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

Authors
  • Wojcik, E1
  • Basto, R
  • Serr, M
  • Scaërou, F
  • Karess, R
  • Hays, T
  • 1 Virginia Tech University, Department of Biology, Blacksburg, Virginia 24061, USA. [email protected]
Type
Published Article
Journal
Nature cell biology
Publication Date
Nov 01, 2001
Volume
3
Issue
11
Pages
1001–1007
Identifiers
PMID: 11715021
Source
Medline
License
Unknown

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.

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