Journal
NEURON
Volume 57, Issue 6, Pages 858-871Publisher
CELL PRESS
DOI: 10.1016/j.neuron.2008.01.010
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Funding
- Intramural NIH HHS Funding Source: Medline
- NINDS NIH HHS [R01 NS039156, R01 NS039156-08, 5R01NS039156-08] Funding Source: Medline
- PHS HHS [R37MM51106] Funding Source: Medline
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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-a 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.
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