Adenine nucleotide translocator

solute carrier family 25 (mitochondrial carrier; adenine nucleotide translocator), member 4
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
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
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 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

• mitochondrial carrier

Footnotes

1. 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.
2. 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.
3. 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.
4. 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.
5. 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)