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.
| Original language | English |
|---|---|
| Pages (from-to) | 943-951 |
| Number of pages | 9 |
| Journal | Biochemical Society Transactions |
| Volume | 43 |
| Issue number | 5 |
| DOIs | |
| Publication status | Published - 9 Oct 2015 |
Keywords
- ATP-binding cassette (ABC) transporter
- glutathione
- haem
- iron
- mitochondria
- oxidative stress
Access to Document
- Schaedler et al (2015)
c 2015 Authors. This is an open access article published by Portland Press Limited and distributed under the Creative Commons Attribution Licence 3.0.
Profiles
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Janneke Balk
- School of Biological Sciences - Group Leader
- Molecular Microbiology - Member
- Plant Sciences - Member
Person: Research Group Member, Academic, Teaching & Research