ABCG5/G8: A structural view to pathophysiology of the hepatobiliary cholesterol secretion

Aiman A. Zein, Rupinder Kaur, Toka O.K. Hussein, Gregory A. Graf, Jyh Yeuan Lee

Research output: Contribution to journalReview articlepeer-review

39 Scopus citations


The ABCG5/G8 heterodimer is the primary neutral sterol transporter in hepatobiliary and transintestinal cholesterol excretion. Inactivating mutations on either the ABCG5 or ABCG8 subunit cause Sitosterolemia, a rare genetic disorder. In 2016, a crystal structure of human ABCG5/G8 in an apo state showed the first structural information on ATPbinding cassette (ABC) sterol transporters and revealed several structural features that were observed for the first time. Over the past decade, several missense variants of ABCG5/G8 have been associated with non-Sitosterolemia lipid phenotypes. In this review, we summarize recent pathophysiological and structural findings of ABCG5/G8, interpret the structure-function relationship in disease-causing variants and describe the available evidence that allows us to build a mechanistic view of ABCG5/G8-mediated sterol transport.

Original languageEnglish
Pages (from-to)1259-1268
Number of pages10
JournalBiochemical Society Transactions
Issue number5
StatePublished - Oct 18 2019

Bibliographical note

Publisher Copyright:
© 2019 The Author(s).

ASJC Scopus subject areas

  • Biochemistry


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