ArticleStructure (London, England : 1993)2015
Structural insights into Ca2+-calmodulin regulation of Plectin 1a-integrin β4 interaction in hemidesmosomes.
Article in Structure (London, England : 1993), 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed, 30 citations in OpenAlex.
- Neurogranin-MYH9 interaction regulates cytoskeletal remodeling in cerebral vasculature.Fluids and barriers of the CNS · 2025Article
- Mechanics of cell sheets: plectin as an integrator of cytoskeletal networks.Open biology · 2025Review
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- Vasculature atrophy causes a stiffened microenvironment that augments epidermal stem cell differentiation in aged skin.Nature aging · 2022Article
- β-III-spectrin N-terminus is required for high-affinity actin binding and SCA5 neurotoxicity.Scientific reports · 2022Article
- Review
- Article
- Unbiased peptoid combinatorial cell screen identifies plectin protein as a potential biomarker for lung cancer stem cells.Scientific reports · 2019Article
- Plectin protects podocytes from adriamycin-induced apoptosis and F-actin cytoskeletal disruption through the integrin α6β4/FAK/p38 MAPK pathway.Journal of cellular and molecular medicine · 2018Article
- Structural basis of the filamin A actin-binding domain interaction with F-actin.Nature structural & molecular biology · 2018Article
- Reply to 'Defining distance restraints in HADDOCK'.Nature protocols · 2018Article
- Structural prediction of protein models using distance restraints derived from cross-linking mass spectrometry data.Nature protocols · 2018Article
- Ensemblator v3: Robust atom-level comparative analyses and classification of protein structure ensembles.Protein science : a publication of the Protein Society · 2018Article
- Structural basis for high-affinity actin binding revealed by a β-III-spectrin SCA5 missense mutation.Nature communications · 2017Article
- Structural insights into cargo recognition by the yeast PTS1 receptor.The Journal of biological chemistry · 2015Article
- Ca2+ signaling in cytoskeletal reorganization, cell migration, and cancer metastasis.BioMed research international · 2015Review
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Authors and funding
12 authors at 5 institutions in 4 countries.
Funding
Abstract
The mechanical stability of epithelial cells, which protect organisms from harmful external factors, is maintained by hemidesmosomes via the interaction between plectin 1a (P1a) and integrin α6β4. Binding of calcium-calmodulin (Ca(2+)-CaM) to P1a together with phosphorylation of integrin β4 disrupts this complex, resulting in disassembly of hemidesmosomes. We present structures of the P1a actin binding domain either in complex with the N-ter lobe of Ca(2+)-CaM or with the first pair of integrin β4 fibronectin domains. Ca(2+)-CaM binds to the N-ter isoform-specific tail of P1a in a unique manner, via its N-ter lobe in an extended conformation. Structural, cell biology, and biochemical studies suggest the following model: binding of Ca(2+)-CaM to an intrinsically disordered N-ter segment of plectin converts it to an α helix, which repositions calmodulin to displace integrin β4 by steric repulsion. This model could serve as a blueprint for studies aimed at understanding how Ca(2+)-CaM or EF-hand motifs regulate F-actin-based cytoskeleton.
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