Structures and functions of mitochondrial ABC transporters

Schaedler, Theresia A, Faust, Belinda, Shintre, Chitra, Carpenter, Elisabeth P, Srinivasan, Vasundara, van Veen, Hendrik W and Balk, Janneke (2015) Structures and functions of mitochondrial ABC transporters. Biochemical Society Transactions, 43 (5). pp. 943-951. ISSN 0300-5127

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Abstract

A small number of physiologically important ATP-binding cassette (ABC) transporters are found in mitochondria. Most are half transporters of the B group forming homodimers and their topology suggests they function as exporters. The results of mutant studies point towards involvement in iron cofactor biosynthesis. In particular, ABC subfamily B member 7 (ABCB7) and its homologues in yeast and plants are required for iron-sulfur (Fe-S) cluster biosynthesis outside of the mitochondria, whereas ABCB10 is involved in haem biosynthesis. They also play a role in preventing oxidative stress. Mutations in ABCB6 and ABCB7 have been linked to human disease. Recent crystal structures of yeast Atm1 and human ABCB10 have been key to identifying substrate-binding sites and transport mechanisms. Combined with in vitro and in vivo studies, progress is being made to find the physiological substrates of the different mitochondrial ABC transporters.

Item Type:	Article
Additional Information:	c 2015 Authors. This is an open access article published by Portland Press Limited and distributed under the Creative Commons Attribution Licence 3.0.
Uncontrolled Keywords:	atp-binding cassette (abc) transporter,glutathione,haem,iron,mitochondria,oxidative stress,sdg 3 - good health and well-being ,/dk/atira/pure/sustainabledevelopmentgoals/good_health_and_well_being
Faculty \ School:	Faculty of Science > School of Biological Sciences
UEA Research Groups:	Faculty of Science > Research Groups > Molecular Microbiology Faculty of Science > Research Groups > Plant Sciences
Depositing User:	Pure Connector
Date Deposited:	04 Jan 2016 12:00
Last Modified:	22 Oct 2022 00:28
URI:	https://ueaeprints.uea.ac.uk/id/eprint/55923
DOI:	10.1042/BST20150118

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