FEBS Letters · 2012 · 36 citations · 11 references
Life SciencesBiochemistryMolecular BiologyMembrane TraffickingProtein-protein InteractionsSignal TransductionEndomembrane SystemEnzyme FunctionGolgi TraffickingOrganelle Contact SitesProtein-lipid InteractionsSecretory PathwayGolgi Apparatus TargetingGolgi Contact SitesGolgi Membrane TraffickingMembrane Targeting By Lipid BindingPhosphatase Activation MechanismsPhosphatase-scaffold InteractionsProtein Phosphatase Complexes
The metal-dependent protein phosphatase family (PPM) governs a number of signaling pathways. PPM1L, originally identified as a negative regulator of stress-activated protein kinase signaling, was recently shown to be involved in the regulation of ceramide trafficking at ER-Golgi membrane contact sites. Here, we identified acyl-CoA binding domain containing 3 (ACBD3) as an interacting partner of PPM1L. We showed that this association, which recruits PPM1L to ER-Golgi membrane contact sites, is mediated by a GOLD (Golgi dynamics) domain in ACBD3. These results suggested that ACBD3 plays a pivotal role in ceramide transport regulation at the ER-Golgi interface.
11
Sharon E. Reed, Elizabeth M. Staley, John P. Mayginnes et al. · Journal of Virological Methods · 2006 · 260 citations