Nestin promotes the phosphorylation-dependent disassembly of vimentin intermediate filaments during mitosis

Department of Cell and Molecular Biology, Northwestern University, 303 East Chicago Avenue, Chicago, IL 60611, USA.
Molecular Biology of the Cell (Impact Factor: 4.47). 05/2003; 14(4):1468-78. DOI: 10.1091/mbc.E02-08-0545
Source: PubMed


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 IFs in nestin-free cells. Nestin is introduced by transient transfection and is positively correlated with the disassembly of vimentin IFs into nonfilamentous aggregates or particles in mitotic but not interphase cells. This nestin-mediated disassembly of IFs 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 IFs during mitosis appears to be a unique feature of nestin-expressing cell types. Furthermore, when the expression of nestin is downregulated by the nestin-specific small interfering RNA in nestin-expressing cells, vimentin IFs remain assembled throughout all stages of mitosis. Previous studies suggest that nonfilamentous vimentin particles are IF precursors and can be transported rapidly between different cytoplasmic compartments along microtubule tracks. On the basis of 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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Available from: Harald Herrmann, Jan 29, 2015
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    • "Nestin interacts with other IF proteins including vimentin, desmin, and synemin to form heterodimers and mixed polymers [9] [10] [11] [12]. Vimentin is a major partner for nestin, and nestin regulates the reorganization, disassembly , and phosphorylation of vimentin during mitosis [13]. Copolymers of nestin and vimentin serve as scaffolds for glucocorticoid receptor molecules [14]. "
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    • "Recent studies have revealed vimentin as highly dynamic polymer, with three types of structures (granules, squiggles, and filaments) coexisting in the cell. Particularly vimentin IF varies in the form of granules and squiggles and have an important role in the assembly and disassembly of IF networks [51]. Vimentin is involved in many important physiological functions, such as signal transduction, gene regulation and distributions of organelles [52]. "
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