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- W2005573345 abstract "Melanocytes synthesize and store melanin within tissue-specific organelles, the melanosomes. Melanin deposition takes place along fibrils found within these organelles and fibril formation is known to depend on trafficking of the membrane glycoprotein Silver/Pmel17. However, correctly targeted, full-length Silver/Pmel17 cannot form fibers. Proteolytic processing in endosomal compartments and the generation of a lumenal Mα fragment that is incorporated into amyloid-like structures is also essential. Dominant White (DWhite), a mutant form of Silver/Pmel17 first described in chicken, causes disorganized fibers and severe hypopigmentation due to melanocyte death. Surprisingly, the DWhite mutation is an insertion of three amino acids into the transmembrane domain; the DWhite-Mα fragment is unaffected. To determine the functional importance of the transmembrane domain in organized fibril assembly, we investigated membrane trafficking and multimerization of Silver/Pmel17/DWhite proteins. We demonstrate that the DWhite mutation changes lipid interactions and disulfide bond-mediated associations of lumenal domains. Thus, partitioning into membrane microdomains and effects on conformation explain how the transmembrane region may contribute to the structural integrity of Silver/Pmel17 oligomers or influence toxic, amyloidogenic properties." @default.
- W2005573345 created "2016-06-24" @default.
- W2005573345 creator A5008456306 @default.
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- W2005573345 date "2009-11-01" @default.
- W2005573345 modified "2023-09-27" @default.
- W2005573345 title "A mutation within the transmembrane domain of melanosomal protein Silver (Pmel17) changes lumenal fragment interactions" @default.
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- W2005573345 doi "https://doi.org/10.1016/j.ejcb.2009.07.001" @default.
- W2005573345 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/2748924" @default.
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- W2005573345 hasPublicationYear "2009" @default.
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