| Annotated protein: | Tyrosine-protein kinase Yes (EC 2.7.10.2) (p61-Yes). Gene symbol: YES1. Taxonomy: Rattus norvegicus (Rat). Uniprot ID: F1LM93 |
| antibody wiki: | |
| SynGO gene info: | SynGO data @ YES1 |
| Ontology domain: | Cellular Component |
| SynGO term: | postsynaptic specialization, intracellular component (GO:0099091) |
| Synapse type(s): | brain, glutamatergic |
| Annotated paper: | Kalia LV, et al. "Interactions between Src family protein tyrosine kinases and PSD-95" Neuropharmacology. 2003 Nov;45(6):720-8 PMID:14529711 |
| Figure(s): | Fig. 1, Fig. 2 and Fig. 4. |
| Annotation description: | Fig. 1. Yes protein tyrosine kinase is partially localized in the PSD fraction. Literal: "The subcellular distribution of Src has been previously determined (Huang et al., 2001) and thus Src was used as a positive control in these experiments. The pattern of relative abundance of Lck and Lyn in the various subcellular fractions, as compared with the starting homogenate (H), was similar to that of Src (Fig. 1A). In contrast, the pattern of relative abundance of Yes was distinct from that of Src (Fig. 1A) but similar to that of Fyn (not illustrated)." Fig. 2, using synaptosomal preparation Yes co-immunoprecipitates with PSD-95. Literal: PSD-95 was immunoprecipitated using a monoclonal anti-PSD-95 antibody and we found a doublet corresponding to PSD-95 in the starting material and immunoprecipitates (Fig. 2). We also found that the immunoprecipitates contained the NR2A subunit of the NMDA receptor (NMDAR2A) indicating that the conditions were appropriate for detecting co-immunoprecipitation of proteins associated with PSD-95. Using these conditions, we found that Lyn, Src, and Yes, but not Lck, were co-immunoprecipitated with PSD-95 (Fig. 2)." Fig. 4. yes binds directly to PSD-95 in a GST-pulldown experiment. Literal: "To determine whether PSD-95 may interact directly with Lyn, Src, or Yes PTKs, we performed in vitro binding experiments with purified recombinant Lyn, Src, and Yes proteins, and GST fusion proteins containing regions of PSD-95. As illustrated in Fig. 4A, these regions were the N-terminal half of PSD-95 including the three PDZ domains (GST-PDZ123), the SH3 domain (GST-SH3), and the guanylate kinase homology domain (GST-GK). We found that GST-PDZ123 pulled down Lyn, Src, or Yes in vitro. Likewise GST-SH3 pulled down each of the three Src family kinases (Fig. 4B). ... From these findings, we concluded that Lyn, Src, and Yes may interact directly with PSD-95 via the PDZ123 or SH3 regions but not the GK region." |
| Evidence tracking, Biological System: | Intact tissue Non-neuronal tissue |
| Evidence tracking, Protein Targeting: | Antibody (detection) |
| Evidence tracking, Experiment Assay: | Western blot Biochemical fractionation (generic) IP + WB/MSMS |
| Annotator(s): | Chiara Verpelli (ORCID:0000-0003-2949-9725) Carlo Sala (ORCID:0000-0003-0662-9523) |
| Lab: | CNR Neuroscience Institute Milan and Dept. of Biotechnology and Translational Medicine, University of Milan, 20129 Milan, Italy |
| SynGO annotation ID: | 1908 |
| Dataset release (version): | 20231201 |
| View annotation as GO-CAM model: |  |