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突触处的活性控制蛋白水解。

Activity-controlled proteolytic cleavage at the synapse.

机构信息

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

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.

出版信息

Trends Neurosci. 2014 Aug;37(8):413-23. doi: 10.1016/j.tins.2014.05.007. Epub 2014 Jun 23.

DOI:10.1016/j.tins.2014.05.007
PMID:24969462
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.

摘要

在突触膜表面或突触或突触周隙的细胞外空间中,通过活性控制的酶促蛋白裂解,是直接调控突触结构、功能和数量的一种方式。最初,人们认为突触处的细胞外蛋白水解是一种使突触摆脱细胞外基质限制的可塑性机制。然而,最近的观察表明,至少部分细胞外蛋白裂解会激活以前隐藏的功能,这些功能调节着突触和神经元回路的适应性变化。在这里,我们重点介绍定位于突触的具有不同功能的肽酶,并结合神经元和突触活动的调节,评估它们在发育和/或成年期突触可塑性背景下的功能。

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