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Vimentin filament organization and stress sensing depend on its single cysteine residue and zinc binding

AutorPérez-Sala, Dolores ; Oeste, Clara L. ; Martínez, Alma E.; Carrasco, María Jesús; Garzón, Beatriz; Cañada, F. Javier
Fecha de publicación2-jun-2015
EditorNature Publishing Group
CitaciónNature Communications 6: 7287 (2015)
ResumenThe vimentin filament network plays a key role in cell architecture and signalling, as well as in epithelial–mesenchymal transition. Vimentin C328 is targeted by various oxidative modifications, but its role in vimentin organization is not known. Here we show that C328 is essential for vimentin network reorganization in response to oxidants and electrophiles, and is required for optimal vimentin performance in network expansion, lysosomal distribution and aggresome formation. C328 may fulfil these roles through interaction with zinc. In vitro, micromolar zinc protects vimentin from iodoacetamide modification and elicits vimentin polymerization into optically detectable structures; in cells, zinc closely associates with vimentin and its depletion causes reversible filament disassembly. Finally, zinc transportdeficient human fibroblasts show increased vimentin solubility and susceptibility to disruption, which are restored by zinc supplementation. These results unveil a critical role of C328 in vimentin organization and open new perspectives for the regulation of intermediate filaments by zinc. DOI: 10.1038/ncomms8287 OPEN 1
Descripción17 pág., 10 figs.
Versión del editorhttp://dx.doi.org/10.1038/ncomms8287
URIhttp://hdl.handle.net/10261/118350
DOI10.1038/ncomms8287
ISSN2041-1723
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