STARD3 regulates late endosome positioning via a GSK3-controlled phosphorylation switch

ABSTRACT: Membrane contact sites (MCS) are dynamic regions where the membranes of two organelles come into close apposition. MCSs play many roles in cellular homeostasis by facilitating inter-organelle lipid exchange and organelle positioning. The late endosome/lysosome (LE/Lys) cholesterol transfer protein STARD3 forms reversible contacts between LE/Lys and the endoplasmic reticulum (ER). This tether protein contains a phospho-FFAT motif (two phenylalanines in an acidic tract) whose interaction with ER-resident VAPs (vesicle-associated membrane protein-associated proteins) is phosphorylation-dependent. In this study, we identify GSK3α and GSK3β as the kinases responsible for phosphorylating serine 209 within the phospho-FFAT motif of STARD3. This phosphorylation event is both necessary and sufficie

SUBMITTER: Julie Eichler 

PROVIDER: S-SCDT-10_1038-S44318-026-00705-3 | biostudies-other |

REPOSITORIES: biostudies-other