Emerin

Emerin

PDB rendering based on 1jei.
Available structures
PDB Ortholog search: PDBe, RCSB
Identifiers
SymbolsEMD ; EDMD; LEMD5; STA
External IDsOMIM: 300384 MGI: 108117 HomoloGene: 91 GeneCards: EMD Gene
RNA expression pattern
More reference expression data
Orthologs
SpeciesHumanMouse
Entrez201013726
EnsemblENSG00000102119ENSMUSG00000001964
UniProtP50402O08579
RefSeq (mRNA)NM_000117NM_007927
RefSeq (protein)NP_000108NP_031953
Location (UCSC)Chr HG1497_PATCH:
153.55 – 153.55 Mb		Chr X:
74.25 – 74.26 Mb
PubMed search

Emerin, together with MAN1, is a LEM domain-containing integral protein of the inner nuclear membrane in vertebrates. The function of MAN1 is not extensively known, but emerin is known to interact with nuclear lamins, barrier-to-autointegration factor (BAF), nesprin-1α, and a transcription repressor.

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. Dreifuss-Emery muscular dystrophy is an X-linked inherited degenerative myopathy resulting from mutation in the emerin gene.[1]

Clinical significance

Mutations in emerin cause X-linked recessive Emery-Dreifuss muscular dystrophy.

Moreover, recent research have found that the absence of functional emerin may decrease the infectivity of HIV-1. Thus, it is speculated that patients suffering from Emery-Dreifuss muscular dystrophy may have immunity to or show an irregular infection pattern to HIV-1.[2]

Interactions

Emerin has been shown to interact with:

References

  1. ↑ "Entrez Gene: EMD emerin (Emery-Dreifuss muscular dystrophy)".
  2. ↑ Li M, Craigie R (June 2006). "The inner-nuclear-envelope protein emerin regulates HIV-1 infectivity". Nature 441 (7093): 581–2. doi:10.1038/441581a. PMID 16738646.
  3. ↑ 3.0 3.1 Lattanzi G, Cenni V, Marmiroli S, Capanni C, Mattioli E, Merlini L et al. (April 2003). "Association of emerin with nuclear and cytoplasmic actin is regulated in differentiating myoblasts". Biochem. Biophys. Res. Commun. 303 (3): 764–70. doi:10.1016/s0006-291x(03)00415-7. PMID 12670476.
  4. ↑ 4.0 4.1 4.2 Wilkinson FL, Holaska JM, Zhang Z, Sharma A, Manilal S, Holt I et al. (June 2003). "Emerin interacts in vitro with the splicing-associated factor, YT521-B". Eur. J. Biochem. 270 (11): 2459–66. doi:10.1046/j.1432-1033.2003.03617.x. PMID 12755701.
  5. ↑ Sakaki M, Koike H, Takahashi N, Sasagawa N, Tomioka S, Arahata K et al. (February 2001). "Interaction between emerin and nuclear lamins". J. Biochem. 129 (2): 321–7. doi:10.1093/oxfordjournals.jbchem.a002860. PMID 11173535.
  6. ↑ Clements L, Manilal S, Love DR, Morris GE (January 2000). "Direct interaction between emerin and lamin A". Biochem. Biophys. Res. Commun. 267 (3): 709–14. doi:10.1006/bbrc.1999.2023. PMID 10673356.

Further reading

  • Gant TM, Wilson KL (1998). "Nuclear assembly.". Annu. Rev. Cell Dev. Biol. 13: 669–95. doi:10.1146/annurev.cellbio.13.1.669. PMID 9442884.
  • Helbling-Leclerc A, Bonne G, Schwartz K (2002). "Emery-Dreifuss muscular dystrophy.". Eur. J. Hum. Genet. 10 (3): 157–61. doi:10.1038/sj.ejhg.5200744. PMID 11973618.
  • Holaska JM, Wilson KL (2006). "Multiple roles for emerin: implications for Emery-Dreifuss muscular dystrophy". The anatomical record. Part A, Discoveries in molecular, cellular, and evolutionary biology 288 (7): 676–80. doi:10.1002/ar.a.20334. PMC 2559942. PMID 16761279.
  • Bione S, Maestrini E, Rivella S, Mancini M, Regis S, Romeo G et al. (1995). "Identification of a novel X-linked gene responsible for Emery-Dreifuss muscular dystrophy". Nat. Genet. 8 (4): 323–7. doi:10.1038/ng1294-323. PMID 7894480.
  • Bione S, Tamanini F, Maestrini E, Tribioli C, Poustka A, Torri G et al. (1994). "Transcriptional organization of a 450-kb region of the human X chromosome in Xq28". Proc. Natl. Acad. Sci. U.S.A. 90 (23): 10977–81. doi:10.1073/pnas.90.23.10977. PMC 47904. PMID 8248200.
  • Nagano A, Koga R, Ogawa M, Kurano Y, Kawada J, Okada R et al. (1996). "Emerin deficiency at the nuclear membrane in patients with Emery-Dreifuss muscular dystrophy". Nat. Genet. 12 (3): 254–9. doi:10.1038/ng0396-254. PMID 8589715.
  • Bione S, Small K, Aksmanovic VM, D'Urso M, Ciccodicola A, Merlini L et al. (1996). "Identification of new mutations in the Emery-Dreifuss muscular dystrophy gene and evidence for genetic heterogeneity of the disease". Hum. Mol. Genet. 4 (10): 1859–63. doi:10.1093/hmg/4.10.1859. PMID 8595407.
  • Yamada T, Kobayashi T (1996). "A novel emerin mutation in a Japanese patient with Emery-Dreifuss muscular dystrophy". Hum. Genet. 97 (5): 693–4. doi:10.1007/BF02281886. PMID 8655156.
  • Chen EY, Zollo M, Mazzarella R, Ciccodicola A, Chen CN, Zuo L et al. (1997). "Long-range sequence analysis in Xq28: thirteen known and six candidate genes in 219.4 kb of high GC DNA between the RCP/GCP and G6PD loci". Hum. Mol. Genet. 5 (5): 659–68. doi:10.1093/hmg/5.5.659. PMID 8733135.
  • Cartegni L, di Barletta MR, Barresi R, Squarzoni S, Sabatelli P, Maraldi N et al. (1998). "Heart-specific localization of emerin: new insights into Emery-Dreifuss muscular dystrophy". Hum. Mol. Genet. 6 (13): 2257–64. doi:10.1093/hmg/6.13.2257. PMID 9361031.
  • Ellis JA, Craxton M, Yates JR, Kendrick-Jones J (1998). "Aberrant intracellular targeting and cell cycle-dependent phosphorylation of emerin contribute to the Emery-Dreifuss muscular dystrophy phenotype". J. Cell. Sci. 111 (6): 781–92. PMID 9472006.
  • Squarzoni S, Sabatelli P, Ognibene A, Toniolo D, Cartegni L, Cobianchi F et al. (1998). "Immunocytochemical detection of emerin within the nuclear matrix". Neuromuscul. Disord. 8 (5): 338–44. doi:10.1016/S0960-8966(98)00031-5. PMID 9673989.
  • Ellis JA, Yates JR, Kendrick-Jones J, Brown CA (1999). "Changes at P183 of emerin weaken its protein-protein interactions resulting in X-linked Emery-Dreifuss muscular dystrophy". Hum. Genet. 104 (3): 262–8. doi:10.1007/s004390050946. PMID 10323252.
  • Clements L, Manilal S, Love DR, Morris GE (2000). "Direct interaction between emerin and lamin A". Biochem. Biophys. Res. Commun. 267 (3): 709–14. doi:10.1006/bbrc.1999.2023. PMID 10673356.
  • Squarzoni S, Sabatelli P, Capanni C, Petrini S, Ognibene A, Toniolo D et al. (2001). "Emerin presence in platelets". Acta Neuropathol. 100 (3): 291–8. doi:10.1007/s004019900169. PMID 10965799.
  • Martins SB, Eide T, Steen RL, Jahnsen T, Skålhegg B S, Collas P (2001). "HA95 is a protein of the chromatin and nuclear matrix regulating nuclear envelope dynamics". J. Cell. Sci. 113 (21): 3703–13. PMID 11034899.
  • Hartley JL, Temple GF, Brasch MA (2001). "DNA Cloning Using In Vitro Site-Specific Recombination". Genome Res. 10 (11): 1788–95. doi:10.1101/gr.143000. PMC 310948. PMID 11076863.
  • Sakaki M, Koike H, Takahashi N, Sasagawa N, Tomioka S, Arahata K et al. (2001). "Interaction between emerin and nuclear lamins". J. Biochem. 129 (2): 321–7. doi:10.1093/oxfordjournals.jbchem.a002860. PMID 11173535.
  • Laguri C, Gilquin B, Wolff N, Romi-Lebrun R, Courchay K, Callebaut I et al. (2001). "Structural characterization of the LEM motif common to three human inner nuclear membrane proteins". Structure 9 (6): 503–11. doi:10.1016/S0969-2126(01)00611-6. PMID 11435115.

External links