The DOI matches its Crossref record; 50 of the 50 references it cites were found in a registry or an index.
Nesprin-2 is a multi-isomeric protein that binds lamin and emerin at the nuclear envelope and forms a subcellular network in skeletal muscle
Abstract
Nesprin-2 is a multi-isomeric, modular protein composed of variable numbers of spectrin-repeats linked to a C-terminal transmembrane domain and/or to N-terminal paired calponin homology (CH) domains. The smaller isoforms of nesprin-2 co-localize with and bind lamin A and emerin at the inner nuclear envelope (NE). In SW-13 cells, which lack lamin A/C, nesprin-2 epitopes and emerin were both mislocalized and formed aggregates in the endoplasmic reticulum (ER). The larger isoforms and other CH-domain-containing isoforms co-localize with heterochromatin within the nucleus and are also present at the outer NE and in multiple cytoplasmic compartments. Nesprin-2 isoforms relocalize during in vitro muscle differentiation of C2C12 myoblasts to the sarcomere of myotubes. Immunogold electron microscopy using antibodies specific for three different epitopes detected nesprin-2 isoforms at multiple locations including intranuclear foci, both membranes of the NE, mitochondria, sarcomeric structures and plasma membrane foci. In adult skeletal muscle, confocal immunolocalization studies demonstrated that nesprin-2 epitopes were present at the Z-line and were also associated with the sarcoplasmic reticulum (SR) in close apposition to SERCA2. These data suggest that nesprin-2 isoforms form a linking network between organelles and the actin cytoskeleton and thus may be important for maintaining sub-cellular spatial organisation. Moreover, its association at the NE with lamin and emerin, the genes mutated in Emery-Dreifuss muscular dystrophy, suggests a mechanism to explain how disruption of the NE leads to muscle dysfunction.
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Cites
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Mutations in the gene encoding lamin A/C cause autosomal dominant Emery-Dreifuss muscular dystrophy
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Functional Organization Of The Nuclear Envelope
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Absence of integrin α7 causes a novel form of muscular dystrophy
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Cited by
Nuclear Shape, Mechanics, and Mechanotransduction
Dahl, K. N., Ribeiro, A. J. S., & Lammerding, J. (2008) · Circulation Research · doi:10.1161/circresaha.108.173989 · Cited by 708
Haque, F., Lloyd, D. J., Smallwood, D. T., Dent, C. L., Shanahan, C. M., Fry, A. M., Trembath, R. C., & Shackleton, S. (2006) · Molecular and Cellular Biology · doi:10.1128/mcb.26.10.3738-3751.2006 · Cited by 503
Self-citationZhang, X., Lei, K., Yuan, X., Wu, X., Zhuang, Y., Xu, T., Xu, R., & Han, M. (2009) · Neuron · doi:10.1016/j.neuron.2009.08.018 · Cited by 462
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Metadata
- Authors
- Zhang, Q., Ragnauth, C. D., Skepper, J. N., Worth, N. F., Warren, D. T., Roberts, R. G., Weissberg, P. L., Ellis, J. A., & Shanahan, C. M.
- Venue
- Journal of Cell Science
- Publisher
- The Company of Biologists
- Published
- 2005-02-15
- Volume
- 118
- Issue
- 4
- Pages
- 673-687
- ISSN
- 0021-9533 (ISSN-L)
- 1477-9137
- OpenAlex
- W2025587626
- Cited by
- 277
- References
- 50
- FWCI
- 8.18
- Type
- journal article
- Language
- en
- Open access
- closed
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- CoChat. (2026). Citation check: Nesprin-2 is a multi-isomeric protein that binds lamin and emerin at the nuclear envelope and forms a subcellular network in skeletal muscle. https://app.cochat.ai/papers/10.1242/jcs.01642
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- Zhang, Q., Ragnauth, C. D., Skepper, J. N., Worth, N. F., Warren, D. T., Roberts, R. G., Weissberg, P. L., Ellis, J. A., & Shanahan, C. M. (2005). Nesprin-2 is a multi-isomeric protein that binds lamin and emerin at the nuclear envelope and forms a subcellular network in skeletal muscle. Journal of Cell Science. https://doi.org/10.1242/jcs.01642
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