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Vol. 10, Issue 1, 35-46, January 1999
Department of Molecular Pharmacology, Albert Einstein College of
Medicine, Bronx, New York 10461
Gp180, a duck protein that was proposed to be a cell surface
receptor for duck hepatitis B virus, is the homolog of
metallocarboxypeptidase D, a mammalian protein thought to
function in the trans-Golgi network (TGN) in the processing of proteins
that transit the secretory pathway. Both gp180 and mammalian
metallocarboxypeptidase D are type I integral membrane proteins that
contain a 58-residue cytosolic C-terminal tail that is highly conserved
between duck and rat. To investigate the regions of the gp180 tail
involved with TGN retention and intracellular trafficking, gp180 and
various deletion and point mutations were expressed in the AtT-20 mouse
pituitary corticotroph cell line. Full length gp180 is enriched in the
TGN and also cycles to the cell surface. Truncation of the C-terminal 56 residues of the cytosolic tail eliminates the enrichment in the TGN
and the retrieval from the cell surface. Truncation of 12-43 residues
of the tail reduced retention in the TGN and greatly accelerated the
turnover of the protein. In contrast, deletion of the C-terminal 45 residues, which truncates a potential YxxL-like sequence (FxxL),
reduced the protein turnover and caused accumulation of the protein on
the cell surface. A point mutation of the FxxL sequence to AxxL slowed
internalization, showing that this element is important for retrieval
from the cell surface. Mutation of a pair of casein kinase II sites
within an acidic cluster showed that they are also important for
trafficking. The present study demonstrates that multiple sequence
elements within the cytoplasmic tail of gp180 participate in TGN localization.
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