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Vol. 13, Issue 12, 4443-4455, December 2002
Department of Cell Biology, The Johns Hopkins University School of
Medicine, Baltimore, Maryland 21205
Ycf1p is the prototypical member of the yeast multidrug
resistance-associated protein (MRP) subfamily of ATP-binding
cassette (ABC) transporters. Ycf1p resides in the vacuolar membrane and mediates glutathione-dependent transport processes that result in
resistance to cadmium and other xenobiotics. A feature common to many
MRP proteins that distinguishes them from other ABC transporters is the
presence of a hydrophobic N-terminal extension (NTE), whose function is
not clearly established. The NTE contains a membrane spanning domain
(MSD0) with five transmembrane spans and a cytosolic linker region
(L0). The goal of this study was to determine the functional
significance of the NTE of Ycf1p by examining the localization and
functional properties of Ycf1p partial molecules, expressed either
singly or together. We show that MSD0 plays a critical role in the
vacuolar membrane trafficking of Ycf1p, whereas L0 is dispensable for
localization. On the other hand, L0 is required for transport function,
as determined by monitoring cadmium resistance. We also examine an
unusual aspect of Ycf1p biology, namely, the posttranslational
proteolytic processing that occurs within a lumenal loop of Ycf1p.
Processing is shown to be Pep4p dependent and thus serves as a
convenient marker for proper vacuolar localization. The processed
fragments associate with each other, suggesting that these natural
cleavage products contribute together to Ycf1p function.
This article has been cited by other articles:
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 P. E. Bandler, C. J. Westlake, C. E. Grant, S. P. C. Cole, and R. G. Deeley Identification of Regions Required for Apical Membrane Localization of Human Multidrug Resistance Protein 2 Mol. Pharmacol., July 1, 2008; 74(1): 9 - 19. [Abstract] [Full Text] [PDF]
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 R. G. Deeley, C. Westlake, and S. P. C. Cole Transmembrane Transport of Endo- and Xenobiotics by Mammalian ATP-Binding Cassette Multidrug Resistance Proteins. Physiol Rev, July 1, 2006; 86(3): 849 - 899. [Abstract] [Full Text] [PDF]
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 C. J. Westlake, S. P.C. Cole, and R. G. Deeley Role of the NH2-terminal Membrane Spanning Domain of Multidrug Resistance Protein 1/ABCC1 in Protein Processing and Trafficking Mol. Biol. Cell, May 1, 2005; 16(5): 2483 - 2492. [Abstract] [Full Text] [PDF]
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 J. Bryan, W. H. Vila-Carriles, G. Zhao, A. P. Babenko, and L. Aguilar-Bryan Toward Linking Structure With Function in ATP-Sensitive K+ Channels Diabetes, December 1, 2004; 53(suppl_3): S104 - S112. [Abstract] [Full Text] [PDF]
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 D. L. Mason, M. P. Mallampalli, G. Huyer, and S. Michaelis A Region within a Lumenal Loop of Saccharomyces cerevisiae Ycf1p Directs Proteolytic Processing and Substrate Specificity Eukaryot. Cell, June 1, 2003; 2(3): 588 - 598. [Abstract] [Full Text] [PDF]
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