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Vol. 13, Issue 6, 1953-1964, June 2002
The Ronald O. Perelman Department of Dermatology and The Department
of Cell Biology, New York University School of Medicine, New York, New
York 10016
The processing of tyrosinase, which catalyzes the limiting reaction
in melanin synthesis, was investigated in melan-p1 melanocytes, which
are null at the p locus. Endoglycosidase H digestion
showed that a significant fraction of tyrosinase was retained in the endoplasmic reticulum. This retention could be rescued either by
transfection of melan-p1 cells with an epitope-tagged wild-type p transcript or by treatment with either bafilomycin A1
or ammonium chloride. We found that the endoplasmic reticulum contains
a significant amount of p protein, thus supporting a role for p within
this compartment. Using immunofluoresence, we showed that most mature full-length tyrosinase in melan-p1 cells was located in the perinuclear area near the Golgi, in contrast to its punctate melanosomal pattern in
wild-type melanocytes. Expression of p in melan-p1 cells restored tyrosinase to melanosomes. Triton X-114 phase separation revealed that
an increased amount of tyrosinase was proteolyzed in melan-p1 cells
compared with wild-type melanocytes. The proteolyzed tyrosinase was no
longer membrane bound, but remained enzymatically active and a large
proportion was secreted into the culture medium of melan-p1 cells. We
conclude that p regulates posttranslational processing of tyrosinase,
and hypopigmentation in melan-p1 cells is the result of altered
tyrosinase processing and trafficking.
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