ArticleThe Journal of cell biology1993
Functional analysis of desmoplakin domains: specification of the interaction with keratin versus vimentin intermediate filament networks.
Article in The Journal of cell biology, 1993. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 55 papers.
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Who cites it
55 citing papers in PubMed, 181 citations in OpenAlex.
- Desmoplakin Mutations in Cardiac Fibroblasts Cause TGFβ1-Mediated Pathological Fibrogenesis in Desmoplakin Cardiomyopathy Via Beclin-1 Regulation.Circulation research · 2026Article
- Desmosomes compartmentalize mRNA and translation in the skin.Developmental cell · 2026Article
- Actomyosin forces trigger a conformational change in desmoplakin within desmosomes.Nature communications · 2025Article
- A truncating variant altering the extreme C-terminal region of desmoplakin (DSP) suggests the crucial functional role of the region: a case report study.BMC medical genomics · 2023Article
- Vimentin and cytokeratin: Good alone, bad together.Seminars in cancer biology · 2022Review
- Roles for Ndel1 in keratin organization and desmosome function.Molecular biology of the cell · 2021Article
- Hemidesmosome-Related Keratin Filament Bundling and Nucleation.International journal of molecular sciences · 2021Article
- Binding of the periplakin linker requires vimentin acidic residues D176 and E187.Communications biology · 2020Article
- Mechanical loading of desmosomes depends on the magnitude and orientation of external stress.Nature communications · 2018Article
- Article
- A rim-and-spoke hypothesis to explain the biomechanical roles for cytoplasmic intermediate filament networks.Journal of cell science · 2017Review
- Mechanism of intermediate filament recognition by plakin repeat domains revealed by envoplakin targeting of vimentin.Nature communications · 2016Article
- Cell adhesion in epidermal development and barrier formation.Current topics in developmental biology · 2015Review
- Interaction of plectin with keratins 5 and 14: dependence on several plectin domains and keratin quaternary structure.The Journal of investigative dermatology · 2014Article
- Disease mutations in desmoplakin inhibit Cx43 membrane targeting mediated by desmoplakin-EB1 interactions.The Journal of cell biology · 2014Article
- Directed expression of a chimeric type II keratin partially rescues keratin 5-null mice.The Journal of biological chemistry · 2014Article
- Mechanistic basis of desmosome-targeted diseases.Journal of molecular biology · 2013Review
- Spectraplakins: master orchestrators of cytoskeletal dynamics.The Journal of cell biology · 2012Review
- Vimentin in cancer and its potential as a molecular target for cancer therapy.Cellular and molecular life sciences : CMLS · 2011Review
- Insights from a desmoplakin mutation identified in lethal acantholytic epidermolysis bullosa.The Journal of investigative dermatology · 2010Article
Corrections and comments
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
Abstract
We previously demonstrated that truncated desmoplakin I (DP I) molecules containing the carboxyl terminus specifically coalign with and disrupt both keratin and vimentin intermediate filament (IF) networks when overexpressed in tissue culture cells (Stappenbeck, T. S., and K. J. Green. J. Cell Biol. 116:1197-1209). These experiments suggested that the DP carboxyl-terminal domain is involved either directly or indirectly in linking IF with the desmosome. Using a similar approach, we have now investigated the behavior of ectopically expressed full-length DP I in cultured cells. In addition, we have further dissected the functional sequences in the carboxyl terminus of DP I that facilitate the interaction with IF networks. Transient transfection of a clone encoding full-length DP I into COS-7 cells produced protein that appeared in some cells to associate with desmosomes and in others to coalign with and disrupt IF. Deletion of the carboxyl terminus from this clone resulted in protein that still appeared capable of associating with desmosomes but not interacting with IF networks. As the amino terminus appeared to be dispensable for IF interaction, we made finer deletions in the carboxyl terminus of DP based on blocks of sequence similarity with the related molecules bullous pemphigoid antigen and plectin. We found a sequence at the very carboxyl terminus of DP that was necessary for coalignment with and disruption of keratin IF but not vimentin IF. Furthermore, the coalignment of specific DP proteins along keratin IF but not vimentin IF was correlated with resistance to extraction by Triton. The striking uncoupling resulting from the deletion of specific DP sequences suggests that the carboxyl terminus of DP interacts differentially with keratin and vimentin IF networks.
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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.