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泛素蛋白酶体系统介导的突触蛋白降解

Synaptic protein degradation by the ubiquitin proteasome system.

作者信息

Bingol Baris, Schuman Erin M

机构信息

Division of Biology 114-96, California Institute of Technology, Howard Hughes Medical Institute Pasadena, CA 91125, USA.

出版信息

Curr Opin Neurobiol. 2005 Oct;15(5):536-41. doi: 10.1016/j.conb.2005.08.016.

Abstract

Synaptic plasticity -- the modulation of synaptic strength between a presynaptic terminal and a postsynaptic dendrite -- is thought to be a mechanism that underlies learning and memory. It has become increasingly clear that regulated protein synthesis is an important mechanism used to regulate the protein content of synapses that results in changes in synaptic strength. Recent experiments have highlighted a role for the opposing process, that is, regulated protein degradation via the ubiquitin-proteasome system, in synaptic plasticity. These recent findings raise exciting questions as to how proteasomal activity can regulate synapses over different temporal and spatial scales.

摘要

突触可塑性——突触前终末与突触后树突之间突触强度的调节——被认为是学习和记忆的潜在机制。越来越清楚的是,受调控的蛋白质合成是一种重要机制,用于调节突触的蛋白质含量,进而导致突触强度的变化。最近的实验突出了相反过程的作用,即通过泛素-蛋白酶体系统进行的受调控的蛋白质降解,在突触可塑性中的作用。这些最新发现引发了关于蛋白酶体活性如何在不同的时间和空间尺度上调节突触的令人兴奋的问题。

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