mGluR1/5-Dependent long-term depression requires the regulated ectodomain cleavage of neuronal pentraxin NPR by TACE

被引：109

作者：

Cho, Richard W. ^{[1
]}

Park, Joo Min ^{[1
]}

Wolff, Steffen B. E. ^{[1
]}

Xu, Desheng ^{[1
]}

Hopf, Carsten ^{[1
]}

Kim, Jin-ah ^{[1
]}

Reddy, Radhika C. ^{[1
]}

Petralia, Ronald S. ^{[3
]}

Perin, Mark S. ^{[4
]}

Linden, David J. ^{[1
]}

Worley, Paul F. ^{[1
,2
]}

机构：

[1] Johns Hopkins Univ, Sch Med, Dept Neurosci, Baltimore, MD 21205 USA

[2] Johns Hopkins Univ, Sch Med, Dept Neurol, Baltimore, MD 21205 USA

[3] Natl Inst Deafness & Other Communicat Disorders, Neurochem Lab, NIH, Bethesda, MD 20892 USA

[4] Cleveland Clin Fdn, Dept Neurosci, Cleveland, OH 44195 USA

来源：

NEURON | 2008年 / 57卷 / 06期

关键词：

D O I：

10.1016/j.neuron.2008.01.010

中图分类号：

Q189 [神经科学];

学科分类号：

071006 ;

摘要：

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.

引用

页码：858 / 871

页数：14

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