Kinetochore dynein: its dynamics and role in the transport of the Rough deal checkpoint protein
Author: ["Edward Wojcik","Renata Basto","Madeline Serr","Frédéric Scaërou","Roger Karess","Thomas Hays"]
Publication: Nature Cell Biology
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Abstract
We describe the dynamics of kinetochore dynein–dynactin in living Drosophila embryos and examine the effect of mutant dynein on the metaphase checkpoint. A functional conjugate of dynamitin with green fluorescent protein accumulates rapidly at prometaphase kinetochores, and subsequently migrates off kinetochores towards the poles during late prometaphase and metaphase. This behaviour is seen for several metaphase checkpoint proteins, including Rough deal (Rod). In neuroblasts, hypomorphic dynein mutants accumulate in metaphase and block the normal redistribution of Rod from kinetochores to microtubules. By transporting checkpoint proteins away from correctly attached kinetochores, dynein might contribute to shutting off the metaphase checkpoint, allowing anaphase to ensue.
Cite this article
Wojcik, E., Basto, R., Serr, M. et al. Kinetochore dynein: its dynamics and role in the transport of the Rough deal checkpoint protein. Nat Cell Biol 3, 1001–1007 (2001). https://doi.org/10.1038/ncb1101-1001