ArticleInternational journal of molecular sciences2020
Unidirectional Regulation of Vimentin Intermediate Filaments to Caveolin-1.
Article in International journal of molecular sciences, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 15 citations in OpenAlex.
- Targeting secreted PLACell death & disease · 2025Article
- Long-term zinc treatment alters the mechanical properties and metabolism of prostate cancer cells.Cancer cell international · 2024Article
- Discovery of Trametinib as an orchestrator for cytoskeletal vimentin remodeling.Journal of molecular cell biology · 2024Article
- The NLRP11 Protein Bridges the Histone Lysine Acetyltransferase KAT7 to Acetylate Vimentin in the Early Stage of Lung Adenocarcinoma.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2023Article
- Interactive mechanisms between caveolin-1 and actin filaments or vimentin intermediate filaments instruct cell mechanosensing and migration.Journal of molecular cell biology · 2023Article
- Caveolae Mechanotransduction at the Interface between Cytoskeleton and Extracellular Matrix.Cells · 2023Review
- Coronavirus and the Cytoskeleton of Virus-Infected Cells.Sub-cellular biochemistry · 2023Article
- Recent Advances in Intermediate Filaments-Volume 1.International journal of molecular sciences · 2022Article
- Article
- Feedback-Driven Mechanisms Between Phosphorylated Caveolin-1 and Contractile Actin Assemblies Instruct Persistent Cell Migration.Frontiers in cell and developmental biology · 2021Article
- Vimentin's side gig: Regulating cellular proteostasis in mammalian systems.Cytoskeleton (Hoboken, N.J.) · 2020Review
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Both the mechanosensitive vimentin cytoskeleton and endocytic caveolae contribute to various active processes such as cell migration, morphogenesis, and stress response. However, the crosstalk between these two systems has remained elusive. Here, we find that the subcellular expression between vimentin and caveolin-1 is mutual exclusive, and vimentin filaments physically arrest the cytoplasmic motility of caveolin-1 vesicles. Importantly, vimentin depletion increases the phosphorylation of caveolin-1 on site Tyr14, and restores the compromised cell migration rate and directionality caused by caveolin-1 deprivation. Moreover, upon hypo-osmotic shock, vimentin-knockout recovers the reduced intracellular motility of caveolin-1 vesicles. In contrary, caveolin-1 depletion shows no effect on the expression, phosphorylation (on sites Ser39, Ser56, and Ser83), distribution, solubility, and cellular dynamics of vimentin filaments. Taken together, our data reveals a unidirectional regulation of vimentin to caveolin-1, at least on the cellular level.
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Registered trials
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