| First Author | Antonelli R | Year | 2014 |
| Journal | Nat Commun | Volume | 5 |
| Pages | 5066 | PubMed ID | 25297980 |
| Mgi Jnum | J:330667 | Mgi Id | MGI:6212919 |
| Doi | 10.1038/ncomms6066 | Citation | Antonelli R, et al. (2014) Pin1-dependent signalling negatively affects GABAergic transmission by modulating neuroligin2/gephyrin interaction. Nat Commun 5:5066 |
| abstractText | The cell adhesion molecule Neuroligin2 (NL2) is localized selectively at GABAergic synapses, where it interacts with the scaffolding protein gephyrin in the post-synaptic density. However, the role of this interaction for formation and plasticity of GABAergic synapses is unclear. Here, we demonstrate that endogenous NL2 undergoes proline-directed phosphorylation at its unique S714-P consensus site, leading to the recruitment of the peptidyl-prolyl cis-trans isomerase Pin1. This signalling cascade negatively regulates NL2's ability to interact with gephyrin at GABAergic post-synaptic sites. As a consequence, enhanced accumulation of NL2, gephyrin and GABAA receptors was detected at GABAergic synapses in the hippocampus of Pin1-knockout mice (Pin1-/-) associated with an increase in amplitude of spontaneous GABAA-mediated post-synaptic currents. Our results suggest that Pin1-dependent signalling represents a mechanism to modulate GABAergic transmission by regulating NL2/gephyrin interaction. |
