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Reference: Burke MA and Ardehali H (2007) Mitochondrial ATP-binding cassette proteins. Transl Res 150(2):73-80

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Abstract

The family of ATP-binding cassette (ABC) proteins is among the largest and most diverse in biology. Members of this family are transmembrane proteins found in all organisms and all biologic membranes from the plasma membrane to intracellular organelles such as the Golgi apparatus, lysosomes, peroxisomes, endoplasmic reticulum, and mitochondria. These proteins are very abundant in bacteria, and given the generally accepted origin of mitochondria from an alpha-proteobacterium, it is logical to assume the mitochondria would also contain these proteins. Mitochondria, however, have surprisingly few ABC proteins and they are dissimilar from those of bacteria. Despite their relative paucity, mitochondrial ABC proteins are believed to play a very important role in cellular homeostasis across very diverse species, including yeast, higher plants, mice, and humans. The yeast protein Atm1p plays a critical role in the transport of Fe/S clusters to the cytosol, and a similar function has been attributed to the homologous human proteins MTABC3 and ABC7. Another yeast protein Mdl1p is a high copy suppressor of ATM1, and regulates cellular resistance to oxidative stress and may be involved in peptide transport across the mitochondrial membrane. The human protein mABC1 has recently been identified to be involved in protection of myocardial cells against oxidative stress. Despite their low numbers, mitochondrial ABC proteins are intricately involved in mitochondrial and cellular homeostasis and may be important mediators of cell survival. In this review, we will discuss the structure, function, physiology, and pathophysiology of these mitochondrial ABC proteins.

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Journal Article
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Burke MA, Ardehali H
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