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Activity-controlled proteolytic cleavage at the synapse.

Peter Sonderegger1, Kazumasa Matsumoto-Miyai2

  • 1Department of Biochemistry, University of Zurich, Winterthurerstrasse 190, CH-8057 Zurich, Switzerland.

Trends in Neurosciences
|June 28, 2014
PubMed
Summary

Enzymatic protein cleavage at synapses regulates their structure and function. This process, controlled by neuronal activity, also activates hidden functions crucial for adaptive changes in neuronal circuits and synaptic plasticity.

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Area of Science:

  • Neuroscience
  • Molecular Biology
  • Biochemistry

Background:

  • Extracellular proteolysis at synapses was initially thought to primarily facilitate synaptic plasticity by overcoming extracellular matrix constraints.
  • Recent findings suggest extracellular protein cleavage also unmasks cryptic functions that drive adaptive synaptic and neuronal circuit modifications.

Purpose of the Study:

  • To investigate the role of activity-regulated peptidases at synapses.
  • To evaluate the function of these peptidases in developmental and adult synaptic plasticity.

Main Methods:

  • Focus on peptidases with specific synaptic localization and function.
  • Analysis of regulation by neuronal and synaptic activity.

Main Results:

  • Activity-controlled enzymatic cleavage directly impacts synaptic structure, function, and number.
  • Extracellular proteolysis contributes to adaptive changes in synapses and neuronal circuits by activating latent functions.

Conclusions:

  • Peptidases regulated by synaptic activity are key players in modulating synaptic plasticity.
  • Understanding these enzymatic processes is crucial for comprehending both developmental and adult brain adaptability.