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Gene Review

Emd  -  emerin

Mus musculus

Synonyms: AW550900, Emerin, Sta
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Disease relevance of Emd


High impact information on Emd

  • The EDMD gene encodes a novel serine-rich protein termed emerin, which contains a 20 amino acid hydrophobic domain at the C terminus, similar to that described for many membrane proteins of the secretory pathway involved in vesicular transport [3].
  • Fibroblasts deficient in lamins A and C contain misshapen and structurally weakened nuclei, and emerin is mislocalized away from the nuclear envelope [4].
  • Interestingly, expression of mechanosensitive genes in response to mechanical strain was impaired in emerin-deficient cells, and prolonged mechanical stimulation increased apoptosis in emerin-deficient cells [1].
  • Thus, emerin-deficient mouse embryo fibroblasts have apparently normal nuclear mechanics but impaired expression of mechanosensitive genes in response to strain, suggesting that emerin mutations may act through altered transcriptional regulation and not by increasing nuclear fragility [1].
  • These include the mislocalization of emerin, an inner nuclear membrane protein, defects in which are implicated in Emery-Dreifuss muscular dystrophy (EDMD), one of the three major X-linked dystrophies [5].

Biological context of Emd


Anatomical context of Emd

  • Identification of tyrosine-phosphorylation sites in the nuclear membrane protein emerin [6].
  • Emerin-lacking mice show minimal motor and cardiac dysfunctions with nuclear-associated vacuoles [9].
  • In this paper, we analyze the interaction between emerin and actin in differentiating mouse myoblasts [10].
  • We demonstrate that emerin and lamin A/C are bound to actin at the late stages of myotube differentiation and in mature muscle [10].
  • A molecular complex in muscle cells formed by lamin A/C, emerin, and nuclear actin has been identified [11].

Associations of Emd with chemical compounds

  • In this study, mutant mice lacking emerin were produced by insertion of a neomycin resistance gene into exon 6 of the coding gene [9].
  • In further experiments, the metabolites from Sta. chartarum or from closely related fungi (atranones B and E, satratoxin G, trichodermin, 7-alpha-hydroxytrichodermol, staplabin, and SMTP-7) and the known fungal toxins sterigmatocystin, citrinin, and ochratoxin A were each tested with Str. californicus [12].

Other interactions of Emd

  • Analysis of Rb1 phosphorylation states showed prolonged hyper-phosphorylation at key developmental stages in Emd null myogenic cells, both in vivo and in vitro [13].
  • Staurosporine treatment and serum starvation promote the cleavage of emerin in cultured mouse myoblasts: involvement of a caspase-dependent mechanism [8].
  • In vivo specific inhibition of caspase 3 or caspase 6 activity completely abolished emerin proteolysis [8].

Analytical, diagnostic and therapeutic context of Emd

  • With a multiprotease approach combined with highly specific phosphopeptide enrichment and nano liquid chromatography tandem mass spectrometry analysis, we identified three tyrosine-phosphorylation sites, Y-75, Y-95, and Y-106, in mouse emerin [6].
  • Emerin-deficient mouse embryo fibroblasts have abnormal nuclear shape, but in contrast to A-type lamin-deficient cells, exhibit nuclear deformations comparable to wild-type cells in cellular strain experiments, and the integrity of emerin-deficient nuclear envelopes appeared normal in a nuclear microinjection assay [1].
  • Electrocardiography showed mild prolongation of atrioventricular conduction time in emerin-lacking male mice older than 40 weeks of age [9].
  • Myoblast apoptosis and emerin degradation were associated with chromatin compaction and detachment from the nuclear lamina, as detected by electron microscopy [8].
  • On the basis of equivalent numbers of bacteria and spores of fungi added to cell cultures, the overall potency to stimulate the production of proinflammatory mediators decreased in the order Ps. fluorescens > Str. californicus > B. cereus > Sta. chartarum > A. versicolor > P. spinulosum [14].


  1. Abnormal nuclear shape and impaired mechanotransduction in emerin-deficient cells. Lammerding, J., Hsiao, J., Schulze, P.C., Kozlov, S., Stewart, C.L., Lee, R.T. J. Cell Biol. (2005) [Pubmed]
  2. Effect of pathogenic mis-sense mutations in lamin A on its interaction with emerin in vivo. Holt, I., Ostlund, C., Stewart, C.L., Man, N., Worman, H.J., Morris, G.E. J. Cell. Sci. (2003) [Pubmed]
  3. Identification of a novel X-linked gene responsible for Emery-Dreifuss muscular dystrophy. Bione, S., Maestrini, E., Rivella, S., Mancini, M., Regis, S., Romeo, G., Toniolo, D. Nat. Genet. (1994) [Pubmed]
  4. Prelamin A and lamin A appear to be dispensable in the nuclear lamina. Fong, L.G., Ng, J.K., Lammerding, J., Vickers, T.A., Meta, M., Coté, N., Gavino, B., Qiao, X., Chang, S.Y., Young, S.R., Yang, S.H., Stewart, C.L., Lee, R.T., Bennett, C.F., Bergo, M.O., Young, S.G. J. Clin. Invest. (2006) [Pubmed]
  5. Loss of A-type lamin expression compromises nuclear envelope integrity leading to muscular dystrophy. Sullivan, T., Escalante-Alcalde, D., Bhatt, H., Anver, M., Bhat, N., Nagashima, K., Stewart, C.L., Burke, B. J. Cell Biol. (1999) [Pubmed]
  6. Identification of tyrosine-phosphorylation sites in the nuclear membrane protein emerin. Schlosser, A., Amanchy, R., Otto, H. FEBS J. (2006) [Pubmed]
  7. Isolation and characterization of the complete mouse emerin gene. Small, K., Wagener, M., Warren, S.T. Mamm. Genome (1997) [Pubmed]
  8. Staurosporine treatment and serum starvation promote the cleavage of emerin in cultured mouse myoblasts: involvement of a caspase-dependent mechanism. Columbaro, M., Mattioli, E., Lattanzi, G., Rutigliano, C., Ognibene, A., Maraldi, N.M., Squarzoni, S. FEBS Lett. (2001) [Pubmed]
  9. Emerin-lacking mice show minimal motor and cardiac dysfunctions with nuclear-associated vacuoles. Ozawa, R., Hayashi, Y.K., Ogawa, M., Kurokawa, R., Matsumoto, H., Noguchi, S., Nonaka, I., Nishino, I. Am. J. Pathol. (2006) [Pubmed]
  10. Association of emerin with nuclear and cytoplasmic actin is regulated in differentiating myoblasts. Lattanzi, G., Cenni, V., Marmiroli, S., Capanni, C., Mattioli, E., Merlini, L., Squarzoni, S., Maraldi, N.M. Biochem. Biophys. Res. Commun. (2003) [Pubmed]
  11. Lamin A N-terminal phosphorylation is associated with myoblast activation: impairment in Emery-Dreifuss muscular dystrophy. Cenni, V., Sabatelli, P., Mattioli, E., Marmiroli, S., Capanni, C., Ognibene, A., Squarzoni, S., Maraldi, N.M., Bonne, G., Columbaro, M., Merlini, L., Lattanzi, G. J. Med. Genet. (2005) [Pubmed]
  12. Synergistic interaction in simultaneous exposure to Streptomyces californicus and Stachybotrys chartarum. Huttunen, K., Pelkonen, J., Nielsen, K.F., Nuutinen, U., Jussila, J., Hirvonen, M.R. Environ. Health Perspect. (2004) [Pubmed]
  13. Loss of emerin at the nuclear envelope disrupts the Rb1/E2F and MyoD pathways during muscle regeneration. Melcon, G., Kozlov, S., Cutler, D.A., Sullivan, T., Hernandez, L., Zhao, P., Mitchell, S., Nader, G., Bakay, M., Rottman, J.N., Hoffman, E.P., Stewart, C.L. Hum. Mol. Genet. (2006) [Pubmed]
  14. Production of proinflammatory mediators by indoor air bacteria and fungal spores in mouse and human cell lines. Huttunen, K., Hyvärinen, A., Nevalainen, A., Komulainen, H., Hirvonen, M.R. Environ. Health Perspect. (2003) [Pubmed]
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