ArticleThe Journal of biological chemistry2016
The Structure of the Plakin Domain of Plectin Reveals an Extended Rod-like Shape.
Article in The Journal of biological chemistry, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.
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Who cites it
25 citing papers in PubMed, 54 citations in OpenAlex.
- Actomyosin forces trigger a conformational change in desmoplakin within desmosomes.Nature communications · 2025Article
- Identification ofJournal of medical genetics · 2025Article
- High matrix stiffness accelerates migration of hepatocellular carcinoma cells through the integrin β1-Plectin-F-actin axis.BMC biology · 2025Article
- Mechanics of cell sheets: plectin as an integrator of cytoskeletal networks.Open biology · 2025Review
- Homozygosity for a RareInternational journal of molecular sciences · 2024Article
- Structure-function analysis of PorXScientific reports · 2024Article
- Pathogen-specific structural features ofmBio · 2023Article
- Overall protein structure quality assessment using hydrogen-bonding parameters.Acta crystallographica. Section D, Structural biology · 2023Article
- Junctional epithelium and hemidesmosomes: Tape and rivets for solving the "percutaneous device dilemma" in dental and other permanent implants.Bioactive materials · 2022Review
- Ancient Origins of Cytoskeletal Crosstalk: Spectraplakin-like Proteins Precede the Emergence of Cortical Microtubule Stabilization Complexes as Crosslinkers.International journal of molecular sciences · 2022Article
- Epiplakin1 promotes the progression of esophageal squamous cell carcinoma by activating the PI3K-AKT signaling pathway.Thoracic cancer · 2022Article
- A novel peptidomimetic therapeutic for selective suppression of lung cancer stem cells over non-stem cancer cells.Bioorganic chemistry · 2021Article
- Review
- KLF5-mediated Eppk1 expression promotes cell proliferation in cervical cancer via the p38 signaling pathway.BMC cancer · 2021Article
- IM30 IDPs form a membrane-protective carpet upon super-complex disassembly.Communications biology · 2020Article
- The plakin domain ofDevelopment (Cambridge, England) · 2019Article
- [Research advances in limb-girdle muscular dystrophy type 2Q].Zhongguo dang dai er ke za zhi = Chinese journal of contemporary pediatrics · 2019Review
- Empirical and Computational Comparison of Alternative Therapeutic Exon Skip Repairs for Duchenne Muscular Dystrophy.Biochemistry · 2019Article
- Genetic regulation of methylation in human endometrium and blood and gene targets for reproductive diseases.Clinical epigenetics · 2019Article
- The dynamic nature of the conserved tegument protein UL37 of herpesviruses.The Journal of biological chemistry · 2018Article
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Authors and funding
7 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Plakins are large multi-domain proteins that interconnect cytoskeletal structures. Plectin is a prototypical plakin that tethers intermediate filaments to membrane-associated complexes. Most plakins contain a plakin domain formed by up to nine spectrin repeats (SR1-SR9) and an SH3 domain. The plakin domains of plectin and other plakins harbor binding sites for junctional proteins. We have combined x-ray crystallography with small angle x-ray scattering (SAXS) to elucidate the structure of the plakin domain of plectin, extending our previous analysis of the SR1 to SR5 region. Two crystal structures of the SR5-SR6 region allowed us to characterize its uniquely wide inter-repeat conformational variability. We also report the crystal structures of the SR7-SR8 region, refined to 1.8 Å, and the SR7-SR9 at lower resolution. The SR7-SR9 region, which is conserved in all other plakin domains, forms a rigid segment stabilized by uniquely extensive inter-repeat contacts mediated by unusually long helices in SR8 and SR9. Using SAXS we show that in solution the SR3-SR6 and SR7-SR9 regions are rod-like segments and that SR3-SR9 of plectin has an extended shape with a small central kink. Other plakins, such as bullous pemphigoid antigen 1 and microtubule and actin cross-linking factor 1, are likely to have similar extended plakin domains. In contrast, desmoplakin has a two-segment structure with a central flexible hinge. The continuous versus segmented structures of the plakin domains of plectin and desmoplakin give insight into how different plakins might respond to tension and transmit mechanical signals.
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