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Vol. 12, Issue 6, 1623-1631, June 2001
*Friedrich Miescher Institut, 4059 Basel, Switzerland; and
A crucial step in lysosomal biogenesis is catalyzed by
"uncovering" enzyme (UCE), which removes a covering
N-acetylglucosamine from the mannose 6-phosphate
(Man-6-P) recognition marker on lysosomal hydrolases. This study shows
that UCE resides in the trans-Golgi network (TGN) and
cycles between the TGN and plasma membrane. The cytosolic domain of UCE
contains two potential endocytosis motifs: 488YHPL and
C-terminal 511NPFKD. YHPL is shown to be the more potent of
the two in retrieval of UCE from the plasma membrane. A
green-fluorescent protein-UCE transmembrane-cytosolic domain fusion
protein colocalizes with TGN 46, as does endogenous UCE in HeLa cells,
showing that the transmembrane and cytosolic domains determine
intracellular location. These data imply that the Man-6-P recognition
marker is formed in the TGN, the compartment where Man-6-P receptors
bind cargo and are packaged into clathrin-coated vesicles.
Department of Internal Medicine, Washington University
School of Medicine, St. Louis, Missouri 63110
Corresponding author. E-mail address:
rkornfel{at}im.wustl.edu.
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