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Additionally, lysosome-related organelles mediate cell type-specific functions. Ch\u00e9diak\u2013Higashi syndrome is an autosomal, recessive disease, in which loss of the protein LYST causes defects in lysosomes and lysosome-related organelles. The molecular function of LYST, however, is largely unknown. Here, we dissected the function of the yeast LYST homolog, Bph1. We show that Bph1 is an endosomal protein and an effector of the minor Rab5 isoform Ypt52. Strikingly, bph1\u0394 mutant cells have lipidated Atg8 on their endosomes, which is sorted via late endosomes into the vacuole lumen under non-autophagy-inducing conditions. In agreement with this, proteomic analysis of bph1\u0394 vacuoles reveals an accumulation of Atg8, reduced flux via selective autophagy, and defective endocytosis. Additionally, bph1\u0394 cells have reduced autophagic flux under starvation conditions. Our observations suggest that Bph1 is a novel Rab5 effector that maintains endosomal functioning. When Bph1 is lost, Atg8 is lipidated at endosomes even during normal growth and ends up in the vacuole lumen. Thus, our results contribute to the understanding of the role of LYST-related proteins and associated diseases.<\/jats:p>","DOI":"10.1242\/jcs.259421","type":"journal-article","created":{"date-parts":[[2022,3,28]],"date-time":"2022-03-28T09:45:08Z","timestamp":1648460708000},"source":"Crossref","is-referenced-by-count":5,"title":["The yeast LYST homolog Bph1 is a Rab5 effector and prevents Atg8 lipidation at endosomes"],"prefix":"10.1242","volume":"135","author":[{"given":"Prado","family":"Vargas Duarte","sequence":"first","affiliation":[{"name":"Osnabr\u00fcck University 1 , Department of Biology\/Chemistry, Biochemistry section, Barbarastrasse 13, 49076 Osnabr\u00fcck , Germany"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Ralph","family":"Hardenberg","sequence":"additional","affiliation":[{"name":"University of Groningen, University Medical Center Groningen 2 Department of Biomedical Sciences of Cells and Systems , , 9700 Groningen , The Netherlands"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Muriel","family":"Mari","sequence":"additional","affiliation":[{"name":"University of Groningen, University Medical Center Groningen 2 Department of Biomedical Sciences of Cells and Systems , , 9700 Groningen , The Netherlands"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Stefan","family":"Walter","sequence":"additional","affiliation":[{"name":"Osnabr\u00fcck University, Center of Cellular Nanoanalytic Osnabr\u00fcck (CellNanOs) 3 , Barbarastrasse 11, 49076 Osnabr\u00fcck , Germany"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-2652-2686","authenticated-orcid":false,"given":"Fulvio","family":"Reggiori","sequence":"additional","affiliation":[{"name":"University of Groningen, University Medical Center Groningen 2 Department of Biomedical Sciences of Cells and Systems , , 9700 Groningen , The Netherlands"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Florian","family":"Fr\u00f6hlich","sequence":"additional","affiliation":[{"name":"Osnabr\u00fcck University, Center of Cellular Nanoanalytic Osnabr\u00fcck (CellNanOs) 3 , Barbarastrasse 11, 49076 Osnabr\u00fcck , Germany"},{"name":"Osnabr\u00fcck University 4 , Department of Biology\/Chemistry, Molecular Membrane Biology section, Barbarastrasse 13, 49076 Osnabr\u00fcck , Germany"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-6978-8284","authenticated-orcid":false,"given":"Ayel\u00e9n","family":"Gonz\u00e1lez Montoro","sequence":"additional","affiliation":[{"name":"Osnabr\u00fcck University, Center of Cellular Nanoanalytic Osnabr\u00fcck (CellNanOs) 3 , Barbarastrasse 11, 49076 Osnabr\u00fcck , Germany"},{"name":"Osnabr\u00fcck University 5 , Department of Biology\/Chemistry, Cellular Communication Laboratory, Barbarastrasse 13, 49076 Osnabr\u00fcck , Germany"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-4331-8695","authenticated-orcid":false,"given":"Christian","family":"Ungermann","sequence":"additional","affiliation":[{"name":"Osnabr\u00fcck University 1 , Department of Biology\/Chemistry, Biochemistry section, Barbarastrasse 13, 49076 Osnabr\u00fcck , Germany"},{"name":"Osnabr\u00fcck University, Center of Cellular Nanoanalytic Osnabr\u00fcck (CellNanOs) 3 , Barbarastrasse 11, 49076 Osnabr\u00fcck , Germany"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"237","published-online":{"date-parts":[[2022,4,28]]},"reference":[{"key":"2024061307355849900_JCS259421C1","doi-asserted-by":"publisher","first-page":"765","DOI":"10.15252\/embr.201643146","article-title":"Conserved Atg8 recognition sites mediate Atg4 association with autophagosomal membranes and Atg8 deconjugation","volume":"18","author":"Abreu","year":"2017","journal-title":"EMBO Rep."},{"key":"2024061307355849900_JCS259421C2","first-page":"645","article-title":"Retromer and the dynamin Vps1 cooperate in the retrieval of transmembrane proteins from vacuoles","volume":"128","author":"Arlt","year":"2015","journal-title":"J. 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