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J. Biol. Chem., Vol. 266, Issue 25, 16269-16272, Sep, 1991
MA Vega, F Rodriguez, B Segui, C Cales, J Alcalde and IV Sandoval
Time course experiments of the localization of rat LIMP II expressed in COS
cells show that the protein is transported directly from the Golgi complex
to lysosomes. Substitution of the tyrosine-lacking carboxyl cytoplasmic
tail of LIMP II for the native cytoplasmic tails of the plasma membrane
proteins CD36 and CD8 resulted in straight transport of both proteins to
lysosomes. The synthetic tyrosine-containing heptapeptide, RGTGVYG, did not
replace the natural carboxyl cytoplasmic tail of LIMP II in its ability to
transport both CD36 and CD8 to lysosomes, and the two constructs were
transported to and expressed at the plasma membrane. Substitution of the
cytoplasmic tails of either CD36 or CD8 for the carboxyl cytoplasmic tail
of LIMP II resulted in transport of the mutants to the plasma membrane
where they underwent endocytosis before accumulating into lysosomes. The
results indicate that a motif contained in the tyrosine-lacking carboxyl
cytoplasmic tail of LIMP II is sufficient to target proteins directly from
the Golgi complex to lysosomes.
Targeting of lysosomal integral membrane protein LIMP II. The tyrosine- lacking carboxyl cytoplasmic tail of LIMP II is sufficient for direct targeting to lysosomes
Centro de Biologia Molecular, Facultad de Ciencias, Universidad Autonoma de Madrid, Spain.
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