Emerin

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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:
153.59 – 153.59 Mb		Chr X:
74.25 – 74.26 Mb
PubMed search
This box:

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.

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 YTHDC1,[3] ACTG2,[4] PSME1[3] and LMNA.[3][4][5][6]

References

  1. ↑ "Entrez Gene: EMD emerin (Emery-Dreifuss muscular dystrophy)". 
  2. ↑ Jacque, JM, Stevenson, M. (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 3.2 Wilkinson, Fiona L; Holaska James M, Zhang Zhayi, Sharma Aarti, Manilal Sushila, Holt Ian, Stamm Stefan, Wilson Katherine L, Morris Glenn E (June 2003). "Emerin interacts in vitro with the splicing-associated factor, YT521-B". Eur. J. Biochem. (Germany) 270 (11): 2459–66. doi:10.1046/j.1432-1033.2003.03617.x. ISSN 0014-2956. PMID 12755701. 
  4. ↑ 4.0 4.1 Lattanzi, Giovanna; Cenni Vittoria, Marmiroli Sandra, Capanni Cristina, Mattioli Elisabetta, Merlini Luciano, Squarzoni Stefano, Maraldi Nadir Mario (April 2003). "Association of emerin with nuclear and cytoplasmic actin is regulated in differentiating myoblasts". Biochem. Biophys. Res. Commun. (United States) 303 (3): 764–70. doi:10.1016/S0006-291X(03)00415-7. ISSN 0006-291X. PMID 12670476. 
  5. ↑ Sakaki, M; Koike H, Takahashi N, Sasagawa N, Tomioka S, Arahata K, Ishiura S (February 2001). "Interaction between emerin and nuclear lamins". J. Biochem. (Japan) 129 (2): 321–7. ISSN 0021-924X. PMID 11173535. 
  6. ↑ Clements, L; Manilal S, Love D R, Morris G E (January 2000). "Direct interaction between emerin and lamin A". Biochem. Biophys. Res. Commun. (UNITED STATES) 267 (3): 709–14. doi:10.1006/bbrc.1999.2023. ISSN 0006-291X. 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, 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, 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, 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, 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, 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, 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, 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, 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, et al. (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, et al. (2001). "Interaction between emerin and nuclear lamins". J. Biochem. 129 (2): 321–7. PMID 11173535. 
  • Laguri C, Gilquin B, Wolff N, 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

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