ATP-binding cassette sub-family G member 8

Definition:

ABCG5 and ABCG8 form an obligate heterodimer that mediates Mg(2+)- and ATP-dependent sterol transport across the cell membrane. Plays an essential role in the selective transport of the dietary cholesterol in and out of the enterocytes and in the selective sterol excretion by the liver into bile. Required for normal sterol homeostasis. The heterodimer with ABCG5 has ATPase activity.

References:

[1]. Jyh-Yeuan Lee, et al. Crystal structure of the human sterol transporter ABCG5/ABCG8. Nature. 2016 May 26;533(7604):561-4. [Content Brief]

[2]. Gregory A Graf, et al. Missense mutations in ABCG5 and ABCG8 disrupt heterodimerization and trafficking. J Biol Chem. 2004 Jun 4;279(23):24881-8. [Content Brief]

[3]. Zhanling Wang, et al. Purification and ATP hydrolysis of the putative cholesterol transporters ABCG5 and ABCG8. Biochemistry. 2006 Aug 15;45(32):9929-39. [Content Brief]

[4]. Brandy J Harvey Johnson, et al. Bile acids stimulate ATP hydrolysis in the purified cholesterol transporter ABCG5/G8. Biochemistry. 2010 Apr 27;49(16):3403-11. [Content Brief]

[5]. K E Berge, et al. Accumulation of dietary cholesterol in sitosterolemia caused by mutations in adjacent ABC transporters. Science. 2000 Dec 1;290(5497):1771-5. [Content Brief]

[6]. K Lu, et al. Two genes that map to the STSL locus cause sitosterolemia: genomic structure and spectrum of mutations involving sterolin-1 and sterolin-2, encoded by ABCG5 and ABCG8, respectively. Am J Hum Genet. 2001 Aug;69(2):278-90. [Content Brief]

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