ArticleMolecular biology of the cell2003
Interaction of the bullous pemphigoid antigen 1 (BP230) and desmoplakin with intermediate filaments is mediated by distinct sequences within their COOH terminus.
Article in Molecular biology of the cell, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 42 papers.
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Who cites it
42 citing papers in PubMed, 106 citations in OpenAlex.
- Plakoglobin phosphorylation at serine 665 is capable of stabilizing cadherin-mediated adhesion in keratinocytes.JCI insight · 2026Article
- Revisiting the human umbilical cord epithelium. An atypical epithelial sheath with distinctive features.Cell and tissue research · 2024Article
- Desmoplakin CSM models unravel mechanisms regulating the binding to intermediate filaments and putative therapeutics for cardiocutaneous diseases.Scientific reports · 2024Article
- How cytoskeletal crosstalk makes cells move: Bridging cell-free and cell studies.Biophysics reviews · 2024Review
- 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
- The cytokine milieu of bullous pemphigoid: Current and novel therapeutic targets.Frontiers in medicine · 2023Review
- Deciphering the Contribution of BP230 Autoantibodies in Bullous Pemphigoid.Antibodies (Basel, Switzerland) · 2022Review
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- Missense Mutations in Desmoplakin Plakin Repeat Domains Have Dramatic Effects on Domain Structure and Function.International journal of molecular sciences · 2022Article
- Insights Into the Pathogenesis of Bullous Pemphigoid: The Role of Complement-Independent Mechanisms.Frontiers in immunology · 2022Review
- Hemidesmosome-Related Keratin Filament Bundling and Nucleation.International journal of molecular sciences · 2021Article
- Strength Through Unity: The Power of the Mega-Scaffold MACF1.Frontiers in cell and developmental biology · 2021Review
- Binding of the periplakin linker requires vimentin acidic residues D176 and E187.Communications biology · 2020Article
- The keratin-desmosome scaffold: pivotal role of desmosomes for keratin network morphogenesis.Cellular and molecular life sciences : CMLS · 2020Article
- Article
- Article
- Spectraplakin family proteins - cytoskeletal crosslinkers with versatile roles.Journal of cell science · 2017Review
- Desmosomes and Intermediate Filaments: Their Consequences for Tissue Mechanics.Cold Spring Harbor perspectives in biology · 2017Review
- Epidermolytic Ichthyosis Sine Epidermolysis.The American Journal of dermatopathology · 2017Article
- Intermediate Filaments and the Plasma Membrane.Cold Spring Harbor perspectives in biology · 2017Review
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Authors and funding
9 authors at 3 institutions in 3 countries.
Funding
Abstract
The bullous pemphigoid antigen 1 (BP230) and desmoplakin (DP) are members of the plakin protein family of cytolinkers. Despite their homology, their COOH termini selectively bind distinct intermediate filaments (IFs). We studied sequences within their COOH termini required for their interaction with the epidermal keratins K5/K14, the simple epithelial keratins K8/K18, and type III IF vimentin by yeast three-hybrid, cell transfection, and overlay assays. The results indicate that BP230 interacts with K5/K14 but not with K8/K18 or vimentin via a region encompassing both the B and C subdomains and the COOH extremity, including a COOH-terminal eight-amino-acid stretch. In contrast, the C subdomain with the COOH-terminal extremity of DP interacts with K5/K14 and K8/K18, and its linker region is able to associate with K8/K18 and vimentin. Furthermore, the potential of DP to interact with IF proteins in yeast seems to be regulated by phosphorylation of Ser 2849 within its COOH terminus. Strikingly, BP230 and DP interacted with cytokeratins only when both type I and type II keratins were present. The head and tail domains of K5/K14 keratins were dispensable for their interaction with BP230 or DP. On the basis of our findings, we postulate that (1) the binding specificity of plakins for various IF proteins depends on their linker region between the highly homologous B and C subdomains and their COOH extremity and (2) the association of DP and BP230 with both epidermal and simple keratins is critically affected by the tertiary structure induced by heterodimerization and involves recognition sites located primarily in the rod domain of these keratins.
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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.