| First Author | Moutin E | Year | 2012 |
| Journal | J Cell Sci | Volume | 125 |
| Issue | Pt 8 | Pages | 2030-40 |
| PubMed ID | 22328512 | Mgi Jnum | J:197297 |
| Mgi Id | MGI:5492019 | Doi | 10.1242/jcs.098160 |
| Citation | Moutin E, et al. (2012) GKAP-DLC2 interaction organizes the postsynaptic scaffold complex to enhance synaptic NMDA receptor activity. J Cell Sci 125(Pt 8):2030-40 |
| abstractText | At glutamatergic brain synapses, scaffolding proteins regulate receptor location and function. The targeting and organization of scaffolding proteins in the postsynaptic density (PSD) is poorly understood, but it is known that a core protein of the glutamatergic receptor postsynaptic scaffold complex, guanylate-kinase-associated protein (GKAP) interacts with dynein light chain 2 (DLC2, also known as DYNLL2), a protein associated with molecular motors. In the present study, we combined BRET imaging, immunostaining and electrophysiological recording to assess the role of the GKAP-DLC2 interaction in the functional organization of the glutamatergic synapse. We found that GKAP-DLC2 interaction in dendritic spine stabilizes scaffolding protein expression at the PSD and enhances synaptic NMDA receptor activity. Moreover, the GKAP-DLC2 functional interaction is favored by sustained synaptic activity. These data identify a regulatory pathway of synaptic transmission that depends on activity-induced remodelling of the postsynaptic scaffold protein complex. |
