion mutants displayed the identical spindle-protrusion phenotypes. Msd1 and Wdr8 were delivered by Pkl1 to mitotic SPBs, where Pkl1 was tethered through Msd1–Wdr8. The spindle-anchoring defect imposed by msd1/wdr8/pkl1 deletions was suppressed by a mutation of the plus end–directed Cut7/kinesin-5, which was shown to be mutual. Intriguingly, Pkl1 motor activity was not required for its anchoring role once targeted to the SPB. Therefore, spindle anchoring through Msd1–Wdr8–Pkl1 is crucial for balancing the Cut7/kinesin-5–mediated outward force at the SPB. Our analysis provides mechanistic insight into the spatiotemporal regulation of two opposing kinesins to ensure mitotic spindle bipolarity.
言語 en
内容記述
内容記述タイプ Other
内容記述 This research was supported by Cancer Research UK (T. Toda).
出版者
出版者 Rockefeller University Press
言語
言語 eng
資源タイプ
資源タイプ識別子 http://purl.org/coar/resource_type/c_6501
資源タイプ journal article
出版タイプ
出版タイプ VoR
出版タイプResource http://purl.org/coar/version/c_970fb48d4fbd8a85
関連情報
識別子タイプ DOI
関連識別子 10.1083/jcb.201412111
関連情報
識別子タイプ DOI
関連識別子 https://doi.org/10.1083/jcb.201412111
収録物識別子
収録物識別子タイプ ISSN
収録物識別子 0021-9525
収録物識別子
収録物識別子タイプ ISSN
収録物識別子 1540-8140
開始ページ
開始ページ 549
書誌情報 Journal of Cell Biology
Journal of Cell Biology

巻 209, 号 4, p. 549-562, 発行日 2015-05-18
旧ID 48612
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