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A more recent version of this article appeared on March 1, 2002
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Submitted on August 15, 2001
Revised on December 5, 2001
Accepted on December 5, 2001
1 University of Cambridge, Department of Clinical Biochemistry, Cambridge Institute for Medical Research, Cambridge, CB2 2XY, UK
2 Department of Biology and Biochemistry, University of Bath, Bath BA2 7AY, UK
3 Department of Biochemistry, School of Medical Sciences, University of Bristol, Bristol BS8 1TD, UK
4 CIMR, University of Cambridge, Wellcome Trust-MRC Building, Addenbrooke's Hospital, Hills Road, Cambridge, CB2 2XY, UK
* Corresponding author. E-mail address: JPL10{at}CAM.AC.UK.
CD63 is a lysosomal membrane protein that belongs to the tetraspanin family. Its carboxyterminal cytoplasmic tail sequence contains the lysosomal targeting motif GYEVM. Strong, tyrosine dependent, interaction of the wild type carboxyterminal tail of CD63 with the AP-3 adaptor subunit µ3 was observed using a yeast two hybrid system. The strength of interaction of mutated tail sequences with µ3 correlated with the degree of lysosomal localisation of similarly mutated human CD63 molecules in stably transfected NRK cells. Mutated CD63 containing the cytosolic tail sequence GYEVI, which interacted strongly with µ3 but not at all with µ2 in the yeast two hybrid system, localised to lysosomes in transfected NRK and NIH-3T3 cells. In contrast, it localized to the cell surface in transfected cells of pearl and mocha mice, which have genetic defects in genes encoding subunits of AP-3, but to lysosomes in functionally rescued mocha cells expressing the 
subunit of AP-3. Thus, AP-3 is absolutely required for the delivery of this mutated CD63 to lysosomes. Using this AP-3 dependent mutant of CD63, we have shown that AP-3 functions in membrane traffic from the trans-Golgi network to lysosomes via an intracellular route which appears to bypass early endosomes.
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