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A more recent version of this article appeared on April 1, 2003
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Submitted on August 29, 2002
Revised on November 24, 2002
Accepted on December 9, 2002
1 Department of Cell and Molecular Biology, Northwestern University,
303 East Chicago Avenue, Chicago, IL 60611, USA
2 Department for Cell Biology, German Cancer Research Center, D-69120
Heidelberg, Germany
* Corresponding author. E-mail address: r-goldman{at}northwestern.edu.
The expression of the intermediate filament (IF) protein, nestin, is closely associated with rapidly proliferating progenitor cells during neurogenesis and myogenesis but little is known about its function. In this study, we examine the effects of nestin expression on the assembly state of vimentin IF in nestin-free cells. Nestin is introduced by transient transfection and is positively correlated with the disassembly of vimentin IF into non-filamentous aggregates or particles in mitotic, but not interphase cells. This nestin-mediated disassembly of IF is dependent on the phosphorylation of vimentin by the maturation/M-phase promoting factor at ser-55 in the amino-terminal head domain. In addition, the disassembly of vimentin IF during mitosis appears to be a unique feature of nestin-expressing cell types. Furthermore, when the expression of nestin is down-regulated by the nestin-specific siRNA in nestin expressing cells, vimentin IF remain assembled throughout all stages of mitosis. Previous studies suggest that non-filamentous vimentin particles are IF precursors and can be transported rapidly between different cytoplasmic compartments along microtubule tracks. Based upon these observations, we speculate that nestin may play a role in the trafficking and distribution of IF proteins and potentially other cellular factors to daughter cells during progenitor cell division.
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