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The spindle-associated transmembrane protein Axs identifies a membranous structure ensheathing the meiotic spindle

Abstract

Mutations in the aberrant X segragation (Axs) gene disrupt the segregation of achiasmate chromosomes during female meiosis in Drosophila melanogaster. We show that Axs encodes the founding member of an eukaryotic family of transmembrane proteins. Axs protein colocalizes with components of the endoplasmic reticulum and is present within a structure ensheathing the meiotic spindle. In both meiotic and mitotic cells, Axs is recruited to the microtubules of assembling spindles. We propose that Axs and the sheath represent novel mediators of meiotic spindle assembly and chromosome segregation.

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Figure 1: Phenotypic analyses and localization of Axs.
Figure 2: Axs protein localization is dependent on microtubules.

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References

  1. Masui, Y. & Clarke, H.J. Int. Rev. Cytol. 57, 185–282 (1979).

    Article  CAS  PubMed  Google Scholar 

  2. Terasaki, M., Runft, L.L. & Hand, A.R. Mol. Biol. Cell 12, 1103–1116 (2001).

    Article  CAS  PubMed  PubMed Central  Google Scholar 

  3. Mehlmann, L.M., Terasaki, M., Jaffe, L.A. & Kline, D. Dev. Biol. 170, 607–615 (1995).

    Article  CAS  PubMed  Google Scholar 

  4. Henson, J.H., Beaulieu, S.M., Kaminer, B. & Begg, D.A. Dev. Biol. 142, 255–269 (1990).

    Article  CAS  PubMed  Google Scholar 

  5. Wise, D. Chromosoma 90, 50–56 (1984).

    Article  CAS  PubMed  Google Scholar 

  6. Wise, D. & Wolniak, S.M. Chromosoma 90, 156–161 (1984).

    Article  CAS  PubMed  Google Scholar 

  7. Whyte, W.L. et al. Genetics 134, 825–835 (1993).

    CAS  PubMed  PubMed Central  Google Scholar 

  8. Theurkauf, W.E. & Hawley, R.S. J. Cell Biol. 116, 1167–1180 (1992).

    Article  CAS  PubMed  Google Scholar 

  9. Hawley, R.S. & Theurkauf, W.E. Trends Genet. 9, 310–317 (1993).

    Article  CAS  PubMed  Google Scholar 

  10. Blower, M.D. & Karpen, G.H. Nature Cell Biol. 3, 730–739 (2001).

    Article  CAS  PubMed  Google Scholar 

  11. Kellogg, D.R., Mitchison, T.J. & Alberts, B.M. Development 103, 675–86 (1988).

    CAS  PubMed  Google Scholar 

  12. Li, K. et al. J. Cell Biol. 141, 455–467 (1998).

    Article  CAS  PubMed  PubMed Central  Google Scholar 

Download references

Acknowledgements

We thank T. Arbel for her efforts in the early part of this work. We also acknowledge the generous collaborative support of M. Kuroda during the early parts of these studies. We are grateful to T. Xie for critically reading the manuscript. We thank C. Orme and H. Peters for technical assistance. This research was supported by a grant to R.S.H. from the National Science Foundation. The wisdom and support of the late DeLill Nasser is gratefully acknowledged.

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Correspondence to R. Scott Hawley.

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The authors declare no competing financial interests.

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Kramer, J., Hawley, R. The spindle-associated transmembrane protein Axs identifies a membranous structure ensheathing the meiotic spindle. Nat Cell Biol 5, 261–263 (2003). https://doi.org/10.1038/ncb944

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