She3p binds to the rod of yeast myosin V and prevents it from dimerizing, forming a single-headed motor complex.

@article{Hodges2008She3pBT,
  title={She3p binds to the rod of yeast myosin V and prevents it from dimerizing, forming a single-headed motor complex.},
  author={Alex R. Hodges and Elena B. Krementsova and Kathleen M Trybus},
  journal={The Journal of biological chemistry},
  year={2008},
  volume={283 11},
  pages={6906-14}
}
Vertebrate myosin Va is a dimeric processive motor that walks on actin filaments to deliver cargo. In contrast, the two class V myosins in budding yeast, Myo2p and Myo4p, are non-processive (Reck-Peterson, S. L., Tyska, M. J., Novick, P. J., and Mooseker, M. S. (2001) J. Cell Biol. 153, 1121-1126). We previously showed that a chimera with the motor domain of Myo4p on the backbone of vertebrate myosin Va was processive, demonstrating that the Myo4p motor domain has a high duty ratio. Here we… CONTINUE READING
Highly Cited
This paper has 47 citations. REVIEW CITATIONS
20 Citations
1 References
Similar Papers

Citations

Publications citing this paper.
Showing 1-10 of 20 extracted citations

References

Publications referenced by this paper.

Single-headed Class V Myosin 6914 JOURNAL OF BIOLOGICAL CHEMISTRY VOLUME

  • A. Heuck, T. G. Du, +7 authors D. Niessing
  • J. Biol. Chem. 10.1074/jbc.M708865200
  • 2007
2 Excerpts

Similar Papers

Loading similar papers…