Structure and Function of Mitochondrial Anion Transport Proteins

Structure and Function of Mitochondrial Anion Transport Proteins J. Membrane Biol. 179, 165–183 (2001) The Journal of DOI: 10.1007/s002320010046 Membrane Biology © Springer-Verlag New York Inc. 2001 Topical Review R.S. Kaplan Department of Biochemistry and Molecular Biology, FUHS/The Chicago Medical School, 3333 Green Bay Road, North Chicago, IL 60064, USA Received: 16 August 2000 Introduction efflux from mitochondria on the dicarboxylate carrier represents a required step in the gluconeogenic pathway. The mitochondrial anion transporters confer a highly Alternatively, in yeast this carrier may catalyze the influx selective permeability upon the mitochondrial inner of malate, thereby providing an anaplerotic function. membrane. To date, at least fourteen anion transporter Pyruvate influx into mitochondria via the pyruvate trans- activities have been clearly identified (see Table porter is a required step for: (i) the complete oxidation of 1). These carriers catalyze a high magnitude flux across glucose and amino acids (thereby providing the energy the inner membrane and as such occupy a particularly source for a substantial portion of the cell’s ATP); and prominent position within eukaryotic cell intermediary (ii) the supply of carbon precursor for the gluconeogenic metabolism. For example, the exchange of cytoplasmic as well as the triacylglycerol and sterol biosynthetic ADP for mitochondrial ATP on the adenine nucleotide The Journal of Membrane Biology Springer Journals

Structure and Function of Mitochondrial Anion Transport Proteins

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Copyright © Inc. by 2001 Springer-Verlag New York
Life Sciences; Biochemistry, general; Human Physiology
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