{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Miao Y"],"funding":["National Natural Science Foundation of China","National Key Research and Development Program of China"],"pagination":["RP96353"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC11584181"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["13"],"pubmed_abstract":["The spatiotemporal transition of small GTPase Rab5 to Rab7 is crucial for early-to-late endosome maturation, yet the precise mechanism governing Rab5-to-Rab7 switching remains elusive. USP8, a ubiquitin-specific protease, plays a prominent role in the endosomal sorting of a wide range of transmembrane receptors and is a promising target in cancer therapy. Here, we identified that USP8 is recruited to Rab5-positive carriers by Rabex5, a guanine nucleotide exchange factor (GEF) for Rab5. The recruitment of USP8 dissociates Rabex5 from early endosomes (EEs) and meanwhile promotes the recruitment of the Rab7 GEF SAND-1/Mon1. In USP8-deficient cells, the level of active Rab5 is increased, while the Rab7 signal is decreased. As a result, enlarged EEs with abundant intraluminal vesicles accumulat"],"journal":["eLife"],"pubmed_title":["Spatiotemporal recruitment of the ubiquitin-specific protease USP8 directs endosome maturation."],"pmcid":["PMC11584181"],"funding_grant_id":["31921002","32321004","32070810","2021YFA0805802","2022YFA1304500","2021YFA0804802","92354305"],"pubmed_authors":["Liu J","Wang B","Li D","Liang Y","Liang J","Miao Y","Du Y","Dang S","He K","Ding M"],"additional_accession":[]},"is_claimable":false,"name":"Spatiotemporal recruitment of the ubiquitin-specific protease USP8 directs endosome maturation.","description":"The spatiotemporal transition of small GTPase Rab5 to Rab7 is crucial for early-to-late endosome maturation, yet the precise mechanism governing Rab5-to-Rab7 switching remains elusive. USP8, a ubiquitin-specific protease, plays a prominent role in the endosomal sorting of a wide range of transmembrane receptors and is a promising target in cancer therapy. Here, we identified that USP8 is recruited to Rab5-positive carriers by Rabex5, a guanine nucleotide exchange factor (GEF) for Rab5. The recruitment of USP8 dissociates Rabex5 from early endosomes (EEs) and meanwhile promotes the recruitment of the Rab7 GEF SAND-1/Mon1. In USP8-deficient cells, the level of active Rab5 is increased, while the Rab7 signal is decreased. As a result, enlarged EEs with abundant intraluminal vesicles accumulat","dates":{"release":"2024-01-01T00:00:00Z","publication":"2024 Nov","modification":"2025-04-04T01:21:24.462Z","creation":"2025-04-04T01:21:24.462Z"},"accession":"S-EPMC11584181","cross_references":{"pubmed":["39576689"],"doi":["10.7554/eLife.96353"]}}