Yeast Homologues of Three BLOC-1 Subunits Highlight KxDL Proteins As Conserved Interactors of BLOC-1

Authors


Timothy P. Levine, tim.levine@ucl.ac.uk

Abstract

Biogenesis of lysosome-related organelle complex-1 (BLOC-1) is one of the four multi-subunit complexes implicated in sorting cargo to lysosome-related organelles, as loss of function of any of these complexes causes Hermansky–Pudlak syndrome. Eight subunits of BLOC-1 interact with each other and with many other proteins. Identifying new interactors of BLOC-1 will increase understanding of its mechanism of action, and studies in model organisms are useful for finding such interactors. PSI-BLAST searches identify homologues in diverse model organisms, but there are significant gaps for BLOC-1, with none of its eight subunits found in Saccharomyces cerevisiae. Here we use more sensitive searches to identify distant homologues for three BLOC-1 subunits in S. cerevisiae: Blos1, snapin and cappuccino (cno). Published data on protein interactions show that in yeast these are likely to form a complex with three other proteins. One of these is the yeast homologue of the previously uncharacterized KxDL protein, which also interacts with Blos1 and cno in higher eukaryotes, suggesting that KxDL proteins are key interactors with BLOC-1.

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