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Functional interactions between OCA2 and the protein complexes BLOC‐1, BLOC‐2, and AP‐3 inferred from epistatic analyses of mouse coat pigmentation
Author(s) -
Hoyle Diego J.,
RodriguezFernandez Imilce A.,
Dell’Angelica Esteban C.
Publication year - 2011
Publication title -
pigment cell and melanoma research
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.618
H-Index - 105
eISSN - 1755-148X
pISSN - 1755-1471
DOI - 10.1111/j.1755-148x.2010.00815.x
Subject(s) - melanosome , biology , mutant , genetics , microbiology and biotechnology , mutation , biogenesis , oculocutaneous albinism , phenotype , albinism , allele , gene , melanin
Summary The biogenesis of melanosomes is a multistage process that requires the function of cell‐type‐specific and ubiquitously expressed proteins. OCA2, the product of the gene defective in oculocutaneous albinism type 2, is a melanosomal membrane protein with restricted expression pattern and a potential role in the trafficking of other proteins to melanosomes. The ubiquitous protein complexes AP‐3, BLOC‐1, and BLOC‐2, which contain as subunits the products of genes defective in various types of Hermansky–Pudlak syndrome, have been likewise implicated in trafficking to melanosomes. We have tested for genetic interactions between mutant alleles causing deficiency in OCA2 (pink‐eyed dilution unstable), AP‐3 (pearl), BLOC‐1 (pallid), and BLOC‐2 (cocoa) in C57BL/6J mice. The pallid allele was epistatic to pink‐eyed dilution, and the latter behaved as a semi‐dominant phenotypic enhancer of cocoa and, to a lesser extent, of pearl. These observations suggest functional links between OCA2 and these three protein complexes involved in melanosome biogenesis.