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Synaptic Autoregulation by Metalloproteases and γ-Secretase
Abstract
The proteolytic machinery comprising metalloproteases and γ-secretase, an intramembrane aspartyl protease involved in Alzheimer's disease, cleaves several substrates in addition to the extensively studied amyloid precursor protein. Some of these substrates, such as N-cadherin, are synaptic proteins involved in synapse remodeling and maintenance. Here we show, in rats and mice, that metalloproteases and γ-secretase are physiologic regulators of synapses. Both proteases are synaptic, with γ-secretase tethered at the synapse by δ-catenin, a synaptic scaffolding protein that also binds to N-cadherin and, through scaffolds, to AMPA receptor and a metalloprotease. Activity-dependent proteolysis by metalloproteases and γ-secretase takes place at both sides of the synapse, with the metalloprotease cleavage being NMDA receptor-dependent. This proteolysis decreases levels of synaptic proteins and diminishes synaptic transmission. Our results suggest that activity-dependent substrate cleavage by synaptic metalloproteases and γ-secretase modifies synaptic transmission, providing a novel form of synaptic autoregulation.
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MT5-MMP can modulate neuronal activity.
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Metadata
- Authors
- Restituito, S., Khatri, L., Ninan, I., Mathews, P. M., Liu, X., Weinberg, R. J., & Ziff, E. B.
- Venue
- The Journal of Neuroscience
- Publisher
- Society for Neuroscience
- Published
- 2011-08-24
- Volume
- 31
- Issue
- 34
- Pages
- 12083-12093
- ISSN
- 0270-6474
- 1529-2401
- PMC
- PMC3169340
- Cited by
- 70
- References
- 5
- Language
- en
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