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• W2125005162 endingPage "32636" @default.
• W2125005162 startingPage "32622" @default.
• W2125005162 abstract "P-glycoprotein (P-gp) is an ATP binding cassette transporter that effluxes a variety of structurally diverse compounds including anticancer drugs. Computational models of human P-gp in the apo- and nucleotide-bound conformation show that the adenine group of ATP forms hydrogen bonds with the conserved Asp-164 and Asp-805 in intracellular loops 1 and 3, respectively, which are located at the interface between the nucleotide binding domains and transmembrane domains. We investigated the role of Asp-164 and Asp-805 residues by substituting them with cysteine in a cysteine-less background. It was observed that the D164C/D805C mutant, when expressed in HeLa cells, led to misprocessing of P-gp, which thus failed to transport the drug substrates. The misfolded protein could be rescued to the cell surface by growing the cells at a lower temperature (27 °C) or by treatment with substrates (cyclosporine A, FK506), modulators (tariquidar), or small corrector molecules. We also show that short term (4-6 h) treatment with 15 μM cyclosporine A or FK506 rescues the pre-formed immature protein trapped in the endoplasmic reticulum in an immunophilin-independent pathway. The intracellularly trapped misprocessed protein associates more with chaperone Hsp70, and the treatment with cyclosporine A reduces the association of mutant P-gp, thus allowing it to be trafficked to the cell surface. The function of rescued cell surface mutant P-gp is similar to that of wild-type protein. These data demonstrate that the Asp-164 and Asp-805 residues are not important for ATP binding, as proposed earlier, but are critical for proper folding and maturation of a functional transporter." @default.
• W2125005162 created "2016-06-24" @default.
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• W2125005162 creator A5075535128 @default.
• W2125005162 creator A5081938413 @default.
• W2125005162 date "2013-11-01" @default.
• W2125005162 modified "2023-10-14" @default.
• W2125005162 title "Mutations in Intracellular Loops 1 and 3 Lead to Misfolding of Human P-glycoprotein (ABCB1) That Can Be Rescued by Cyclosporine A, Which Reduces Its Association with Chaperone Hsp70" @default.
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• W2125005162 doi "https://doi.org/10.1074/jbc.m113.498980" @default.
• W2125005162 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/3820894" @default.
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• W2125005162 hasPublicationYear "2013" @default.
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