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

CITE.CC academic search helps you expand the influence of your papers.

Tags:  general   CellBiology   CancerResearch   DevelopmentalBiology   StemCells   Biological

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

View full text

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

Regulation of microglial expression of integrins by poly(ADP-ribose) polymerase-1

A new phospholipase-C–calcium signalling pathway mediated by cyclic AMP and a Rap GTPase