Emerin

Quality 0.50 · 0 views · Updated 2 months ago

Protein-coding gene in humans

title: "Emerin" type: doc version: 1 created: 2026-02-28 author: "Wikipedia contributors" status: active scope: public tags: ["molecular-biology"] description: "Protein-coding gene in humans" topic_path: "science/biology" source: "https://en.wikipedia.org/wiki/Emerin" license: "CC BY-SA 4.0" wikipedia_page_id: 0 wikipedia_revision_id: 0

::summary Protein-coding gene in humans ::

Emerin is a protein that in humans is encoded by the EMD gene, also known as the STA gene. Emerin, together with LEMD3, is a LEM domain-containing integral protein of the inner nuclear membrane in vertebrates. Emerin is highly expressed in cardiac and skeletal muscle. In cardiac muscle, emerin localizes to adherens junctions within intercalated discs where it appears to function in mechanotransduction of cellular strain and in beta-catenin signaling. Mutations in emerin cause X-linked recessive Emery–Dreifuss muscular dystrophy, cardiac conduction abnormalities and dilated cardiomyopathy.

It is named after Alan Emery.

Structure

Emerin is a 29.0 kDa (34 kDa observed MW) protein composed of 254 amino acids. Emerin is a serine-rich protein with an N-terminal 20-amino acid hydrophobic region that is flanked by charged residues; the hydrophobic region may be important for anchoring the protein to the membrane, with the charged terminal tails being cytosolic. In cardiac, skeletal, and smooth muscle, emerin localizes to the inner nuclear membrane; expression of emerin is highest in skeletal and cardiac muscle. In cardiac muscle specifically, emerin also resides at adherens junctions within intercalated discs.

Function

Emerin is a serine-rich nuclear membrane protein and a member of the nuclear lamina-associated protein family. It mediates membrane anchorage to the cytoskeleton. Emery–Dreifuss muscular dystrophy is an X-linked inherited degenerative myopathy resulting from mutation in the EMD (also known clinically as STA) gene. Emerin appears to be involved in mechanotransduction, as emerin-deficient mouse fibroblasts failed to transduce normal mechanosensitive gene expression responses to strain stimuli. In cardiac muscle, emerin is also found complexed to beta-catenin at adherens junctions of intercalated discs, and cardiomyocytes from hearts lacking emerin showed beta-catenin redistribution as well as perturbed intercalated disc architecture and myocyte shape. This interaction appears to be regulated by glycogen synthase kinase 3 beta.

Clinical significance

Mutations in emerin cause X-linked recessive Emery–Dreifuss muscular dystrophy, which is characterized by early contractures in the Achilles tendons, elbows and post-cervical muscles; muscle weakness proximal in the upper limbs and distal in lower limbs; along with cardiac conduction defects that range from sinus bradycardia, PR prolongation to complete heart block. In these patients, immunostaining of emerin is lost in various tissues, including muscle, skin fibroblasts, and leukocytes, however diagnostic protocols involve mutational analysis rather than protein staining. In nearly all cases, mutations result in a complete deletion, or undetectable levels, of emerin protein. Approximately 20% of cases have X chromosomes with an inversion within the Xq28 region.

Moreover, recent research have found that the absence of functional emerin may decrease the infectivity of HIV-1. Thus, it is speculated that patients with Emery–Dreifuss muscular dystrophy may have immunity to or show an irregular infection pattern to HIV-1.

Interactions

Emerin has been shown to interact with:

References

References

  1. {{cite Q. Q29581774
  2. "Protein sequence of human EMD (Uniprot ID: P50402)".
  3. (Dec 1994). "Identification of a novel X-linked gene responsible for Emery–Dreifuss muscular dystrophy". Nature Genetics.
  4. (Mar 1996). "Emerin deficiency at the nuclear membrane in patients with Emery–Dreifuss muscular dystrophy". Nature Genetics.
  5. (Jun 1996). "The Emery–Dreifuss muscular dystrophy protein, emerin, is a nuclear membrane protein". Human Molecular Genetics.
  6. (Dec 1997). "Heart-specific localization of emerin: new insights into Emery–Dreifuss muscular dystrophy". Human Molecular Genetics.
  7. (Feb 1999). "Distribution of emerin and lamins in the heart and implications for Emery–Dreifuss muscular dystrophy". Human Molecular Genetics.
  8. "Entrez Gene: EMD emerin (Emery–Dreifuss muscular dystrophy)".
  9. (29 August 2005). "Abnormal nuclear shape and impaired mechanotransduction in emerin-deficient cells.". The Journal of Cell Biology.
  10. (March 2010). "Identification of an emerin-beta-catenin complex in the heart important for intercalated disc architecture and beta-catenin localisation.". Cellular and Molecular Life Sciences.
  11. (Jun 2000). "Emery–Dreifuss muscular dystrophy - a 40 year retrospective". Neuromuscular Disorders.
  12. (Jan 1998). "Emerin deletions occurring on both Xq28 inversion backgrounds". Human Molecular Genetics.
  13. (Jun 2006). "Virology: HIV goes nuclear". Nature.
  14. (Apr 2003). "Association of emerin with nuclear and cytoplasmic actin is regulated in differentiating myoblasts". Biochemical and Biophysical Research Communications.
  15. (Sep 2014). "The molecular basis of emerin-emerin and emerin-BAF interactions". Journal of Cell Science.
  16. (Feb 2003). "Transcriptional repressor germ cell-less (GCL) and barrier to autointegration factor (BAF) compete for binding to emerin in vitro". The Journal of Biological Chemistry.
  17. (Mar 2004). "Emerin binding to Btf, a death-promoting transcriptional repressor, is disrupted by a missense mutation that causes Emery–Dreifuss muscular dystrophy". European Journal of Biochemistry.
  18. (Mar 2010). "Identification of an emerin-beta-catenin complex in the heart important for intercalated disc architecture and beta-catenin localisation". Cellular and Molecular Life Sciences.
  19. (Jul 2006). "The inner nuclear membrane protein emerin regulates beta-catenin activity by restricting its accumulation in the nucleus". The EMBO Journal.
  20. (Feb 2001). "Interaction between emerin and nuclear lamins". Journal of Biochemistry.
  21. (Jan 2000). "Direct interaction between emerin and lamin A". Biochemical and Biophysical Research Communications.
  22. (Dec 2001). "Nesprins: a novel family of spectrin-repeat-containing proteins that localize to the nuclear membrane in multiple tissues". Journal of Cell Science.
  23. (Aug 2002). "Nesprin-1alpha self-associates and binds directly to emerin and lamin A in vitro". FEBS Letters.
  24. (Aug 2007). "Distinct functional domains in nesprin-1alpha and nesprin-2beta bind directly to emerin and both interactions are disrupted in X-linked Emery–Dreifuss muscular dystrophy". Experimental Cell Research.
  25. (Feb 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.
  26. (Feb 2008). "LUMA interacts with emerin and influences its distribution at the inner nuclear membrane". Journal of Cell Science.
  27. (Jun 2003). "Emerin interacts in vitro with the splicing-associated factor, YT521-B". European Journal of Biochemistry.

::callout[type=info title="Wikipedia Source"] This article was imported from Wikipedia and is available under the Creative Commons Attribution-ShareAlike 4.0 License. Content has been adapted to SurfDoc format. Original contributors can be found on the article history page. ::

molecular-biology