ArticleThe Journal of cell biology1990
A protein antigenically related to nuclear lamin B mediates the association of intermediate filaments with desmosomes.
Article in The Journal of cell biology, 1990. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 46 citations in OpenAlex.
- Desmin cytoskeleton in healthy and failing heart.Heart failure reviews · 2000Review
- IFAP 300 is common to desmosomes and hemidesmosomes and is a possible linker of intermediate filaments to these junctions.The Journal of cell biology · 1994Article
- Regulated docking of nuclear membrane vesicles to vimentin filaments during mitosis.The Journal of cell biology · 1993Article
- Host cell factors controlling vimentin organization in the Xenopus oocyte.The Journal of cell biology · 1992Article
- Identification of an epithelial protein related to the desmosome and intermediate filament network.The Journal of cell biology · 1992Article
- The desmoplakin carboxyl terminus coaligns with and specifically disrupts intermediate filament networks when expressed in cultured cells.The Journal of cell biology · 1992Article
- Filensin: a new vimentin-binding, polymerization-competent, and membrane-associated protein of the lens fiber cell.The Journal of cell biology · 1991Article
- Integrin alpha 6/beta 4 complex is located in hemidesmosomes, suggesting a major role in epidermal cell-basement membrane adhesion.The Journal of cell biology · 1991Article
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Desmosomes are specialized domains of epithelial cell plasma membranes engaged in the anchoring of intermediate filaments (IF). So far, the desmosomal component(s) responsible for this binding has not been unambiguously identified. In the present work, we have examined bovine muzzle epidermis desmosomes for the presence of protein(s) structurally and functionally related to lamin B, the major receptor for IF in the nuclear envelope (Georgatos, S. D., and G. Blobel. 1987. J. Cell Biol. 105:105-115). By using polyclonal antibodies to lamin B in immunoblotting experiments, we find that a desmosomal protein of 140-kD shares epitope(s) with lamin B. Immunoelectron microscopic and urea extraction experiments show that this protein is a peripheral protein localized at the cytoplasmic side of the desmosomes (desmosomal plaques). Furthermore, this protein binds vimentin in an in vitro assay. Since this binding is inhibited by lamin B antibodies, the epitopes common to the 140-kD protein and to lamin B may be responsible for anchoring of intermediate filaments to desmosomes. These data suggest that lamin B-related proteins (see also Cartaud, A., J. C. Courvalin, M. A. Ludosky, and J. Cartaud. 1989. J. Cell Biol. 109:1745-1752) together with lamin B, provide cells with several nucleation sites, which can account for the multiplicity of IF organization in tissues.
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