ArticlePloS one2016
Structure of the Intermediate Filament-Binding Region of Desmoplakin.
Article in PloS one, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 26 citations in OpenAlex.
- Desmosomes compartmentalize mRNA and translation in the skin.Developmental cell · 2026Article
- Prevention of Protease-Induced Degradation of Desmoplakin via Small Molecule Binding.Journal of personalized medicine · 2024Article
- Challenges and Opportunities in the Oral Delivery of Recombinant Biologics.Pharmaceutics · 2023Review
- Missense Mutations in Desmoplakin Plakin Repeat Domains Have Dramatic Effects on Domain Structure and Function.International journal of molecular sciences · 2022Article
- Desmogleins 1, 3, and E-cadherin immunohistochemical expression within mucocutaneous pemphigus vulgaris.The Pan African medical journal · 2022Article
- Insights Into Genetics and Pathophysiology of Arrhythmogenic Cardiomyopathy.Current heart failure reports · 2021Review
- The attributes of plakins in cancer and disease: perspectives on ovarian cancer progression, chemoresistance and recurrence.Cell communication and signaling : CCS · 2021Review
- Recent insight into intermediate filament structure.Current opinion in cell biology · 2021Review
- Binding of the periplakin linker requires vimentin acidic residues D176 and E187.Communications biology · 2020Article
- Biomedical potential of mammalian spectraplakin proteins: Progress and prospect.Experimental biology and medicine (Maywood, N.J.) · 2019Review
- A rim-and-spoke hypothesis to explain the biomechanical roles for cytoplasmic intermediate filament networks.Journal of cell science · 2017Review
- Desmosomes and Intermediate Filaments: Their Consequences for Tissue Mechanics.Cold Spring Harbor perspectives in biology · 2017Review
Corrections and comments
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Authors and funding
5 authors at 3 institutions in 2 countries.
Funding
Abstract
Desmoplakin (DP) is a cytoskeletal linker protein that connects the desmosomal cadherin/plakoglobin/plakophilin complex to intermediate filaments (IFs). The C-terminal region of DP (DPCT) mediates IF binding, and contains three plakin repeat domains (PRDs), termed PRD-A, PRD-B and PRD-C. Previous crystal structures of PRDs B and C revealed that each is formed by 4.5 copies of a plakin repeat (PR) and has a conserved positively charged groove on its surface. Although PRDs A and B are linked by just four amino acids, B and C are separated by a 154 residue flexible linker, which has hindered crystallographic analysis of the full DPCT. Here we present the crystal structure of a DPCT fragment spanning PRDs A and B, and elucidate the overall architecture of DPCT by small angle X-ray scattering (SAXS) analysis. The structure of PRD-A is similar to that of PRD-B, and the two domains are arranged in a quasi-linear arrangement, and separated by a 4 amino acid linker. Analysis of the B-C linker region using secondary structure prediction and the crystal structure of a homologous linker from the cytolinker periplakin suggests that the N-terminal ~100 amino acids of the linker form two PR-like motifs. SAXS analysis of DPCT indicates an elongated but non-linear shape with Rg = 51.5 Å and Dmax = 178 Å. These data provide the first structural insights into an IF binding protein containing multiple PRDs and provide a foundation for studying the molecular basis of DP-IF interactions.
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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.