Abstract
Beige and Chediak Higashi (BEACH) domain-containing proteins (BDCPs) are facilitators of membrane-dependent cellular processes in eukaryotes. Mutations in BDCPs cause malfunctions of endosomal compartments in various cell types. Recently, the molecular analysis of the BDCP homolog gene SPIRRIG (SPI) has revealed a molecular function in P-bodies and the regulation of RNA stability. We therefore aimed to analyze, whether SPI has also a role in membrane-dependent processes. In this study, we show that SPI physically interacts with endosomal sorting complex required for transport associated ATPase Suppressor of K+-transport growth defect1 (SKD1) and its positive regulator, LYST Interacting Protein 5 (LIP5) and report genetic interactions between SPI and SKD1 and LIP5. We further show that the endosomal transport route of soluble proteins to the lytic vacuole is disturbed in spi lip5 double mutants but not in the single mutants. These vacuolar transport defects were suppressed by additional expression of SKD1. Our results indicate that the BEACH domain protein SPI has in addition to a role in P-bodies a function in endosomal transport routes.
Highlights
Beige and Chediak Higashi (BEACH) domain-containing proteins (BDCPs) were first identified during the characterization of the human Chediak Higashi Syndrome (CHS) and the Beige phenotype in mouse (Barbosa et al, 1996; Perou et al, 1996)
We demonstrate that SPI physically interacts with Lysosomal Trafficking Regulator (LYST) Interacting Protein 5 (LIP5) and Suppressor of K+-transport growth defect1 (SKD1) from Arabidopsis thaliana
We examined the protein interactions of the Arabidopsis BDCP SPI with LIP5 and SKD1
Summary
Beige and Chediak Higashi (BEACH) domain-containing proteins (BDCPs) were first identified during the characterization of the human Chediak Higashi Syndrome (CHS) and the Beige phenotype in mouse (Barbosa et al, 1996; Perou et al, 1996). The corresponding gene was termed Lysosomal Trafficking Regulator (LYST) (Barbosa et al, 1996; Nagle et al, 1996; Perou et al, 1996). The LYST protein contains three conserved motifs at the C-terminus: a Pleckstrin-Homology Domain (PH-Domain), the BEACH domain and a WD40 repeat motif. WD40 repeats and BDCP SPI Regulates Vacuolar Transport
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