Biochemistry and pharmacology of the human multidrug resistance gene product, ABCG2
Related Experiment Video
Updated: Jul 12, 2026

Methods to Discover Alternative Promoter Usage and Transcriptional Regulation of Murine Bcrp1
Published on: May 27, 2016
1Department of Pharmacology and Toxicology, Walther Oncology Center/Walther Cancer Institute and IU Cancer Center, Indiana University School of Medicine, Indianapolis, IN 46202, USA. jianzhan@iupui.edu
Abstract:
ABCG2 is a half ATP-binding cassette (ABC) transporter that facilitates efflux of a wide variety of substrates ranging from natural products to synthetic anticancer drugs. Over-expression of ABCG2 has been shown to cause multidrug resistance in both laboratory model cell lines and in clinical settings. The polymorphism in ABCG2 has also been suggested to affect the function and clinical outcome in cancer patients. More recently, ABCG2 has been suggested to play a protective role for cancer and normal stem cells. Thus, ABCG2 is an ideal target for therapeutic development to chemo-sensitize drug resistant cancers. In this paper, the recent progress on understanding the structure, function, and pharmacology of ABCG2 and its role in drug resistance and cancer stem cells will be reviewed.
Related Concept Videos
ABC Transporters: Exporter
Pharmacogenetics of Drug Transporters: P-Glycoprotein and Solute Carrier Transporters
Carrier-Mediated Transport
Active transport involves two types of membrane-spanning transporters: uptake and efflux. Uptake transporters are expressed in the small...
ABC Transporters: Importer
In bacteria, based on the number of transmembrane helices and the chemical nature of their substrates, the ABC importers can be divided into three types:
Hepatic Drug Clearance: Role of Transporters
Membrane Transporters
Transporters are mainly composed of alpha-helices, built from bundles of ten or more helices traversing the plasma membrane. The solute-binding sites are located midway, where some of the helices are broken or distorted, making space for the binding site through...

