ArticleThe Journal of cell biology1988
Cytoskeleton-associated plectin: in situ localization, in vitro reconstitution, and binding to immobilized intermediate filament proteins.
Article in The Journal of cell biology, 1988. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 54 papers.
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Who cites it
54 citing papers in PubMed, 162 citations in OpenAlex.
- Plectin affects cell viscoelasticity at small and large deformations.Biophysical journal · 2026Article
- Phosphorylation of plectin by Akt3 promotes triple-negative breast cancer cell invasive migration.iScience · 2025Article
- Optogenetic and chemical genetic tools for rapid repositioning of vimentin intermediate filaments.The Journal of cell biology · 2025Article
- Mechanics of cell sheets: plectin as an integrator of cytoskeletal networks.Open biology · 2025Review
- Intermediate filament dysregulation in astrocytes in the human disease model ofMolecular biology of the cell · 2023Article
- Intermediate filament dysregulation and astrocytopathy in the human disease model ofbioRxiv : the preprint server for biology · 2023Article
- Review
- The vimentin cytoskeleton: when polymer physics meets cell biology.Physical biology · 2020Article
- Vimentin Diversity in Health and Disease.Cells · 2018Review
- Complexes of α6β4 integrin and vimentin act as signaling hubs to regulate epithelial cell migration.Journal of cell science · 2018Article
- Intermediate Filaments and the Plasma Membrane.Cold Spring Harbor perspectives in biology · 2017Review
- Intermediate Filaments: Structure and Assembly.Cold Spring Harbor perspectives in biology · 2016Review
- Article
- Stress Conditions Increase Vimentin Cleavage by Omi/HtrA2 Protease in Human Primary Neurons and Differentiated Neuroblastoma Cells.Molecular neurobiology · 2015Article
- Plakins, a versatile family of cytolinkers: roles in skin integrity and in human diseases.The Journal of investigative dermatology · 2014Review
- Plectin-intermediate filament partnership in skin, skeletal muscle, and peripheral nerve.Histochemistry and cell biology · 2013Review
- The muscle dystrophy-causing ΔK32 lamin A/C mutant does not impair the functions of the nucleoplasmic lamin-A/C-LAP2α complex in mice.Journal of cell science · 2013Article
- Mathematical modeling of the impact of actin and keratin filaments on keratinocyte cell spreading.Biophysical journal · 2012Article
- Article
- The structure of the plakin domain of plectin reveals a non-canonical SH3 domain interacting with its fourth spectrin repeat.The Journal of biological chemistry · 2011Article
Corrections and comments
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The association and interaction of plectin (Mr 300,000) with intermediate filaments and filament subunit proteins were studied. Immunoelectron microscopy of whole mount cytoskeletons from various cultured cell lines (rat glioma C6, mouse BALB/c 3T3, and Chinese hamster ovary) and quick-frozen, deep-etched replicas of Triton X-100-extracted rat embryo fibroblast cells revealed that plectin was primarily located at junction sites and branching points of intermediate filaments. These results were corroborated by in vitro recombination studies using vimentin and plectin purified from C6 cells. Filaments assembled from mixtures of both proteins were extensively crosslinked by oligomeric plectin structures, as demonstrated by electron microscopy of negatively stained and rotary-shadowed specimens as well as by immunoelectron microscopy; the binding of plectin structures on the surface of filaments and cross-link formation occurred without apparent periodicity. Plectin's cross-linking of reconstituted filaments was also shown by ultracentrifugation experiments. As revealed by the rotary-shadowing technique, filament-bound plectin structures were oligomeric and predominantly consisted of a central globular core region of 30-50 nm with extending filaments or filamentous loops. Solid-phase binding to proteolytically degraded vimentin fragments suggested that plectin interacts with the helical rod domain of vimentin, a highly conserved structural element of all intermediate filament proteins. Accordingly, plectin was found to bind to the glial fibrillar acidic protein, the three neurofilament polypeptides, and skin keratins. These results suggest that plectin is a cross-linker of vimentin filaments and possibly also of other intermediate filament types.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.