Overcoming the “resolution gap”: combination of super-resolution microscopy and cryo-electron tomography for mitochondria-vimentin binding sites identification

Progress in fundamental research is directly related to the emergence of new research methods that not only expand the established classical concepts, but can provide information that fundamentally changes them. According to our data, vimentin filaments, binding to mitochondria, determine their distribution and mobility in cells, affect the level of their membrane potential, there is a region responsible for the interaction of vimentin filaments with mitochondria in the N-terminal part of the vimentin molecule and similar amino acid sequences are found in other proteins, for example, in desmin. Since direct interaction of vimentin filaments with microtubules and actin filaments has already been shown, these facts together allowed us to assume that the connection of individual cytoskeleton components with each other and with mitochondria is not limited to interaction through cross-linker and motor proteins. Vimentin (and possibly other intermediate filament proteins) can regulate cytoskeletal interactions with mitochondria. A revolutionary study performed using cryo-electron tomography and fundamentally changing our understanding of the three-dimensional structure of vimentin filaments motivated us to use the capabilities of the cryo-electron microscopy method to try to identify the binding sites of vimentin with other cytoskeletal components and mitochondria. To meet this challenge is fundamentally possible if we combine super-resolution microscopy and cryo-electron tomography, which will bridge the existing “resolution gap” and solve associated problems.

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