Ubiquitylation of a melanosomal protein by HECT-E3 ligases serves as sorting signal for lysosomal degradation
Details
Serval ID
serval:BIB_4B6755BF3529
Type
Article: article from journal or magazin.
Collection
Publications
Institution
Title
Ubiquitylation of a melanosomal protein by HECT-E3 ligases serves as sorting signal for lysosomal degradation
Journal
Molecular Biology of the Cell
ISSN
1059-1524 (Print)
Publication state
Published
Issued date
04/2005
Volume
16
Number
4
Pages
1777-87
Notes
Journal Article
Research Support, Non-U.S. Gov't --- Old month value: Apr
Research Support, Non-U.S. Gov't --- Old month value: Apr
Abstract
The production of pigment by melanocytic cells of the skin involves a series of enzymatic reactions that take place in specialized organelles called 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 homologous to E6-AP C-terminus (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.
Keywords
Antigens, Neoplasm
Cell Line
Humans
Lysosomes/*metabolism
Melanosomes/chemistry/*metabolism
Neoplasm Proteins/genetics/*metabolism
Proteasome Endopeptidase Complex/genetics/metabolism
Protein Binding
Repressor Proteins/genetics/*metabolism
Ubiquitin/*metabolism
Ubiquitin-Protein Ligases/genetics/*metabolism
Pubmed
Web of science
Create date
28/01/2008 12:17
Last modification date
20/08/2019 14:59