{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"omics_type":["Unknown"],"volume":["8"],"submitter":["Steffens A"],"funding":["Deutsche Forschungsgemeinschaft"],"pubmed_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 "],"journal":["Frontiers in plant science"],"pagination":["1969"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC5701936"],"repository":["biostudies-literature"],"pubmed_title":["Physical, Functional and Genetic Interactions between the BEACH Domain Protein SPIRRIG and LIP5 and SKD1 and Its Role in Endosomal Trafficking to the Vacuole in Arabidopsis."],"pmcid":["PMC5701936"],"pubmed_authors":["Hulskamp M","Steffens A","Jakoby M"],"additional_accession":[]},"is_claimable":false,"name":"Physical, Functional and Genetic Interactions between the BEACH Domain Protein SPIRRIG and LIP5 and SKD1 and Its Role in Endosomal Trafficking to the Vacuole in Arabidopsis.","description":"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 ","dates":{"release":"2017-01-01T00:00:00Z","publication":"2017","modification":"2025-04-18T19:47:10.738Z","creation":"2019-03-27T03:02:56Z"},"accession":"S-EPMC5701936","cross_references":{"pubmed":["29209342"],"doi":["10.3389/fpls.2017.01969"]}}