Mutations in Mlph, encoding a member of the Rab effector family, cause the melanosome transport defects observed in leaden mice.

ABSTRACT: The d, ash, and ln coat color mutations provide a unique model system for the study of vesicle transport in mammals. All three mutant loci encode genes that are required for the polarized transport of melanosomes, the specialized, pigment-containing organelles of melanocytes, to the neighboring keratinocytes and eventually into coat hairs. Genetic studies suggest that these genes function in the same or overlapping pathways and are supported by biochemical studies showing that d encodes an actin-based melanosome transport motor, MyoVa, whereas ash encodes Rab27a, a protein that localizes to the melanosome and is postulated to serve as the MyoVa receptor. Here we show that ln encodes melanophilin (Mlph), a previously undescribed protein with homology to Rab effectors such as granuphilin, Sl

SUBMITTER: Matesic LE 

PROVIDER: S-EPMC56945 | biostudies-literature | 2001 Aug

REPOSITORIES: biostudies-literature