| First Author | Jiang CH | Year | 2021 |
| Journal | Proc Natl Acad Sci U S A | Volume | 118 |
| Issue | 9 | PubMed ID | 33627404 |
| Mgi Jnum | J:305642 | Mgi Id | MGI:6509753 |
| Doi | 10.1073/pnas.2019194118 | Citation | Jiang CH, et al. (2021) The amino-terminal domain of GluA1 mediates LTP maintenance via interaction with neuroplastin-65. Proc Natl Acad Sci U S A 118(9):e2019194118 |
| abstractText | Long-term potentiation (LTP) has long been considered as an important cellular mechanism for learning and memory. LTP expression involves NMDA receptor-dependent synaptic insertion of AMPA receptors (AMPARs). However, how AMPARs are recruited and anchored at the postsynaptic membrane during LTP remains largely unknown. In this study, using CRISPR/Cas9 to delete the endogenous AMPARs and replace them with the mutant forms in single neurons, we have found that the amino-terminal domain (ATD) of GluA1 is required for LTP maintenance. Moreover, we show that GluA1 ATD directly interacts with the cell adhesion molecule neuroplastin-65 (Np65). Neurons lacking Np65 exhibit severely impaired LTP maintenance, and Np65 deletion prevents GluA1 from rescuing LTP in AMPARs-deleted neurons. Thus, our study reveals an essential role for GluA1/Np65 binding in anchoring AMPARs at the postsynaptic membrane during LTP. |
