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利用光学可控蛋白研究神经元功能。

Investigating neuronal function with optically controllable proteins.

作者信息

Zhou Xin X, Pan Michael, Lin Michael Z

机构信息

Department of Bioengineering, Stanford University Stanford, CA, USA.

Department of Pediatrics, Stanford University Stanford, CA, USA.

出版信息

Front Mol Neurosci. 2015 Jul 21;8:37. doi: 10.3389/fnmol.2015.00037. eCollection 2015.

DOI:10.3389/fnmol.2015.00037
PMID:26257603
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC4508517/
Abstract

In the nervous system, protein activities are highly regulated in space and time. This regulation allows for fine modulation of neuronal structure and function during development and adaptive responses. For example, neurite extension and synaptogenesis both involve localized and transient activation of cytoskeletal and signaling proteins, allowing changes in microarchitecture to occur rapidly and in a localized manner. To investigate the role of specific protein regulation events in these processes, methods to optically control the activity of specific proteins have been developed. In this review, we focus on how photosensory domains enable optical control over protein activity and have been used in neuroscience applications. These tools have demonstrated versatility in controlling various proteins and thereby cellular functions, and possess enormous potential for future applications in nervous systems. Just as optogenetic control of neuronal firing using opsins has changed how we investigate the function of cellular circuits in vivo, optical control may yet yield another revolution in how we study the circuitry of intracellular signaling in the brain.

摘要

在神经系统中,蛋白质活性在空间和时间上受到高度调控。这种调控使得在发育和适应性反应过程中,神经元的结构和功能能够得到精细调节。例如,神经突延伸和突触形成都涉及细胞骨架和信号蛋白的局部和瞬时激活,从而使微结构能够快速且局部地发生变化。为了研究特定蛋白质调控事件在这些过程中的作用,人们开发了光学控制特定蛋白质活性的方法。在这篇综述中,我们重点关注光感结构域如何实现对蛋白质活性的光学控制,以及其在神经科学应用中的情况。这些工具已证明在控制各种蛋白质从而调控细胞功能方面具有多功能性,并且在神经系统的未来应用中具有巨大潜力。正如利用视蛋白对神经元放电进行光遗传学控制改变了我们在体内研究细胞回路功能的方式一样,光学控制可能会在我们研究大脑细胞内信号传导回路的方式上引发又一次革命。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/0332/4508517/1be2c002454c/fnmol-08-00037-g007.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/0332/4508517/f9d3f7f95540/fnmol-08-00037-g001.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/0332/4508517/e13d3e1c8eef/fnmol-08-00037-g002.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/0332/4508517/83c562f662aa/fnmol-08-00037-g003.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/0332/4508517/ab8497777291/fnmol-08-00037-g004.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/0332/4508517/34bd796f00aa/fnmol-08-00037-g005.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/0332/4508517/38d4339d15d3/fnmol-08-00037-g006.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/0332/4508517/1be2c002454c/fnmol-08-00037-g007.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/0332/4508517/f9d3f7f95540/fnmol-08-00037-g001.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/0332/4508517/e13d3e1c8eef/fnmol-08-00037-g002.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/0332/4508517/83c562f662aa/fnmol-08-00037-g003.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/0332/4508517/ab8497777291/fnmol-08-00037-g004.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/0332/4508517/34bd796f00aa/fnmol-08-00037-g005.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/0332/4508517/38d4339d15d3/fnmol-08-00037-g006.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/0332/4508517/1be2c002454c/fnmol-08-00037-g007.jpg

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