Journal of cell scienceJul 27, 2026

Vimentin filaments help form cell cleaning structures at contact points between energy and recycling systems during starvation

Longevity & Aging Weekly Brief ↗PubMed ↗DOI ↗

Updated Aug 3, 2026

Abstract

Starvation induces a rapid, perinuclear compaction of vimentin intermediate filaments.

Vimentin intermediate filaments show enhanced overlap with the endoplasmic reticulum during starvation.
This overlap is associated with transient phosphorylation of vimentin at serine 56.
Autophagic proteins accumulate at the interface between vimentin and the endoplasmic reticulum, linking autophagosome formation processes.
Disruption of vimentin dynamics through knockout or drug treatment significantly impairs autophagy triggered by starvation.
Vimentin intermediate filaments are identified as crucial coordinators for the mobilization of endosome-ER membrane contact sites, essential for autophagosome formation.

Simplified

Macroautophagy (autophagy) is a fundamental catabolic process requiring the biogenesis of the autophagosome to support cell survival during stress. Although the roles of F-actin and microtubule cytoskeleton in autophagy are well established, the contribution of intermediate filaments (IFs) remains poorly understood. Here, we investigated the role of the type III IF vimentin in supporting the early steps of starvation-induced autophagy. We demonstrate that starvation triggers a rapid, perinuclear compaction of vimentin IFs, which showed enhanced overlap with the endoplasmic reticulum (ER) and correlated with transient vimentin phosphorylation at serine 56. We reveal that autophagic proteins accumulate at the vimentin-ER interface, physically connecting the autophagosome biogenesis machinery to the vimentin IF network. Knockout or pharmacological perturbation of vimentin-IFs dynamics using withaferin-A significantly impairs starvation-induced autophagic flux. Mechanistically, we reveal that vimentin IFs are essential coordinators for the mobilization of endosome-ER membrane contact sites (EERCS), a crucial hub for autophagosome nucleation. Together, our findings uncover a novel role for vimentin IFs as a dynamic cytoskeletal coordinator that spatially organizes membrane contact sites to promote the efficient initiation of autophagosome biogenesis in response to nutrient stress.

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Vimentin filaments help form cell cleaning structures at contact points between energy and recycling systems during starvation

Abstract

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