Kinetochore dynein: its dynamics and role in the transport of the Rough deal checkpoint protein

E Wojcik1, R Basto, M Serr

  • 1Virginia Tech University, Department of Biology, Blacksburg, Virginia 24061, USA. ewojcik@vt.edu

Nature Cell Biology
|November 21, 2001
PubMed

Insights

Kinetochore dynein-dynactin motors help remove checkpoint proteins from kinetochores in Drosophila embryos. This motor activity is crucial for timely progression through metaphase and entry into anaphase.

Area of Science:

  • Cell Biology
  • Molecular Motors
  • Genetics

Background:

  • The kinetochore-microtubule interface is critical for chromosome segregation.
  • The spindle assembly checkpoint (SAC) ensures proper chromosome attachment before anaphase.
  • Dynein-dynactin complexes are involved in various cellular transport processes.

Purpose of the Study:

  • To investigate the dynamics of kinetochore dynein-dynactin in living Drosophila embryos.
  • To determine the role of dynein in regulating metaphase checkpoint proteins.
  • To understand how dynein influences the transition from metaphase to anaphase.

Main Methods:

  • Live imaging of fluorescently tagged proteins in Drosophila embryos.
  • Analysis of kinetochore protein dynamics during mitosis.
  • Assessment of metaphase arrest in dynein mutants.

Main Results:

  • Dynamitin-GFP accumulates at prometaphase kinetochores and moves poleward.
  • This dynamic behavior is shared by metaphase checkpoint proteins like Rough deal (Rod).
  • Dynein mutants cause Rod accumulation at kinetochores and prolong metaphase arrest.

Conclusions:

  • Kinetochore dynein-dynactin facilitates the removal of checkpoint proteins from correctly attached kinetochores.
  • This removal by dynein is essential for timely SAC silencing.
  • Dynein-mediated transport contributes to the metaphase-to-anaphase transition.

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