ABCMdb

PMID: 15139851

Alqawi O, Bates S, Georges E
Arginine482 to threonine mutation in the breast cancer resistance protein ABCG2 inhibits rhodamine 123 transport while increasing binding.
Biochem J. 2004 Sep 1;382(Pt 2):711-6., 2004-09-01 [PubMed]

Sentences

No. Mutations Sentence Comment

1 ABCG2 p.Arg482Thr J. (2004) 382, 711-716 (Printed in Great Britain) 711 Arginine482 to threonine mutation in the breast cancer resistance protein ABCG2 inhibits rhodamine 123 transport while increasing binding Omar ALQAWI*, Susan BATES† and Elias GEORGES*1 *Institute of Parasitology, McGill University, Macdonald Campus, Ste-Anne de Bellevue, Quebec, Canada H9 X3V9, and †Cancer Therapeutics Branch, National Cancer Institute, Bethesda, MD 20892, U.S.A. ABCG2 [also known as BCRP (breast cancer resistance protein) or MXR] is an ABC (ATP-binding cassette) protein shown to confer multidrug resistance. Login to comment 3 ABCG2 p.Arg482Thr Later studies demonstrated the presence of a point mutation (Arg482 to Thr) in ABCG2 in MCF-7/ AdrVp1000 cells. Login to comment 26 ABCG2 p.Arg482Thr Analysis of ABCG2 cDNA sequences from these cell lines revealed mutations at position 482: Arg482 to Thr in MCF-7/ AdrVp1000 cells, and to Gly in S1-M1-81 cells. Login to comment 139 ABCG2 p.Arg482Thr For example, it is plausible that the Arg482 to Thr change in the third transmembrane domain affects ABCG2 protein interactions (either homo- or hetero-protein interactions), which in turn leads to a gain in transport function. Login to comment