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Vol. 9, Issue 8, 2125-2144, August 1998
Department of Biochemistry, University of Bristol School of
Medicine, University Walk, Bristol BS8 1TD, England
TGN38 is one of the few known resident integral membrane proteins
of the trans-Golgi network (TGN). Since it cycles constitutively between the TGN and the plasma membrane, TGN38 is ideally suited as a
model protein for the identification of post-Golgi trafficking motifs.
Several studies, employing chimeric constructs to detect such motifs
within the cytosolic domain of TGN38, have identified the sequence
333YQRL336 as an autonomous signal capable of
localizing reporter proteins to the TGN. In addition, one group has
found that an upstream serine residue, S331, may also play a role in
TGN38 localization. However, the nature and degree of participation of
S331 in the localization of TGN38 remain uncertain, and the effect has
been studied in chimeric constructs only. Here we investigate the role of S331 in the context of full-length TGN38. Mutations that abolish the
hydroxyl moiety at position 331 (A, D, and E) lead to missorting of
endocytosed TGN38 to the lysosome. Conversely, mutation of S331 to T
has little effect on the endocytic trafficking of TGN38. Together,
these findings indicate that the S331 hydroxyl group has a direct or
indirect effect on the ability of the cytosolic tail of TGN38 to
interact with trafficking and/or sorting machinery at the level of the
early endosome. In addition, mutation of S331 to either A or D results
in increased levels of TGN38 at the cell surface. The results confirm
that S331 plays a critical role in the intracellular trafficking of
TGN38 and further reveal that TGN38 undergoes a signal-mediated
trafficking step at the level of the endosome.
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