{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Wright EB"],"funding":["NINDS NIH HHS","University of Arizona","National Institutes of Health","NIH HHS"],"pagination":["jcs263908"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC12377713"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["138(15)"],"pubmed_abstract":["Disruption of endolysosomal acidification causes toxic protein accumulation and neuronal dysfunction linked to neurodevelopmental and neurodegenerative disorders. However, the molecular mechanisms regulating neuronal endolysosomal pH remain unclear. Transmembrane protein 184B (TMEM184B) is a conserved seven-pass transmembrane protein that is essential for synaptic function, and its sequence disruption is associated with neurodevelopmental disorders. Here, we identify TMEM184B as a key regulator of endolysosomal acidification. TMEM184B localizes to early and late endosomes, and proteomic analysis confirms that TMEM184B interacts with endosomal proteins, including the vacuolar ATPase (V-ATPase), a multi-subunit proton pump crucial for lumenal acidification. Tmem184b-mutant mouse cortical neu"],"journal":["Journal of cell science"],"pubmed_title":["TMEM184B modulates endolysosomal acidification via the vesicular proton pump."],"pmcid":["PMC12377713"],"funding_grant_id":["NS105680","R01 NS105680"],"pubmed_authors":["Langlais PR","Bhattacharya MRC","Larsen EG","Padilla-Rodriguez M","Wright EB"],"additional_accession":[]},"is_claimable":false,"name":"TMEM184B modulates endolysosomal acidification via the vesicular proton pump.","description":"Disruption of endolysosomal acidification causes toxic protein accumulation and neuronal dysfunction linked to neurodevelopmental and neurodegenerative disorders. However, the molecular mechanisms regulating neuronal endolysosomal pH remain unclear. Transmembrane protein 184B (TMEM184B) is a conserved seven-pass transmembrane protein that is essential for synaptic function, and its sequence disruption is associated with neurodevelopmental disorders. Here, we identify TMEM184B as a key regulator of endolysosomal acidification. TMEM184B localizes to early and late endosomes, and proteomic analysis confirms that TMEM184B interacts with endosomal proteins, including the vacuolar ATPase (V-ATPase), a multi-subunit proton pump crucial for lumenal acidification. Tmem184b-mutant mouse cortical neu","dates":{"release":"2025-01-01T00:00:00Z","publication":"2025 Aug","modification":"2026-05-09T17:57:28.135Z","creation":"2026-04-08T01:08:11.763Z"},"accession":"S-EPMC12377713","cross_references":{"pubmed":["40586707"],"doi":["10.1242/jcs.263908"]}}