ArticlePloS one2013
Large-scale modelling of the divergent spectrin repeats in nesprins: giant modular proteins.
Article in PloS one, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.
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Who cites it
26 citing papers in PubMed.
- Nuclear Lamins: A Molecular Bridge Coupling Extracellular Mechanical Cues to Intranuclear Signal Transduction and Gene Regulation.International journal of molecular sciences · 2026Review
- A distinct isoform of Msp300 (nesprin) organizes the perinuclear microtubule-organizing center in adipocytes.Molecular biology of the cell · 2025Article
- Article
- Apoptosis-induced translocation of nesprin-2 from the nuclear envelope to mitochondria is associated with mitochondrial dysfunction.Nucleus (Austin, Tex.) · 2024Article
- Exome sequencing implicates ancestry-related Mendelian variation at SYNE1 in childhood-onset essential hypertension.JCI insight · 2024Article
- Nesprin proteins: bridging nuclear envelope dynamics to muscular dysfunction.Cell communication and signaling : CCS · 2024Review
- Nesprin-1: novel regulator of striated muscle nuclear positioning and mechanotransduction.Biochemical Society transactions · 2023Review
- Mena regulates nesprin-2 to control actin-nuclear lamina associations, trans-nuclear membrane signalling and gene expression.Nature communications · 2023Article
- BiallelicGenes · 2021Article
- Predicting Protein-Protein Interactions from Matrix-Based Protein Sequence Using Convolution Neural Network and Feature-Selective Rotation Forest.Scientific reports · 2019Article
- A Glance at the Nuclear Envelope Spectrin Repeat Protein 3.BioMed research international · 2019Review
- Nesprins and Lamins in Health and Diseases of Cardiac and Skeletal Muscles.Frontiers in physiology · 2018Review
- The mechano-sensing role of the unique SH3 insertion in plakin domains revealed by Molecular Dynamics simulations.Scientific reports · 2017Article
- The nesprin-cytoskeleton interface probed directly on single nuclei is a mechanically rich system.Nucleus (Austin, Tex.) · 2017Article
- Fascin Regulates Nuclear Movement and Deformation in Migrating Cells.Developmental cell · 2016Article
- N-terminal nesprin-2 variants regulate β-catenin signalling.Experimental cell research · 2016Article
- Concise Review: Plasma and Nuclear Membranes Convey Mechanical Information to Regulate Mesenchymal Stem Cell Lineage.Stem cells (Dayton, Ohio) · 2016Review
- Cell Mechanosensitivity is Enabled by the LINC Nuclear Complex.Current molecular biology reports · 2016Article
- Polygenic inheritance of cryptorchidism susceptibility in the LE/orl rat.Molecular human reproduction · 2016Article
- Nesprin-2-dependent ERK1/2 compartmentalisation regulates the DNA damage response in vascular smooth muscle cell ageing.Cell death and differentiation · 2015Article
Corrections and comments
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Authors and funding
7 authors.
Funding
Abstract
Nesprin-1 and nesprin-2 are nuclear envelope (NE) proteins characterized by a common structure of an SR (spectrin repeat) rod domain and a C-terminal transmembrane KASH [Klarsicht-ANC-Syne-homology] domain and display N-terminal actin-binding CH (calponin homology) domains. Mutations in these proteins have been described in Emery-Dreifuss muscular dystrophy and attributed to disruptions of interactions at the NE with nesprins binding partners, lamin A/C and emerin. Evolutionary analysis of the rod domains of the nesprins has shown that they are almost entirely composed of unbroken SR-like structures. We present a bioinformatical approach to accurate definition of the boundaries of each SR by comparison with canonical SR structures, allowing for a large-scale homology modelling of the 74 nesprin-1 and 56 nesprin-2 SRs. The exposed and evolutionary conserved residues identify important pbs for protein-protein interactions that can guide tailored binding experiments. Most importantly, the bioinformatics analyses and the 3D models have been central to the design of selected constructs for protein expression. 1D NMR and CD spectra have been performed of the expressed SRs, showing a folded, stable, high content α-helical structure, typical of SRs. Molecular Dynamics simulations have been performed to study the structural and elastic properties of consecutive SRs, revealing insights in the mechanical properties adopted by these modules in the cell.
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