| http://purl.uniprot.org/citations/19272020 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/19272020 | http://www.w3.org/2000/01/rdf-schema#comment | "PtdIns(3,5)P(2) is one of the seven regulatory PPIn (polyphosphoinositides) that are ubiquitous in eukaryotes. It controls membrane trafficking at multiple points in the endosomal/lysosomal system and consequently regulates the size, shape and acidity of at least one endo-lysosomal compartment. PtdIns(3,5)P(2) appears to exert this control via multiple effector proteins, with each effector specific for a subset of the various PtdIns(3,5)P(2)-dependent processes. Some putative PtdIns(3,5)P(2) effectors have been identified, including Atg18p-related PROPPIN [beta-propeller(s) that bind PPIn] proteins and the epsin-like proteins Ent3p and Ent5p, whereas others remain to be defined. One of the principal functions of PtdIns(3,5)P(2) is to regulate the fission/fragmentation of endo-lysosomal sub-compartments. PtdIns(3,5)P(2) is required for vesicle formation during protein trafficking between endo-lysosomes and also for fragmentation of endo-lysosomes into smaller compartments. In yeast, hyperosmotic stress accelerates the latter process. In the present review we highlight and discuss recent studies that reveal the role of the HOPS-CORVET complex and the vacuolar H(+)-ATPase in the process of endo-lysosome fission, and speculate on connections between these machineries and the Fab1p pathway. We also discuss new evidence linking PtdIns(3,5)P(2) and PtdIns5P to the regulation of exocytosis."xsd:string |
| http://purl.uniprot.org/citations/19272020 | http://purl.org/dc/terms/identifier | "doi:10.1042/bj20081950"xsd:string |
| http://purl.uniprot.org/citations/19272020 | http://purl.uniprot.org/core/author | "Kobayashi T."xsd:string |
| http://purl.uniprot.org/citations/19272020 | http://purl.uniprot.org/core/author | "Dong K."xsd:string |
| http://purl.uniprot.org/citations/19272020 | http://purl.uniprot.org/core/author | "Dove S.K."xsd:string |
| http://purl.uniprot.org/citations/19272020 | http://purl.uniprot.org/core/author | "Michell R.H."xsd:string |
| http://purl.uniprot.org/citations/19272020 | http://purl.uniprot.org/core/author | "Williams F.K."xsd:string |
| http://purl.uniprot.org/citations/19272020 | http://purl.uniprot.org/core/date | "2009"xsd:gYear |
| http://purl.uniprot.org/citations/19272020 | http://purl.uniprot.org/core/name | "Biochem J"xsd:string |
| http://purl.uniprot.org/citations/19272020 | http://purl.uniprot.org/core/pages | "1-13"xsd:string |
| http://purl.uniprot.org/citations/19272020 | http://purl.uniprot.org/core/title | "Phosphatidylinositol 3,5-bisphosphate and Fab1p/PIKfyve underPPIn endo-lysosome function."xsd:string |
| http://purl.uniprot.org/citations/19272020 | http://purl.uniprot.org/core/volume | "419"xsd:string |
| http://purl.uniprot.org/citations/19272020 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/19272020 |
| http://purl.uniprot.org/citations/19272020 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/19272020 |
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| http://purl.uniprot.org/uniprot/#_P34756-mappedCitation-19272020 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/19272020 |
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