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Preprint Highlight: Vimentin intermediate filaments organize organellar ER architecture in response to stress.

Organelle trafficking responds to nutritional and homeostatic cues and is facilitated by cytoskeletal and motor proteins. However, the mechanisms that control organelle retention at a given position are poorly understood. The authors identify the intermediate filament protein vimentin as the key player in the perinuclear retention of ER membranes and endolysosomes upon stress. Using quantitative microscopy, proximity biotinylation, and other biochemistry techniques, they show that vimentin interacts with the ER ubiquitin ligase RNF26 at the perinuclear region, anchoring the ER and its interacting endolysosome network at this location. These findings reveal a previously unappreciated function of vimentin and intermediate cytoskeletal filaments in organelle positioning and highlight the importance of organelle dynamics and cross-talk in the stress response.