Introduction of ABCG8
ABCG8 is ATP-binding cassette subfamily G member 8 which is encoded by the ABCG8 gene in humans. It belongs to the superfamily of ATP-binding cassette (ABC) transporters. ABC proteins are able to transport various kinds of molecules across extra- and intra-cellular membranes. They can be classified into seven distinct subfamilies including ABC1, MDR/TAP, MRP, ALD, OABP, GCN20, and White. The protein encoded by ABCG8 belongs to White family, and functions as a half-transporter to limit intestinal absorption and promote biliary excretion of sterols. It is expressed in a tissue-specific manner in the liver, colon, and intestine. This gene is tandemly arrayed on chromosome 2, in a head-to-head orientation with family member ABCG5.
|Basic Information of ABCG8|
|Protein Name||ATP-binding cassette sub-family G member 8|
|Organism||Homo sapiens (Human)|
Function of ABCG8 Membrane Protein
ABCG8 is ATP-binding cassette sub-family G member 8 which belongs to the ABCG subfamily. They all are half transporters which are composed of a single nucleotide-binding domain and a single transmembrane domain. It has been reported that mutations in this gene may contribute to sterol accumulation and atherosclerosis. In addition, it has been observed in patients with sitosterolemia. Like another member, ABCG5 forms an obligate heterodimer via interacting with ABCG8, and the heterodimer can mediate Mg2+ and ATP-dependent sterol transport across the cell membranes. Furthermore, both ABCG5 and ABCG8 play critical roles in the regulation of sterol absorption and excretion which were identified as new pathways of sterol transport.
Fig.1 Structure of the G5G8 heterodimer. (Lee, 2016)
Application of ABCG8 Membrane Protein in Literature
This article identifies a novel ABCG8 mutation by exome sequencing in this family, and indicates ABCG8’s gene dosage effect.
This article shows that the intestinal transporter ABCG5 and ABCG8 mediate the hypocholesterolemic effects of Eryngium carlinae F. Delaroche.
This review summarizes the current state of ABCG5 and ABCG8, also the remaining key conceptual and mechanistic issues are highlighted.
This article shows us the first case of sitosterolemia which is caused by heterozygous mutations in ABCG5 and ABCG8.
These studies indicate that between the presence of site mutation in ABCG8, and the presence of gallstones, no association was observed.
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