γ-Tubulin complex-mediated anchoring of spindle microtubules to spindle-pole bodies requires Msd1 in fission yeast

Mika Toya, Masamitsu Sato, Uta Haselmann, Kazuhide Asakawa, Damian Brunner, Claude Antony, Takashi Toda*

*この研究の対応する著者

研究成果: Article査読

41 被引用数 (Scopus)

抄録

The anchoring of microtubules to subcellular structures is critical for cell polarity and motility. Although the process of anchoring cytoplasmic microtubules to the centrosome has been studied in some detail1-4, it is not known how spindle microtubules are anchored to the mitotic centrosome and, particularly, whether anchoring and nucleation of mitotic spindles are functionally separate. Here, we show that a fission yeast coiled-coil protein, Msd1, is required for anchoring the minus end of spindle microtubules to the centrosome equivalent, the spindle-pole body (SPB). msd1 deletion causes spindle microtubules to abnormally extend beyond SPBs, which results in chromosome missegregation. Importantly, this protruding spindle is phenocopied by the amino-terminal deletion mutant of Alp4, a component of the γ-tubulin complex5 (γ-TuC), which lacks the potential Msd1-interacting domain. We propose that Msd1 interacts with γ-TuC, thereby specifically anchoring the minus end of microtubules to SPBs without affecting microtubule nucleation.

本文言語English
ページ(範囲)646-653
ページ数8
ジャーナルNature Cell Biology
9
6
DOI
出版ステータスPublished - 2007 6月
外部発表はい

ASJC Scopus subject areas

  • 細胞生物学

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