{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Adoff H"],"funding":["NIGMS NIH HHS","NIH HHS"],"pagination":["ar114"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC12404652"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["36(9)"],"pubmed_abstract":["Endosomes are a central sorting hub for membrane cargos. DNAJC13/RME-8 plays a critical role in endosomal trafficking by regulating the endosomal recycling and degradative pathways. DNAJC13 localizes to endosomes through its N-terminal Pleckstrin Homology (PH)-like domain, which binds endosomal phosphatidylinositol-3-phosphate (PI(3)P). However, little is known about how DNAJC13 localization is regulated. Here, we show that two regions within DNAJC13, its J domain and disordered C-terminus, act as negative regulators of its PH-like domain. Using a structure-function approach, we map these control points to a conserved YLT motif in the disordered C-terminus as well as the catalytic HPD triad in its J domain. Mutation of either motif enhances DNAJC13 endosomal localization in cells and incre"],"journal":["Molecular biology of the cell"],"pubmed_title":["DNAJC13 localization to endosomes is opposed by its J domain and its disordered C-terminus."],"pmcid":["PMC12404652"],"funding_grant_id":["S10 OD034224","R35 GM137835","T32 GM142619"],"pubmed_authors":["Adoff H","Lobingier BT","Novy B","Holland E"],"additional_accession":[]},"is_claimable":false,"name":"DNAJC13 localization to endosomes is opposed by its J domain and its disordered C-terminus.","description":"Endosomes are a central sorting hub for membrane cargos. DNAJC13/RME-8 plays a critical role in endosomal trafficking by regulating the endosomal recycling and degradative pathways. DNAJC13 localizes to endosomes through its N-terminal Pleckstrin Homology (PH)-like domain, which binds endosomal phosphatidylinositol-3-phosphate (PI(3)P). However, little is known about how DNAJC13 localization is regulated. Here, we show that two regions within DNAJC13, its J domain and disordered C-terminus, act as negative regulators of its PH-like domain. Using a structure-function approach, we map these control points to a conserved YLT motif in the disordered C-terminus as well as the catalytic HPD triad in its J domain. Mutation of either motif enhances DNAJC13 endosomal localization in cells and incre","dates":{"release":"2025-01-01T00:00:00Z","publication":"2025 Sep","modification":"2026-06-03T06:06:47.504Z","creation":"2026-04-25T03:21:17.38Z"},"accession":"S-EPMC12404652","cross_references":{"pubmed":["40737286"],"doi":["10.1091/mbc.E24-12-0575"]}}