| First Author | Cho RW | Year | 2008 |
| Journal | Neuron | Volume | 57 |
| Issue | 6 | Pages | 858-71 |
| PubMed ID | 18367087 | Mgi Jnum | J:136046 |
| Mgi Id | MGI:3795027 | Doi | 10.1016/j.neuron.2008.01.010 |
| Citation | Cho RW, et al. (2008) mGluR1/5-dependent long-term depression requires the regulated ectodomain cleavage of neuronal pentraxin NPR by TACE. Neuron 57(6):858-71 |
| abstractText | Matrix metalloproteases (MMPs) play a role in remodeling the extracellular matrix during brain development and have been implicated in synaptic plasticity. Here, we report that a member of the neuronal pentraxin (NP) family, neuronal pentraxin receptor (NPR), undergoes regulated cleavage by the MMP tumor necrosis factor-alpha converting enzyme (TACE). NPR is enriched at excitatory synapses where it associates with AMPA-type glutamate receptors (AMPAR) and enhances synaptogenesis. However, in response to activation of group 1 mGluRs (mGluR1/5), TACE cleaves NPR and releases the pentraxin domain from its N-terminal transmembrane domain. Cleaved NPR rapidly accumulates in endosomes where it colocalizes with AMPAR. This process is necessary for mGluR1/5-dependent LTD in hippocampal and cerebellar synapses. These observations suggest that cleaved NPR functions to 'capture' AMPAR for endocytosis and reveal a bifunctional role of NPs in both synapse strengthening and weakening. |
