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J Biol Chem, Vol. 274, Issue 12, 8061-8067, March 19, 1999
From the Lactase-phlorizin hydrolase (LPH) is an apical
protein in intestinal cells. The location of sorting signals in LPH was
investigated by preparing a series of mutants that lacked the LPH
cytoplasmic domain or had the cytoplasmic domain of LPH replaced by
sequences that comprised basolateral targeting signals and overlapping
internalization signals of various potency. These signals are mutants
of the cytoplasmic domain of the influenza hemagglutinin (HA), which
have been shown to be dominant in targeting HA to the basolateral
membrane. The LPH-HA chimeras were expressed in Madin-Darby canine
kidney (MDCK) and colon carcinoma (Caco-2) cells, and their transport
to the cell surface was analyzed. All of the LPH mutants were targeted correctly to the apical membrane. Furthermore, the LPH-HA chimeras were
internalized, indicating that the HA tails were available to interact
with the cytoplasmic components of clathrin-coated pits. The
introduction of a strong basolateral sorting signal into LPH was not
sufficient to override the strong apical signals of the LPH external
domain or transmembrane domains. These results show that basolateral
sorting signals are not always dominant over apical sorting signals in
proteins that contain each and suggest that sorting of basolateral from
apical proteins occurs within a common compartment where competition
for sorting signals can occur.
Hierarchy of Sorting Signals in Chimeras of Intestinal
Lactase-Phlorizin Hydrolase and the Influenza Virus Hemagglutinin
,,
,**, and¶
Department of Physiological Chemistry,
School of Veterinary Medicine Hannover, D-30559 Hannover, Germany, the
¶ Protein Secretion Group, Heinrich Heine University of
Düsseldorf, D-40225 Düsseldorf, Germany, the
Department of Biochemistry, University of Texas Southwestern
Medical Center, Dallas, Texas 75235, and the ** Institute of
Molecular Biology Division I, University of Zürich, CH-8057
Zürich, Switzerland
Copyright © 1999 by The American Society for Biochemistry and Molecular Biology, Inc.
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