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Vol. 273, Issue 2, 950-956, January 9, 1998
From the Department of Microbiology and Immunology, Emory
University School of Medicine, Atlanta, Georgia 30322
Transmembrane glycoproteins with type 1 topology
can be retrieved to the endoplasmic reticulum (ER) by a retrieval
signal containing a di-lysine (KK) motif near the C terminus. To
investigate the structural requirements for ER retrieval, we have
constructed mutants of the simian immunodeficiency virus (SIV) envelope
(Env) protein with cytoplasmic tails of different lengths and
containing a KK motif at the 
3 and 4 positions. Such proteins were
found to be retained intracellularly when the signal was located 18 amino acids or more away from the membrane spanning domain. The retrieval signal was found to be functional even when placed at the
distal end of the wild-type SIV Env protein with 164 amino acids in the
cytoplasmic tail, as shown by the lack of proteolytic processing and
lack of cell surface expression of the mutant proteins. However,
proteins with a cytoplasmic tail length of 13 amino acids or less
having the di-lysine motif at the 3 and 4 positions were not
retrieved to the ER since they were found to be processed and
transported to the cell surface. The surface-expressed proteins were
found to be functional in inducing cell fusion, whereas the proteins
retained intracellularly were defective in fusion activity. We also
found that the KK motif introduced near an amphipathic helical region
in the cytoplasmic tail was not functional. These results demonstrate
that the ability of the KK motif to cause protein retrieval and
retention in the endoplasmic reticulum depends on the length and
structure of the cytoplasmic domain. The ER retrieval of the mutant
proteins was found to correlate with increased intracellular binding to
COP proteins.
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