Mitochondrial elongation factor 2

MIEF2
Available structures
PDBOrtholog search: PDBe RCSB
Identifiers
AliasesMIEF2, MID49, SMCR7, mitochondrial elongation factor 2
External IDsMGI: 2144199 HomoloGene: 27354 GeneCards: MIEF2
Gene location (Human)
Chr.Chromosome 17 (human)[1]
Band17p11.2Start18,260,534 bp[1]
End18,266,552 bp[1]
Orthologs
SpeciesHumanMouse
Entrez

125170

237781

Ensembl

ENSG00000284495
ENSG00000177427

ENSMUSG00000018599

UniProt

Q96C03

Q5NCS9

RefSeq (mRNA)

NM_148886
NM_001144900
NM_139162

NM_001009927

RefSeq (protein)

NP_001138372
NP_631901
NP_683684

NP_001009927

Location (UCSC)Chr 17: 18.26 – 18.27 MbChr 11: 60.73 – 60.73 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Mitochondrial elongation factor 2 is a protein that in humans is encoded by the MIEF2 gene. [5]

Function

This gene encodes an outer mitochondrial membrane protein that functions in the regulation of mitochondrial morphology. It can directly recruit the fission mediator dynamin-related protein 1 (Drp1) to the mitochondrial surface. The gene is located within the Smith-Magenis syndrome region on chromosome 17. Alternative splicing results in multiple transcript variants encoding different isoforms. [provided by RefSeq, Jun 2011].

References

  1. 1 2 3 ENSG00000177427 GRCh38: Ensembl release 89: ENSG00000284495, ENSG00000177427 - Ensembl, May 2017
  2. 1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000018599 - Ensembl, May 2017
  3. ↑ "Human PubMed Reference:".
  4. ↑ "Mouse PubMed Reference:".
  5. ↑ "Entrez Gene: Mitochondrial elongation factor 2". Retrieved 2018-04-01.

Further reading

  • Sarimski K (2004). "Communicative competence and behavioural phenotype in children with Smith-Magenis syndrome". Genet. Couns. 15 (3): 347–55. PMID 15517828.
  • Palmer CS, Osellame LD, Laine D, Koutsopoulos OS, Frazier AE, Ryan MT (June 2011). "MiD49 and MiD51, new components of the mitochondrial fission machinery". EMBO Rep. 12 (6): 565–73. doi:10.1038/embor.2011.54. PMC 3128275. PMID 21508961.
  • Palmer CS, Osellame LD, Laine D, Koutsopoulos OS, Frazier AE, Ryan MT (June 2011). "MiD49 and MiD51, new components of the mitochondrial fission machinery". EMBO Rep. 12 (6): 565–73. doi:10.1038/embor.2011.54. PMC 3128275. PMID 21508961.
  • Losón OC, Song Z, Chen H, Chan DC (March 2013). "Fis1, Mff, MiD49, and MiD51 mediate Drp1 recruitment in mitochondrial fission". Mol. Biol. Cell. 24 (5): 659–67. doi:10.1091/mbc.E12-10-0721. PMC 3583668. PMID 23283981.
  • Liu T, Yu R, Jin SB, Han L, Lendahl U, Zhao J, Nistér M (November 2013). "The mitochondrial elongation factors MIEF1 and MIEF2 exert partially distinct functions in mitochondrial dynamics". Exp. Cell Res. 319 (18): 2893–904. doi:10.1016/j.yexcr.2013.07.010. PMID 23880462.
  • Palmer CS, Elgass KD, Parton RG, Osellame LD, Stojanovski D, Ryan MT (September 2013). "Adaptor proteins MiD49 and MiD51 can act independently of Mff and Fis1 in Drp1 recruitment and are specific for mitochondrial fission". J. Biol. Chem. 288 (38): 27584–93. doi:10.1074/jbc.M113.479873. PMC 3779755. PMID 23921378.
  • Xu S, Cherok E, Das S, Li S, Roelofs BA, Ge SX, Polster BM, Boyman L, Lederer WJ, Wang C, Karbowski M (January 2016). "Mitochondrial E3 ubiquitin ligase MARCH5 controls mitochondrial fission and cell sensitivity to stress-induced apoptosis through regulation of MiD49 protein". Mol. Biol. Cell. 27 (2): 349–59. doi:10.1091/mbc.E15-09-0678. PMC 4713136. PMID 26564796.
  • Otera H, Miyata N, Kuge O, Mihara K (February 2016). "Drp1-dependent mitochondrial fission via MiD49/51 is essential for apoptotic cristae remodeling". J. Cell Biol. 212 (5): 531–44. doi:10.1083/jcb.201508099. PMC 4772499. PMID 26903540.
  • Atkins K, Dasgupta A, Chen KH, Mewburn J, Archer SL (November 2016). "The role of Drp1 adaptor proteins MiD49 and MiD51 in mitochondrial fission: implications for human disease". Clin. Sci. 130 (21): 1861–74. doi:10.1042/CS20160030. PMID 27660309.

This article incorporates text from the United States National Library of Medicine, which is in the public domain.


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