| Annotated protein: | Cofilin-1 (Cofilin, non-muscle isoform). Gene symbol: CFL1. Taxonomy: Rattus norvegicus (Rat). Uniprot ID: P45592 |
| antibody wiki: | |
| SynGO gene info: | SynGO data @ CFL1 |
| Ontology domain: | Biological Process |
| SynGO term: | modification of postsynaptic actin cytoskeleton (GO:0098885) |
| Synapse type(s): | hippocampus, glutamatergic |
| Annotated paper: | Morishita W, et al. "Distinct triggering and expression mechanisms underlie LTD of AMPA and NMDA synaptic responses" Nat Neurosci. 2005 Aug;8(8):1043-50 PMID:16025109 |
| Figure(s): | Fig. 6 |
| Annotation description: | Electrophysiology evidences showed that LTD of NMDAR EPSCs is blocked by a peptide that inhibits cofilin-1. 29/5/2017 Pim -Cofilin dom.neg. phospho-peptide was traced back to sequence MASGVAVSDGVIKVFN via PMID:15572107. Blast on uniprot website showed two ungapped hits in rat sequences (P45592(cofilin); A0A0G2KA35(partial cofilin clone in TrEMBL)). The peptide therefore can be regarded seen as specific for cofilin 1. - Uniprot states for cofillin-1: "Binds to F-actin and exhibits pH-sensitive F-actin depolymerizing activity" Since cofillin itself is known to exhibit actin-depolymerase activity, I have left the "regulates...." modification of synaptic structure uncheck since I reasoned that cofilin is performing the structure modification itself. - Fig.6 shows that loading of postsynaptic neurons with a a phosphorylated cofilin peptide bloacked LTD of NMDAR EPSCs. |
| Evidence tracking, Biological System: | Intact tissue |
| Evidence tracking, Protein Targeting: | Antagonist / agonist |
| Evidence tracking, Experiment Assay: | Whole-cell patch clamp |
| Annotator(s): | Alexandros Kanellopoulos (ORCID:0000-0002-2094-7491) Vittoria Mariano (ORCID:0000-0002-9848-0262) Achsel Tilmann (ORCID:0000-0002-1190-4481) Claudia Bagni (ORCID:0000-0002-4419-210X) |
| Lab: | Department of Fundamental Neurosciences, University of Lausanne, CH-1006 Lausanne, Switzerland; Dept Biomedicine and Prevention, University of Rome Tor Vergata, 00133 Rome, Italy |
| Additional literature: | Binds to F-actin and exhibits pH-sensitive F-actin depolymerizing activity. Activity of Cofilin Is Involved in the Spine Shrinkage Associated with LTD, in Hippocampal slices from Sprague-Dawley rat (P14 and P18) Figure 4. @ PMID:15572107 |
| SynGO annotation ID: | 507 |
| Dataset release (version): | 20231201 |
| View annotation as GO-CAM model: |  |