Emerin

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Emerin
Protein EMD PDB 1jei.png
PDB rendering based on 1jei.
Available structures
PDB Ortholog search: PDBe, RCSB
Identifiers
Symbols EMD ; EDMD; LEMD5; STA
External IDs OMIM300384 MGI108117 HomoloGene91 GeneCards: EMD Gene
RNA expression pattern
PBB GE EMD 209477 at tn.png
More reference expression data
Orthologs
Species Human Mouse
Entrez 2010 13726
Ensembl ENSG00000102119 ENSMUSG00000001964
UniProt P50402 O08579
RefSeq (mRNA) NM_000117 NM_007927
RefSeq (protein) NP_000108 NP_031953
Location (UCSC) Chr HG1497_PATCH:
153.55 – 153.55 Mb
Chr X:
74.25 – 74.26 Mb
PubMed search [1] [2]

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[edit]

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[edit]

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[edit]

Emerin has been shown to interact with:

References[edit]

  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. ^ a b 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. ^ a b c 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[edit]

External links[edit]