CHRNE

Acetylcholine receptor subunit epsilon is a protein that in humans is encoded by the CHRNE gene.[5][6]

CHRNE
Available structures
PDBOrtholog search: PDBe RCSB
Identifiers
AliasesCHRNE, ACHRE, CMS1D, CMS1E, CMS2A, FCCMS, SCCMS, CMS4A, CMS4B, CMS4C, cholinergic receptor nicotinic epsilon subunit
External IDsOMIM: 100725 MGI: 87894 HomoloGene: 60 GeneCards: CHRNE
Gene location (Human)
Chr.Chromosome 17 (human)[1]
Band17p13.2Start4,897,771 bp[1]
End4,934,438 bp[1]
RNA expression pattern
More reference expression data
Orthologs
SpeciesHumanMouse
Entrez

1145

11448

Ensembl

ENSG00000108556

ENSMUSG00000014609

UniProt

Q04844

P20782

RefSeq (mRNA)

NM_000080

NM_009603

RefSeq (protein)

NP_000071

NP_033733

Location (UCSC)Chr 17: 4.9 – 4.93 MbChr 11: 70.61 – 70.62 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Acetylcholine receptors at mature mammalian neuromuscular junctions are pentameric protein complexes composed of four subunits in the ratio of two alpha subunits to one beta, one epsilon, and one delta subunit. The achetylcholine receptor changes subunit composition shortly after birth when the epsilon subunit replaces the gamma subunit seen in embryonic receptors. Mutations in the epsilon subunit are associated with congenital myasthenic syndrome.[6]

Role in health and disease

Congenital myasthenic syndrome (CMS) is associated with genetic defects that affect proteins of the neuromuscular junction. Postsynaptic defects are the most frequent cause of CMS and often result in abnormalities in the acetylcholine receptor (AChR). The majority of mutations causing CMS are found in the AChR subunits genes.[7]

Out of all mutations associated with CMS, more than half are mutations in one of the four genes encoding the adult AChR subunits. Mutations of the AChR often result in endplate deficiency. The most common AChR gene mutation that underlies CMS is the mutation of the CHRNE gene. The CHRNE gene codes for the epsilon subunit of the AChR. Most mutations are autosomal recessive loss-of-function mutations and as a result there is endplate AChR deficiency. CHRNE is associated with changing the kinetic properties of the AChR.[8] One type of mutation of the epsilon subunit of the AChR introduces an arginine (Arg) into the binding site at the α/ε subunit interface of the receptor. The addition of a cationic Arg into the anionic environment of the AChR binding site greatly reduces the kinetic properties of the receptor. The result of the newly introduced ARG is a 30-fold reduction of agonist affinity, 75-fold reduction of gating efficiency, and an extremely weakened channel opening probability. This type of mutation results in an extremely fatal form of CMS.[9]

See also

References

  1. GRCh38: Ensembl release 89: ENSG00000108556 - Ensembl, May 2017
  2. GRCm38: Ensembl release 89: ENSMUSG00000014609 - Ensembl, May 2017
  3. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. Beeson D, Brydson M, Betty M, Jeremiah S, Povey S, Vincent A, Newsom-Davis J (Sep 1993). "Primary structure of the human muscle acetylcholine receptor. cDNA cloning of the gamma and epsilon subunits". Eur J Biochem. 215 (2): 229–38. doi:10.1111/j.1432-1033.1993.tb18027.x. PMID 7688301.
  6. "Entrez Gene: CHRNE cholinergic receptor, nicotinic, epsilon".
  7. Cossins, J.; Burke, G.; Maxwell, S.; Spearman, H.; Man, S.; Kuks, J.; Vincent, A.; Palace, J.; Fuhrer, C.; Beeson, D. (2006). "Diverse molecular mechanisms involved in AChR deficiency due to rapsyn mutations" (PDF). Brain. 129 (10): 2773–2783. doi:10.1093/brain/awl219. PMID 16945936.
  8. Abicht, A.; Dusl, M.; Gallenmüller, C.; Guergueltcheva, V.; Schara, U.; Della Marina, A.; Wibbeler, E.; Almaras, S.; Mihaylova, V.; Von Der Hagen, M.; Huebner, A.; Chaouch, A.; Müller, J. S.; Lochmüller, H. (2012). "Congenital myasthenic syndromes: Achievements and limitations of phenotype-guided gene-after-gene sequencing in diagnostic practice: A study of 680 patients". Human Mutation. 33 (10): 1474–1484. doi:10.1002/humu.22130. PMID 22678886. S2CID 30868022.
  9. Shen, X. -M.; Brengman, J. M.; Edvardson, S.; Sine, S. M.; Engel, A. G. (2012). "Highly fatal fast-channel syndrome caused by AChR subunit mutation at the agonist binding site". Neurology. 79 (5): 449–454. doi:10.1212/WNL.0b013e31825b5bda. PMC 3405251. PMID 22592360.

Further reading

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