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J Biol Chem, Vol. 274, Issue 30, 21139-21148, July 23, 1999
From the Division of Molecular Cell Biology, Department of Biology,
University of Oslo, Oslo 0316, Norway
Targeting of many transmembrane proteins to
post-Golgi compartments is dependent on cytoplasmically exposed sorting
signals. The most widely used signals conform to the tyrosine- or the
leucine-based motifs. Both types of signals have been implicated in
protein localization to the same intracellular compartments, but
previous results from both cell-free experiments and studies of
transfected cell lines have indicated that the two types of signals
interact with separate components of the sorting machinery. We have
overexpressed several transmembrane proteins in stably transfected
Madin-Darby canine kidney cells using an inducible promoter system.
Overexpression of proteins containing tyrosine- or leucine-based
sorting signals resulted in reduced internalization of the transferrin
receptor, whereas recycling and polarized distribution was not
influenced. Our results indicate that proteins with tyrosine- and
leucine-based sorting signals can be transported along common saturable pathways.
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