Adenine nucleotide translocator
solute carrier family 25 (mitochondrial carrier; adenine nucleotide translocator), member 4 | |
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Identifiers | |
Symbol | SLC25A4 |
Alt. symbols | PEO3, PEO2, ANT1 |
Entrez | 291 |
HUGO | 10990 |
OMIM | 103220 |
RefSeq | NM_001151 |
UniProt | P12235 |
Other data | |
Locus | Chr. 4 q35 |
solute carrier family 25 (mitochondrial carrier; adenine nucleotide translocator), member 5 | |
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Identifiers | |
Symbol | SLC25A5 |
Alt. symbols | ANT2 |
Entrez | 292 |
HUGO | 10991 |
OMIM | 300150 |
RefSeq | NM_001152 |
UniProt | P05141 |
Other data | |
Locus | Chr. X q24-q26 |
solute carrier family 25 (mitochondrial carrier; adenine nucleotide translocator), member 6 | |
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Identifiers | |
Symbol | SLC25A6 |
Alt. symbols | ANT3 |
Entrez | 293 |
HUGO | 10992 |
OMIM | 403000 |
RefSeq | NM_001636 |
UniProt | P12236 |
Other data | |
Locus | Chr. Y p |
Adenine nucleotide translocator (ANT), also known as the ADP/ATP translocator, exports ATP from the mitochondrial matrix and imports ADP into the matrix.[1] ANT is the most plentiful protein in the inner mitochondrial membrane.[1]
Function
ANT has long been thought to function asymmetrically as a homodimer of subunits in the inner mitochondrial membrane. The dimer was thought to be a gated pore through which ADP and ATP were exchanged between the mitochondrial matrix and the cytoplasm. The dimer hypothesis was first challenged when the three-dimensional structure of ANT was discovered to be a monomer.[2] Further work has shown that ANT functions as a monomer in detergents[3] and in mitochondrial membranes.[4][5]
ANT is an important structural component of the mitochondrial permeability transition pore[1] which can open and lead to cell death through apoptosis or necrosis.
Types
In humans, there exist three paraologous ANT isoforms:
- SLC25A4 – found primarily in heart and skeletal muscle
- SLC25A5 – primarily expressed in fibroblasts
- SLC25A6 – primarily express in liver
See also
Footnotes
- 1 2 3 Kaukonen J, Juselius JK, Tiranti V, Kyttälä A, Zeviani M, Comi GP, Keränen S, Peltonen L, Suomalainen A (2000). "Role of adenine nucleotide translocator 1 in mtDNA maintenance". Science. 289 (5480): 782–785. doi:10.1126/science.289.5480.782. PMID 10926541.
- ↑ Pebay-Peyroula E, Dahout-Gonzalez C, Kahn R, Trézéguet V, Lauquin GJ, Brandolin G (November 2003). "Structure of mitochondrial ADP/ATP carrier in complex with carboxyatractyloside". Nature. 426 (6962): 39–44. doi:10.1038/nature02056. PMID 14603310.
- ↑ Bamber L, Slotboom DJ, Kunji ER (August 2007). "Yeast mitochondrial ADP/ATP carriers are monomeric in detergents as demonstrated by differential affinity purification". J. Mol. Biol. 371 (2): 388–95. doi:10.1016/j.jmb.2007.05.072. PMID 17572439.
- ↑ Bamber L, Harding M, Monné M, Slotboom DJ, Kunji ER (June 2007). "The yeast mitochondrial ADP/ATP carrier functions as a monomer in mitochondrial membranes". Proc. Natl. Acad. Sci. U.S.A. 104 (26): 10830–4. doi:10.1073/pnas.0703969104. PMC 1891095. PMID 17566106.
- ↑ Kunji ER, Crichton PG (March 2010). "Mitochondrial carriers function as monomers". Biochim Biophys Acta. 1797 (6–7): 817–831. doi:10.1016/j.bbabio.2010.03.023. PMID 20362544.
External links
- Adenine Nucleotide Translocator 1 at the US National Library of Medicine Medical Subject Headings (MeSH)
- Adenine Nucleotide Translocator 2 at the US National Library of Medicine Medical Subject Headings (MeSH)
- Adenine Nucleotide Translocator 3 at the US National Library of Medicine Medical Subject Headings (MeSH)