SUMO化与人类疾病发病机制。
Sumoylation and human disease pathogenesis.
作者信息
Sarge Kevin D, Park-Sarge Ok-Kyong
机构信息
Department of Molecular and Cellular Biochemistry, Chandler Medical Center, University of Kentucky, Lexington, KY 40536, USA.
出版信息
Trends Biochem Sci. 2009 Apr;34(4):200-5. doi: 10.1016/j.tibs.2009.01.004. Epub 2009 Mar 11.
Abstract
Covalent modification by SUMO polypeptides, or sumoylation, is an important regulator of the functional properties of many proteins. Among these are several 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 amyloid-beta peptide levels, indicating a potential role in Alzheimer's disease, and for decreased lamin A sumoylation as a causative factor in familial dilated cardiomyopathy.
摘要
小泛素样修饰蛋白（SUMO）多肽的共价修饰，即SUMO化，是许多蛋白质功能特性的重要调节因子。其中包括几种与人类疾病相关的蛋白质，这些疾病包括癌症、亨廷顿舞蹈症、阿尔茨海默病、帕金森病，以及脊髓小脑共济失调1型和肌萎缩侧索硬化症。最近的报告揭示了两个新的经SUMO修饰的与人类疾病相关的蛋白质例子：淀粉样前体蛋白和核纤层蛋白A。这些发现表明SUMO化在调节β淀粉样肽水平方面具有功能，这暗示了其在阿尔茨海默病中的潜在作用，以及核纤层蛋白A SUMO化减少是家族性扩张型心肌病的一个致病因素。
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