Global InformationABC transporter information
| ABC Transporter, NBD | |||||||||
|---|---|---|---|---|---|---|---|---|---|
 Vitamin B12 transporter, BtuCD PDB 1l7v | |||||||||
| Identifiers | |||||||||
| Symbol | ABC_tran | ||||||||
| Pfam | PF00005 | ||||||||
| InterPro | IPR003439 | ||||||||
| PROSITE | PDOC00185 | ||||||||
| SCOP2 | 1b0u / SCOPe / SUPFAM | ||||||||
| TCDB | 3.A.1 | ||||||||
| OPM superfamily | 17 | ||||||||
| OPM protein | 3g5u | ||||||||
| |||||||||
The ABC transporters, ATP synthase (ATP)-binding cassette transporters are a transport system superfamily that is one of the largest and possibly one of the oldest gene families. It is represented in all extant phyla, from prokaryotes to humans.[1][2][3] ABC transporters belong to translocases.
ABC transporters often consist of multiple subunits, one or two of which are transmembrane proteins and one or two of which are membrane-associated AAA ATPases.[citation needed] The ATPase subunits utilize the energy of adenosine triphosphate (ATP) binding and hydrolysis to provide the energy needed for the translocation of substrates across membranes, either for uptake or for export of the substrate.
Most of the uptake systems also have an extracytoplasmic receptor, a solute binding protein. Some homologous ATPases function in non-transport-related processes such as translation of RNA and DNA repair.[4][5] ABC transporters are considered to be an ABC superfamily based on the similarities of the sequence and organization of their ATP-binding cassette (ABC) domains, even though the integral membrane proteins appear to have evolved independently several times, and thus comprise different protein families.[6] Like the ABC exporters, it is possible that the integral membrane proteins of ABC uptake systems also evolved at least three times independently, based on their high resolution three-dimensional structures.[7] ABC uptake porters take up a large variety of nutrients, biosynthetic precursors, trace metals and vitamins, while exporters transport lipids, sterols, drugs, and a large variety of primary and secondary metabolites. Some of these exporters in humans are involved in tumor resistance, cystic fibrosis and a range of other inherited human diseases. High level expression of the genes encoding some of these exporters in both prokaryotic and eukaryotic organisms (including human) result in the development of resistance to multiple drugs such as antibiotics and anti-cancer agents.
Hundreds of ABC transporters have been characterized from both prokaryotes and eukaryotes.[8] ABC genes are essential for many processes in the cell, and mutations in human genes cause or contribute to several human genetic diseases.[9] Forty eight ABC genes have been reported in humans. Among these, many have been characterized and shown to be causally related to diseases present in humans such as cystic fibrosis, adrenoleukodystrophy, Stargardt disease, drug-resistant tumors, Dubin–Johnson syndrome, Byler's disease, progressive familiar intrahepatic cholestasis, X-linked sideroblastic anemia, ataxia, and persistent and hyperinsulimenic hypoglycemia.[8] ABC transporters are also involved in multiple drug resistance, and this is how some of them were first identified. When the ABC transport proteins are overexpressed in cancer cells, they can export anticancer drugs and render tumors resistant.[10]
- ^ Fath, M. J.; Kolter, R. (December 1993). "ABC transporters: bacterial exporters". Microbiological Reviews. 57 (4): 995–1017. doi:10.1128/MMBR.57.4.995-1017.1993. ISSN 0146-0749. PMC 372944. PMID 8302219.
- ^ Jones PM, George AM (Mar 2004). "The ABC transporter structure and mechanism: perspectives on recent research". Cellular and Molecular Life Sciences. 61 (6): 682–99. doi:10.1007/s00018-003-3336-9. PMID 15052411. S2CID 21422822.
- ^ Ponte-Sucre A, ed. (2009). ABC Transporters in Microorganisms. Caister Academic. ISBN 978-1-904455-49-3.
- ^ Davidson AL, Dassa E, Orelle C, Chen J (Jun 2008). "Structure, function, and evolution of bacterial ATP-binding cassette systems". Microbiology and Molecular Biology Reviews. 72 (2): 317–64, table of contents. doi:10.1128/MMBR.00031-07. PMC 2415747. PMID 18535149.
- ^ Goffeau A, de Hertogh B, Baret PV (2013). "ABC Transporters". In Lane WJ, Lennarz MD (eds.). Encyclopedia of Biological Chemistry (Second ed.). London: Academic Press. pp. 7–11. doi:10.1016/B978-0-12-378630-2.00224-3. ISBN 978-0-12-378631-9.
- ^ Wang B, Dukarevich M, Sun EI, Yen MR, Saier MH (Sep 2009). "Membrane porters of ATP-binding cassette transport systems are polyphyletic". The Journal of Membrane Biology. 231 (1): 1–10. doi:10.1007/s00232-009-9200-6. PMC 2760711. PMID 19806386.
- ^ ter Beek J, Guskov A, Slotboom DJ (Apr 2014). "Structural diversity of ABC transporters". The Journal of General Physiology. 143 (4): 419–35. doi:10.1085/jgp.201411164. PMC 3971661. PMID 24638992.
- ^ a b Choi CH (Oct 2005). "ABC transporters as multidrug resistance mechanisms and the development of chemosensitizers for their reversal". Cancer Cell International. 5: 30. doi:10.1186/1475-2867-5-30. PMC 1277830. PMID 16202168.
- ^ Dean M, Hamon Y, Chimini G (Jul 2001). "The human ATP-binding cassette (ABC) transporter superfamily". Journal of Lipid Research. 42 (7): 1007–17. doi:10.1016/S0022-2275(20)31588-1. PMID 11441126.
- ^ Scott MP, Lodish HF, Berk A, Kaiser, C, Krieger M, Bretscher A, Ploegh H, Amon A (2012). Molecular Cell Biology. San Francisco: W. H. Freeman. ISBN 978-1-4292-3413-9.