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Vol. 12, Issue 11, 3451-3464, November 2001

Pmel17 Initiates Premelanosome Morphogenesis within Multivesicular Bodies

Joanne F. Berson,* Dawn C. Harper,* Danielle Tenza,dagger Graça Raposo,dagger and Michael S. Marks*Dagger

 *Department of Pathology and Laboratory Medicine, University of Pennsylvania, Philadelphia, Pennsylvania 19104; and  dagger Institut Curie UMR 144, CNRS, Paris, France 75005

Melanosomes are tissue-specific organelles within which melanin is synthesized and stored. The melanocyte-specific glycoprotein Pmel17 is enriched in the lumen of premelanosomes, where it associates with characteristic striations of unknown composition upon which melanin is deposited. However, Pmel17 is synthesized as an integral membrane protein. To clarify its physical linkage to premelanosomes, we analyzed the posttranslational processing of human Pmel17 in pigmented and transfected nonpigmented cells. We show that Pmel17 is cleaved in a post-Golgi compartment into two disulfide-linked subunits: a large lumenal subunit, Malpha , and an integral membrane subunit, Mbeta . The two subunits remain associated intracellularly, indicating that detectable Malpha remains membrane bound. We have previously shown that Pmel17 accumulates on intralumenal membrane vesicles and striations of premelanosomes in pigmented cells. In transfected nonpigmented cells Pmel17 associates with the intralumenal membrane vesicles of multivesicular bodies; cells overexpressing Pmel17 also display structures resembling premelanosomal striations within these compartments. These results suggest that Pmel17 is sufficient to drive the formation of striations from within multivesicular bodies and is thus directly involved in the biogenesis of premelanosomes.

Dagger Corresponding author. E-mail address: marksm{at}mail.med.upenn.edu.

Molecular Biology of the Cell
Vol. 12, 3451-3464, November 2001
Copyright © 2001 by The American Society for Cell Biology


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