Ubiquitin C-terminal hydrolase L1 (UCH-L1): structure, distribution and roles in brain function and dysfunction.
Ubiquitin C-terminal hydrolase L1 (UCH-L1): structure, distribution and roles in brain function and dysfunction.
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DOI：
10.1042/bcj20160082
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发表时间：
2016-08-15
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影响因子：
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通讯作者：
Henley JM
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文献类型：
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作者：
Bishop P;Rocca D;Henley JM
泛素C-末端水解酶L1（UCH-L1）是脑中极其丰富的蛋白质，值得注意的是，估计其占总神经元蛋白质的1-5%。虽然它只包含223个氨基酸，但它具有迄今为止发现的最复杂的3D打结结构之一。除了在神经元中的表达外，UCH-L1在其他健康组织中的表达非常有限，但在几种癌症中高度表达。虽然UCH-L1被归类为去泛素化酶（DUB），但UCH-L1的直接功能仍然是个谜，并且已经提出了广泛的替代功能。UCH-L1对于神经元发育不是必需的，但对于维持轴突完整性是绝对必需的，并且UCH-L1功能障碍与神经退行性疾病有关。在这里，我们回顾UCH-L1的特性，以及如何了解其复杂的结构可以提供新的见解，其在神经元功能和病理学的作用。
Ubiquitin C-terminal hydrolase L1 (UCH-L1) is an extremely abundant protein in the brain where, remarkably, it is estimated to make up 1–5% of total neuronal protein. Although it comprises only 223 amino acids it has one of the most complicated 3D knotted structures yet discovered. Beyond its expression in neurons UCH-L1 has only very limited expression in other healthy tissues but it is highly expressed in several forms of cancer. Although UCH-L1 is classed as a deubiquitinating enzyme (DUB) the direct functions of UCH-L1 remain enigmatic and a wide array of alternative functions has been proposed. UCH-L1 is not essential for neuronal development but it is absolutely required for the maintenance of axonal integrity and UCH-L1 dysfunction is implicated in neurodegenerative disease. Here we review the properties of UCH-L1, and how understanding its complex structure can provide new insights into its roles in neuronal function and pathology.