ArticleBMC cell biology2016
Specific localization of nesprin-1-α2, the short isoform of nesprin-1 with a KASH domain, in developing, fetal and regenerating muscle, using a new monoclonal antibody.
Article in BMC cell biology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed, 31 citations in OpenAlex.
- Selective disruption of microtubule formation at the nuclear envelope impairs the bone resorption capacity of osteoclasts.Journal of cell science · 2026Article
- The role of inner nuclear membrane protein emerin in myogenesis.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2025Review
- 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
- Nesprin-1 LINC complexes recruit microtubule cytoskeleton proteins and drive pathology in Lmna-mutant striated muscle.Human molecular genetics · 2023Article
- Myogenin controls via AKAP6 non-centrosomal microtubule-organizing center formation at the nuclear envelope.eLife · 2021Article
- Article
- Nuclear Mechanotransduction in Skeletal Muscle.Cells · 2021Review
- Lamin A/C Assembly Defects inCells · 2020Article
- Nesprin-1-alpha2 associates with kinesin at myotube outer nuclear membranes, but is restricted to neuromuscular junction nuclei in adult muscle.Scientific reports · 2019Article
- LEM domain-containing protein 3 antagonizes TGFβ-SMAD2/3 signaling in a stiffness-dependent manner in both the nucleus and cytosol.The Journal of biological chemistry · 2018Article
- Linker of nucleoskeleton and cytoskeleton complex proteins in cardiomyopathy.Biophysical reviews · 2018Review
- The Pathogenesis and Therapies of Striated Muscle Laminopathies.Frontiers in physiology · 2018Review
- Nesprins and Lamins in Health and Diseases of Cardiac and Skeletal Muscles.Frontiers in physiology · 2018Review
- Nesprin-1α-Dependent Microtubule Nucleation from the Nuclear Envelope via Akap450 Is Necessary for Nuclear Positioning in Muscle Cells.Current biology : CB · 2017Article
- Muscle Development: Nucleating Microtubules at the Nuclear Envelope.Current biology : CB · 2017Article
- Multiple Isoforms of Nesprin1 Are Integral Components of Ciliary Rootlets.Current biology : CB · 2017Article
- Novel nesprin-1 mutations associated with dilated cardiomyopathy cause nuclear envelope disruption and defects in myogenesis.Human molecular genetics · 2017Article
- Lamins and nesprin-1 mediate inside-out mechanical coupling in muscle cell precursors through FHOD1.Scientific reports · 2017Article
- Recent advances in pericentriolar material organization: ordered layers and scaffolding gels.F1000Research · 2017Review
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Authors and funding
8 authors at 4 institutions in 2 countries.
Funding
Abstract
backgroundNesprin-1-giant (1008kD) is a protein of the outer nuclear membrane that links nuclei to the actin cytoskeleton via amino-terminal calponin homology domains. The short nesprin-1 isoform, nesprin-1-α2, is present only in skeletal and cardiac muscle and several pathogenic mutations occur within it, but the functions of this short isoform without calponin homology domains are unclear. The aim of this study was to determine mRNA levels and protein localization of nesprin-1-α2 at different stages of muscle development in order to shed light on its functions.
resultsmRNA levels of all known nesprin-1 isoforms with a KASH domain were determined by quantitative PCR. The mRNA for the 111 kD muscle-specific short isoform, nesprin-1-α2, was not detected in pre-differentiation human myoblasts but was present at significant levels in multinucleate myotubes. We developed a monoclonal antibody against the unique amino-terminal sequence of nesprin-1-α2, enabling specific immunolocalization for the first time. Nesprin-1-α2 protein was undetectable in pre-differentiation myoblasts but appeared at the nuclear rim in post-mitotic, multinucleate myotubes and reached its highest levels in fetal muscle. In muscle from a Duchenne muscular dystrophy biopsy, nesprin-1-α2 protein was detected mainly in regenerating fibres expressing neonatal myosin. Nesprin-1-giant was present at all developmental stages, but was also highest in fetal and regenerating fibres. In fetal muscle, both isoforms were present in the cytoplasm, as well as at the nuclear rim. A pathogenic early stop codon (E7854X) in nesprin-1 caused reduced mRNA levels and loss of protein levels of both nesprin-1-giant and (unexpectedly) nesprin-1-α2, but did not affect myogenesis in vitro.
conclusionsNesprin-1-α2 mRNA and protein expression is switched on during myogenesis, alongside other known markers of muscle differentiation. The results show that nesprin-1-α2 is dynamically controlled and may be involved in some process occurring during early myofibre formation, such as re-positioning of nuclei.
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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.