| Annotated protein: | Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) (EC 1.2.1.12) (Peptidyl-cysteine S-nitrosylase GAPDH) (EC 2.6.99.-). Gene symbol: GAPDH. Taxonomy: Bos taurus (Bovine). Uniprot ID: P10096 |
| antibody wiki: | |
| SynGO gene info: | SynGO data @ GAPDH |
| Ontology domain: | Cellular Component |
| SynGO term: | extrinsic component of synaptic vesicle membrane (GO:0098850) |
| Synapse type(s): | cerebrum |
| Annotated paper: | Ikemoto A, et al. "Glycolysis and glutamate accumulation into synaptic vesicles. Role of glyceraldehyde phosphate dehydrogenase and 3-phosphoglycerate kinase" J Biol Chem. 2003 Feb 21;278(8):5929-40 PMID:12488440 |
| Figure(s): | Figure 1, 5 |
| Annotation description: | Results Section 1: -Literal: "Purified syn- aptic vesicles were allowed to react with [3-32P]1,3-BPG for 10 s and subjected to SDS-PAGE at either neutral (Fig. 1A) or alkaline (Fig. 1B) pH (39, 40). Electrophoresis at neutral pH revealed incorporation of a radioactive moiety of [3-32P]1,3- BPG into vesicular proteins of Mr 37,000 and 29,000. In contrast, electrophoresis at alkaline pH revealed only the 29- kDa protein, which appears to retain more of the 32P label than when electrophoresis was conducted at neutral pH. These re- sults indicate that both the 29- and 37-kDa vesicular proteins can incorporate a 32P-containing moiety; however, the stability of the labeled proteins differs depending on pH. Incorporation of the radioactive moiety into the 37-kDa protein was stimu- lated by Mg2 but not affected by 3-PG. Labeling of the 29-kDa protein was inhibited by Mg2 and completely blocked by 3-PG. The linkage of the 32P-containing moiety to the 37-kDa protein was labile in the presence of 0.2 M hydroxylamine (data not shown). These observations suggested that the 37- and 29-kDa proteins might be GAPDH and PGM, respectively. This was confirmed by immunoprecipitation with antibodies directed against these proteins (Fig. 1C). Thus, labeling of the 37-kDa GAPDH with [3-32P]1,3-BPG probably occurs by formation of a thioester bond between a cysteine residue and the 3-phospho- glyceroyl moiety of 1,3-BPG; thioester bonds are known to be labile at alkaline pH. Labeling of the 29-kDa PGM probably represents phosphorylation of a histidine residue that is labile at either neutral or acidic pH." 24/01/2018 Pim - GAPDH is membrane bound. Literal: " To determine the nature of the interaction of GAPDH with synaptic vesicles, synaptic vesicles were treated with various concentrations of NaCl (Fig. 1 F). GAPDH was dissociated from synaptic vesicles with increasing salt concentrations. At 0.8 M NaCl, only about 10% of GAPDH was found to remain associated with synaptic vesicle membranes. At physiologic ionic strength, GAPDH is associated with synaptic vesicle membranes, although it does also occur in the cytosol fractions" |
| Evidence tracking, Biological System: | Intact tissue |
| Evidence tracking, Protein Targeting: | Antagonist / agonist Antibody (detection) |
| Evidence tracking, Experiment Assay: | Western blot Biochemical fractionation (generic) Transmembrane transport assay |
| Annotator(s): | Rita Reig-Viader (ORCID:0000-0002-6893-6177) Àlex Bayés (ORCID:0000-0002-5265-6306) |
| Lab: | Molecular Physiology of the Synapse Laboratory, Biomedical Research Institute Sant Pau, 08025 Barcelona, Spain and and Universitat Autnoma de Cerdanyola del Valls, Spain Barcelona, 08193 Bellaterra |
| SynGO annotation ID: | 2348 |
| Dataset release (version): | 20231201 |
| View annotation as GO-CAM model: |  |