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MBC in Press, published online ahead of print February 9, 2005
Mol. Biol. Cell 10.1091/mbc.E04-09-0803

A more recent version of this article appeared on April 1, 2005
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Submitted on September 14, 2004
Accepted on January 31, 2005

Ubiquitylation of a Melanosomal Protein by HECT-E3 Ligases Serves as Sorting Signal for Lysosomal Degradation

Frédéric Lévy, Katja Muehlethaler, Suzanne Salvi, Anne-Lise Peitrequin, Cecilia K. Lindholm, Jean-Charles Cerottini, and Donata Rimoldi

Ludwig Institute for Cancer Research, Lausanne Branch, University of Lausanne, CH-1066 Epalinges, Switzerland

Monitoring Editor: Juan S. Bonifacino

The production of pigment by melanocytic cells of the skin involves a series of enzymatic reactions that take place in specialized organelles, termed melanosomes. Melan-A/MART-1 is a melanocytic transmembrane protein with no enzymatic activity that accumulates in vesicles at the trans side of the Golgi and in melanosomes. We show here that, in melanoma cells, Melan-A associates with two HECT-E3 ubiquitin ligases, NEDD4 and Itch, and is ubiquitylated. Both NEDD4 and Itch participate in the degradation of Melan-A. A mutant Melan-A lacking ubiquitin-acceptor residues displays increased half-life and, in pigmented cells, accumulates in melanosomes. These results suggest that ubiquitylation regulates the lysosomal sorting and degradation of Melan-A/MART-1 from melanosomes in melanocytic cells.

Address correspondence to: Frédéric Lévy (Frederic.Levy{at}isrec.unil.ch) or Donata Rimoldi (Donata.Rimoldi{at}isrec.unil.ch)




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