| Annotated protein: | Alpha/beta hydrolase domain-containing protein 17A (Abhydrolase domain-containing protein 17A) (EC 3.1.2.22). Gene symbol: ABHD17A. Taxonomy: Rattus norvegicus (Rat). Uniprot ID: Q5XIJ5 |
| antibody wiki: | |
| SynGO gene info: | SynGO data @ ABHD17A |
| Ontology domain: | Cellular Component |
| SynGO term: | anchored component of postsynaptic density membrane (GO:0099031) |
| Synapse type(s): | hippocampus, glutamatergic |
| Annotated paper: | Yokoi N, et al. "Identification of PSD-95 Depalmitoylating Enzymes" J Neurosci. 2016 Jun 15;36(24):6431-44 PMID:27307232 |
| Figure(s): | Fig.3A, H |
| Annotation description: | Figure 3: "Subcellular distribution of ABHD17" - "We further examined the localization of ABHD17B mutants (Fig. 2D) together with endogenous PSD-95 in neurons (Fig. 3D). Although overexpression of wild-type ABHD17B robustly reduced the PSD-95 cluster intensity and spine density (analyzed in detail in Fig. 6), ABHD17B was overlapped with or apposed to endogenous PSD-95 in the surviving dendritic spine. Enzymatically inactive ABHD17B-D235A, which did not affect PSD-95 clusters, was distributed to the plasma membrane and some vesicular-like structure in dendritic shafts and spines. ABHD17B-D235A clearly showed the colocalization with or apposition to PSD-95 and TfR in the dendritic spines. Palmitoylation-deficient ABHD17B-5CS showed diffuse cytoplasmic localization in the dendritic shaft and spines, and myristoylated N-myr-ABHD17B was distributed to the plasma membrane of dendritic shafts/spines more diffusely without making clear clusters than ABHD17B WT and D235A. Interestingly, ABHD17B-5CS and N-myr-ABHD17B, which were partially overlapped with endogenous PSD-95 in the dendritic spine, did not affect the PSD-95 clusters, possibly correlated with their loss of enzymatic activity (Fig. 2F)." - "All the ABHD17 members were distributed to the microsomal P3 (containing ER, Golgi apparatus, and parts of endosomes) and synaptosome fractions, and some populations localized in the PSD fraction (Fig. 3H)." |
| Evidence tracking, Biological System: | Intact tissue Cultured neurons |
| Evidence tracking, Protein Targeting: | Over-expression Antibody (detection) |
| Evidence tracking, Experiment Assay: | Confocal Western blot Biochemical fractionation (generic) |
| Annotator(s): | Pim van Nierop (ORCID:0000-0003-0593-3443) Guus Smit (ORCID:0000-0002-2286-1587) Matthijs Verhage (ORCID:0000-0002-2514-0216) |
| Lab: | Department of Functional Genomics, Department of Molecular and Cellular Neurobiology, Center for Neurogenomics and Cognitive Research, Vrije Universiteit Amsterdam, 1081 HV Amsterdam, The Netherlands |
| Additional literature: | The ABHD17 proteins are targeted to membranes by a palmitoylated N-terminal cysteine cluster. This membrane targeting is essential for their enzymatic activity. @ PMID:19092927 |
| SynGO annotation ID: | 2630 |
| Dataset release (version): | 20231201 |
| View annotation as GO-CAM model: |  |