Sumoylation and human disease pathogenesis.

Sumoylation and human disease pathogenesis.
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DOI:
10.1016/j.tibs.2009.01.004
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发表时间:
2009-04
影响因子:
13.8
通讯作者:
Park-Sarge OK
Park-Sarge OK
中科院分区:
生物学1区
文献类型:
--
作者:
Sarge KD;Park-Sarge OK

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SUMO 多肽的共价修饰或苏酰化是许多蛋白质功能特性的重要调节剂。其中有许多与人类疾病有关的蛋白质,包括癌症、亨廷顿病、阿尔茨海默病和帕金森病,以及脊髓小脑共济失调 1 和肌萎缩侧索硬化症。最近的报告揭示了两个经过 SUMO 修饰的人类疾病相关蛋白的新例子:淀粉样蛋白前体蛋白和核纤层蛋白 A。这些发现指出了苏木化在调节 Aβ 肽水平方面的功能,表明其在阿尔茨海默病中具有潜在作用,并且核纤层蛋白 A 苏木化减少是家族性扩张型心肌病的致病因素。
Covalent modification by SUMO polypeptides, or sumoylation, is an important regulator of the functional properties of many proteins. Among these are a number of proteins implicated in human diseases, including cancer, Huntington’s, Alzheimer’s, and Parkinson’s Diseases, as well as spinocerebellar ataxia 1 and amyotrophic lateral sclerosis. Recent reports reveal two new examples of human disease-associated proteins that are SUMO modified: amyloid precursor protein and lamin A. These findings point to a function for sumoylation in modulating Aβ peptide levels, suggesting a potential role in Alzheimer’s Disease, and for decreased lamin A sumoylation as a causative factor in familial dilated cardiomyopathy.
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