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J Biol Chem, Vol. 273, Issue 45, 29451-29461, November 6, 1998
From the Institut de Biologie de Lille, CNRS EP 525 Institut
Pasteur de Lille, BP 447, 59021 Lille Cédex, France
In mammalian cells, the mannose 6-phosphate
receptors (MPRs) and the lysosomal glycoproteins, lysosomal-associated
membrane protein (LAMP) I, lysosomal integral membrane protein (LIMP)
II, are directly transported from the trans-Golgi network to endosomes and lysosomes. While MPR traffic relies on the AP-1 adaptor complex, we
report that proper targeting of LAMP I and LIMP II to lysosomes requires the AP-3 adaptor-like complex. Overexpression of these proteins, which contain either a tyrosine- or a
di-leucine-based-sorting motif, promotes AP-3 recruitment on membranes.
Inhibition of AP-3 function using antisense oligonucleotides leads to a
selective misrouting of both LAMP I and LIMP II to the cell surface
without affecting MPR trafficking. These results provide evidence that AP-3 functions in the intracellular targeting of transmembrane glycoproteins to lysosomes.
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