tailieunhanh - Báo cáo khoa học: Structural requirements for the apical sorting of human multidrug resistance protein 2 (ABCC2)

The human multidrug resistance protein 2 (MRP2, symbol ABCC2) is a polytopic membrane glycoprotein of 1545 amino acids which exports anionic conjugates across the apical membrane of polarized cells. A chimeric protein composed of C-proximal MRP2 and N-proximal MRP1 localized to the apicalmembraneof polarizedMadin±Darby canine kidney cells (MDCKII) indicating involvement of the carboxy-proximal part of human MRP2 in apical sorting. | Eur. J. Biochem. 269 1866-1876 2002 FEBS 2002 doi Structural requirements for the apical sorting of human multidrug resistance protein 2 ABCC2 Anne T. Nies1 Jorg Konig1 Yunhai Cui1 Manuela Brom1 Herbert Spring2 and Dietrich Keppler1 1 Division of Tumor Biochemistry Deutsches Krebsforschungszentrum Heidelberg Germany 2Division of Cell Biology Deutsches Krebsforschungszentrum Heidelberg Germany The human multidrug resistance protein 2 MRP2 symbol ABCC2 is a polytopic membrane glycoprotein of 1545 amino acids which exports anionic conjugates across the apical membrane of polarized cells. A chimeric protein composed of C-proximal MRP2 and N-proximal MRP1 localized to the apical membrane of polarized Madin-Darby canine kidney cells MDCKII indicating involvement of the carboxy-proximal part of human MRP2 in apical sorting. When compared to other MRP family members MRP2 has a seven-amino-acid extension at its C-terminus with the last three amino acids TKF comprising a PDZ-interacting motif. In order to analyze whether this extension is required for apical sorting of MRP2 we generated MRP2 constructs mutated and stepwise truncated at their C-termini. These constructs were fused via their N-termini to green fluorescent protein GFP and were transiently transfected into polarized liver-derived human HepG2 cells. Quantitative analysis showed that full-length GFP-MRP2 was localized to the apical membrane in 73 of transfected polarized cells whereas it remained on intracellular membranes in 27 of cells. Removal of the C-terminal TKF peptide and stepwise deletion of up to 11 amino acids did not change this predominant apical distribution. However apical localization was largely impaired when GFP-MRP2 was C-terminally truncated by 15 or more amino acids. Thus neither the PDZ-interacting TKF motif nor the full seven-amino-acid extension were necessary for apical sorting of MRP2. Instead our data indicate that a deletion of at least 15 C-terminal .

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