ArticleThe Journal of cell biology1985
The binding of vimentin to human erythrocyte membranes: a model system for the study of intermediate filament-membrane interactions.
Article in The Journal of cell biology, 1985. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.
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Who cites it
29 citing papers in PubMed, 129 citations in OpenAlex.
- TheFrontiers in cellular and infection microbiology · 2020Article
- A rim-and-spoke hypothesis to explain the biomechanical roles for cytoplasmic intermediate filament networks.Journal of cell science · 2017Review
- Lens ion homeostasis relies on the assembly and/or stability of large connexin 46 gap junction plaques on the broad sides of differentiating fiber cells.American journal of physiology. Cell physiology · 2015Article
- Lipid droplets, perilipins and cytokeratins--unravelled liaisons in epithelium-derived cells.PloS one · 2013Article
- Article
- Inhibition of glucocorticoid-induced alteration of vimentin by a glucocorticoid receptor antagonist RU486 in the organ-cultured rat lens.Molecular vision · 2011Article
- Splice variant-specific interaction of the NMDA receptor subunit NR1 with neuronal intermediate filaments.The Journal of neuroscience : the official journal of the Society for Neuroscience · 1998Article
- Small, membrane-bound, alternatively spliced forms of ankyrin 1 associated with the sarcoplasmic reticulum of mammalian skeletal muscle.The Journal of cell biology · 1997Article
- Molecular composition of the node of Ranvier: identification of ankyrin-binding cell adhesion molecules neurofascin (mucin+/third FNIII domain-) and NrCAM at nodal axon segments.The Journal of cell biology · 1996Article
- Expression of vimentin in cultured human keratinocytes is associated with cell - extracellular matrix junctions.Archives of dermatological research · 1996Article
- Ank3 (epithelial ankyrin), a widely distributed new member of the ankyrin gene family and the major ankyrin in kidney, is expressed in alternatively spliced forms, including forms that lack the repeat domain.The Journal of cell biology · 1995Article
- The cytoplasmic tail of CD44 is required for basolateral localization in epithelial MDCK cells but does not mediate association with the detergent-insoluble cytoskeleton of fibroblasts.The Journal of cell biology · 1993Article
- Host cell factors controlling vimentin organization in the Xenopus oocyte.The Journal of cell biology · 1992Article
- Changing patterns in cytoskeletal mRNA expression and protein synthesis during murine erythropoiesis in vivo.Proceedings of the National Academy of Sciences of the United States of America · 1992Article
- Restin: a novel intermediate filament-associated protein highly expressed in the Reed-Sternberg cells of Hodgkin's disease.The EMBO journal · 1992Article
- Interaction domains of neurofilament light chain and brain spectrin.The Biochemical journal · 1991Article
- Assembly of amino-terminally deleted desmin in vimentin-free cells.The Journal of cell biology · 1990Article
- A protein antigenically related to nuclear lamin B mediates the association of intermediate filaments with desmosomes.The Journal of cell biology · 1990Article
- Presence of a protein immunologically related to lamin B in the postsynaptic membrane of Torpedo marmorata electrocyte.The Journal of cell biology · 1989Article
- Overexpression of the vimentin gene in transgenic mice inhibits normal lens cell differentiation.The Journal of cell biology · 1989Article
Corrections and comments
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Authors and funding
2 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
We have characterized the association of the intermediate filament protein, vimentin, with the plasma membrane, using radioiodinated lens vimentin and various preparations of human erythrocyte membrane vesicles. Inside-out membrane vesicles (IOVs), depleted of spectrin and actin, bind I125-vimentin in a saturable manner unlike resealed, right-side-out membranes which bind negligible amounts of vimentin in an unsaturable fashion. The binding of vimentin to IOVs is abolished by trypsin or acid treatment of the vesicles. Extraction of protein 4.1 or reconstitution of the membranes with purified spectrin do not basically affect the association. However, removal of ankyrin (band 2.1) significantly lowers the binding. Upon reconstitution of depleted vesicles with purified ankyrin, the vimentin binding function is restored. If ankyrin is added in excess the binding of vimentin to IOVs is quantitatively inhibited, whereas protein 4.1, the cytoplasmic fragment of band 3, band 6, band 4.5 (catalase), or bovine serum albumin do not influence it. Preincubation of the IOVs with a polyclonal anti-ankyrin antibody blocks 90% of the binding. Preimmune sera and antibodies against spectrin, protein 4.1, glycophorin A, and band 3 exhibit no effect. On the basis of these data, we propose that vimentin is able to associate specifically with the erythrocyte membrane skeleton and that ankyrin constitutes its major attachment site.
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