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 detail^{1, 2, 3, 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 -tubulin complex⁵ (-TuC), which lacks the potential Msd1-interacting domain. We propose that Msd1 interacts with -TuC, thereby specifically anchoring the minus end of microtubules to SPBs without affecting microtubule nucleation.

1. Laboratory of Cell Regulation, Cancer Research UK, London Research Institute, Lincoln's Inn Fields Laboratories, 44 Lincoln's Inn Fields, London WC2A 3PX, UK.
2. Cell Biology and Biophysics Program, European Molecular Biology Laboratory, Meyerhofstrasse 1, D-69117 Heidelberg, Germany.
3. Current address: Laboratory for Developmental Genetics, RIKEN Center for Developmental Biology, 2-2-3 Minatojima-minamimachi, Chuo-ku, Kobe 650-0047, Japan.
4. Current address: Department of Biophysics and Biochemistry, Graduate School of Science, University of Tokyo, Tokyo 113-0033, Japan.
5. Current address: Division of Molecular and Developmental Biology, Department of Developmental Genetics, National Institute of Genetics, Yata 1111, Mishima, Shizuoka 411-8540, Japan.

Correspondence to: Takashi Toda¹ e-mail: toda@cancer.org.uk

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