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Papers In Press, published online ahead of print December 13, 2004
Dept of Molecular Medicine, National Public Health Institute, Helsinki 00251
Corresponding Author: aija.kyttala{at}ktl.fi
CLN3 is a transmembrane protein with a predominant localisation in lysosomes in nonneuronal cells, but is also found in endosomes and the synaptic region in neuronal cells. Mutations in the CLN3 gene result in juvenile neuronal ceroid lipofuscinosis or Batten disease, which currently is the most common cause of childhood dementia. We have recently reported that the lysosomal targeting of CLN3 is facilitated by two targeting motifs; a dileucine-type motif in a cytoplasmic loop domain, and an unusual motif in the carboxyterminal cytoplasmic tail comprising a methionine and a glycine separated by nine amino acids (Kyttälä et al., Mol Biol Cell, 15, 2004). In this study we have investigated the pathways and mechanisms of CLN3 sorting using biochemical binding assays and immunofluorescence methods. The dileucine motif of CLN3 bound both AP-1 and AP-3 in vitro, and expression of mutated CLN3 in AP-1 or AP-3 deficient mouse fibroblasts showed that both adaptor complexes are required for sequential sorting of CLN3 via this motif. Our data indicate the involvement of complex sorting machinery in trafficking of CLN3 and emphasise the diversity of parallel and sequential sorting pathways in the trafficking of membrane proteins.
J. Biol. Chem, 10.1074/jbc.M411862200
Submitted on October 19, 2004
Revised on December 10, 2004
Accepted on December 13, 2004
AP-1 and AP-3 facilitate lysosomal targeting of batten disease protein CLN3 via its dileucine motif
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