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Deletion of Mia1/Alp7 activates Mad2-dependent spindle assembly checkpoint in fission yeast

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Figure 1: Spindle assembly checkpoint is activated in an alp7-deleted strain.

References

  1. Musacchio, A. & Hardwick, K.G. The spindle checkpoint: structural insights into dynamic signalling. Nature Rev. Mol. Cell Biol. 3, 731–41 (2002).

    Article  CAS  Google Scholar 

  2. Uhlmann, F., Lottspeich, F. & Nasmyth, K. Sister-chromatid separation at anaphase onset is promoted by cleavage of the cohesin subunit Scc1. Nature 400, 37–42 (1999).

    Article  CAS  Google Scholar 

  3. Gachet, Y., Tournier, S., Millar, J.B. & Hyams, J.S. A MAP kinase-dependent actin checkpoint ensures proper spindle orientation in fission yeast. Nature 412, 352–355 (2001).

    Article  CAS  Google Scholar 

  4. Oliferenko, S. & Balasubramanian, M.K. Astral microtubules monitor metaphase spindle alignment in fission yeast. Nature Cell Biol. 4, 816–820 (2002).

    Article  CAS  Google Scholar 

  5. Radcliffe, P., Hirata, D., Childs, D., Vardy, L. & Toda, T. Identification of novel temperature-sensitive lethal alleles in essential β-tubulin and nonessential α2-tubulin genes as fission yeast polarity mutants. Mol. Biol. Cell 9, 1757–1771 (1998).

    Article  CAS  Google Scholar 

  6. Zeng, X. et al. Slk19p is a centromere protein that functions to stabilize mitotic spindles. J. Cell Biol. 146, 415–426 (1999).

    Article  CAS  Google Scholar 

  7. Ikui, A.E., Furuya, K., Yanagida, M. & Matsumoto, T. Control of localization of a spindle checkpoint protein, Mad2, in fission yeast. J. Cell Sci. 115, 1603–1610 (2002).

    CAS  PubMed  Google Scholar 

  8. Garcia, M.A., Vardy, L., Koonrugsa, N. & Toda, T. Fission yeast ch-TOG/XMAP215 homologue Alp14 connects mitotic spindles with the kinetochore and is a component of the Mad2-dependent spindle checkpoint. EMBO J. 20, 3389–3401 (2001).

    Article  CAS  Google Scholar 

  9. Nabetani, A., Koujin, T., Tsutsumi, C., Haraguchi, T. & Hiraoka, Y. A conserved protein, Nuf2, is implicated in connecting the centromere to the spindle during chromosome segregation: a link between the kinetochore function and the spindle checkpoint. Chromosoma 110, 322–334 (2001).

    Article  CAS  Google Scholar 

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Acknowledgements

We thank J.-P. Javerzat and T. Matsumoto for strains, K. Gull for monoclonal the anti-α-tubulin antibody TAT-1, and A. Fujita and A. Minoda for analysing alp7 mutants at the initial stage. We are grateful to M. Balasubramanian and S. Oliferenko for sending a mia1 deletion strain and communicating unpublished results. We also thank J.S. Hyams and Y. Gachet for helpful discussions. This work is supported by Cancer Research UK, a Human Frontier Science Program research grant (to T.T.) and the Medical Research Council (to J.B.A.M.).

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Correspondence to Takashi Toda.

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Sato, M., Koonrugsa, N., Toda, T. et al. Deletion of Mia1/Alp7 activates Mad2-dependent spindle assembly checkpoint in fission yeast. Nat Cell Biol 5, 764–766 (2003). https://doi.org/10.1038/ncb0903-764

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