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

Journal of Cell Biology Volume 209 Issue 4 Page 549-562 published_at 2015-05-18
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Title ( eng )
The Msd1–Wdr8–Pkl1 complex anchors microtubule minus ends to fission yeast spindle pole bodies
Creator
Ikebe Chiho
Source Title
Journal of Cell Biology
Volume 209
Issue 4
Start Page 549
End Page 562
Abstract
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.
Descriptions
This research was supported by Cancer Research UK (T. Toda).
Language
eng
Resource Type journal article
Publisher
Rockefeller University Press
Date of Issued 2015-05-18
Rights
© 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/).
Publish Type Version of Record
Access Rights open access
Source Identifier
[ISSN] 0021-9525
[ISSN] 1540-8140
[DOI] 10.1083/jcb.201412111
[DOI] https://doi.org/10.1083/jcb.201412111