title: Activity-controlled proteolytic cleavage at the synapse.
abstract: Activity-controlled enzymatic cleavage of proteins on the surface of synaptic membranes or in the synaptic or perisynaptic interstitial compartment represents a direct way to regulate synaptic structure, function, and number. Extracellular proteolysis at synapses was initially understood to be plasticity enabling by freeing synapses from the constraints provided by the extracellular matrix. However, recent observations indicate that at least part of the extracellular protein cleavage results in activation of previously cryptic functions that regulate adaptive changes of synapses and neuronal circuits. Here, we focus on peptidases with distinct localization and function at synapses combined with regulation by neuronal and synaptic activity, and evaluate their function in the context of developmental and/or adult synaptic plasticity.
authors: Department of Biochemistry, University of Zurich, Winterthurerstrasse 190, CH-8057 Zurich, Switzerland. Electronic address: Peter.Sonderegger@bioc.uzh.ch.
authors: Peter
authors: P
authors: Sonderegger
authors: Department of Neurophysiology, Akita University Graduate School of Medicine, 1-1-1 Hondo, Akita, Akita 010-8543, Japan; Kansai University of Nursing and Health Sciences, 1456-4 Shizuki, Awaji, Hyogo 656-2131, Japan.
authors: Kazumasa
authors: K
authors: Matsumoto-Miyai
mesh_terms: D000818:Animals; D005109:Extracellular Matrix / Q000187:drug effects / Q000502:physiology; D006801:Humans; D009415:Nerve Net / Q000187:drug effects / Q000502:physiology*; D010447:Peptide Hydrolases / Q000494:pharmacology; D059748:Proteolysis / Q000187:drug effects; D013569:Synapses / Q000187:drug effects / Q000502:physiology*
chemical_list: D010447:Peptide Hydrolases