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Vol. 273, Issue 1, 186-193, January 2, 1998
From the European Molecular Biology Laboratory, Meyerhofstrasse 1, D-69012 Heidelberg, Federal Republic of Germany
In polarized Madin-Darby canine kidney (MDCK)
cells, sorting of membrane proteins in the trans-Golgi network for
basolateral delivery depends on the presence of cytoplasmic
determinants that are related or unrelated to clathrin-coated pit
localization signals. Whether these signals mediate basolateral protein
sorting through common or distinct pathways is unknown. The cytoplasmic
domain of the cation-dependent mannose 6-phosphate receptor
(CD-MPR) contains clathrin-coated pit localization signals that are
necessary for endocytosis and lysosomal enzyme targeting. In this
study, we have addressed the function of these signals in polarized
sorting of the CD-MPR. A chimeric protein, made of the luminal domain of the influenza virus hemagglutinin fused to the transmembrane and
cytoplasmic domains of the CD-MPR was stably expressed in MDCK cells.
This chimera (HCD) is able to interact with the AP-1 Golgi-specific
assembly proteins and is detected on the basolateral plasma membrane of
MDCK cells where it is endocytosed. Deletion analysis and site-directed
mutagenesis of the cytoplasmic domain of the CD-MPR indicate that HCD
chimeras devoid of clathrin-coated pit localization signals are still
transported to the basolateral membrane where they accumulate. A HCD
chimera containing only the transmembrane domain and the 12 membrane-proximal amino acids of the CD-MPR cytoplasmic tail is also
found on the basolateral membrane but is unable to interact with the
AP-1 assembly proteins. However, the overexpression of this mutant
results in partial apical delivery. It is concluded, therefore, that
the basolateral transport of this chimera requires a saturable sorting
machinery distinct from AP-1.
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