Molecular organization and mechanics of single vimentin filaments revealed by super-resolution imaging

Intermediate filaments (IFs) are involved in key cellular functions including polarization, migration, and protection against large deformations. These functions are related to their remarkable ability to extend without breaking, a capacity that should be determined by the molecular organization of subunits within filaments. However, this structure-mechanics relationship remains poorly understood at the molecular level. Here, using super-resolution microscopy (SRM), we show that vimentin filaments exhibit a similar to 49-nanometer axial repeat both in cells and in vitro. As unit-length filaments (ULFs) were measured at similar to 59 nanometers, this demonstrates a partial overlap of ULFs during filament assembly. Using an SRM-compatible stretching device, we also provide evidence that the extensibility of vimentin is due to the unfolding of its subunits and not to their sliding, thus establishing a direct link between the structural organization and its mechanical properties. Overall, our results pave the way for future studies of IF assembly, mechanical, and structural properties in cells.

Automated summary

Intermediate filaments play key roles in cellular functions and their mechanical properties. This study used super-resolution microscopy to reveal the molecular organization of vimentin filaments and provided evidence for the partial overlap of subunits during filament assembly. The researchers also found that the extensibility of vimentin is due to the unfolding of its subunits, establishing a direct link between structure and mechanics.