Department of Molecular and Cellular Biochemistry, University of Kentucky, Lexington, Kentucky, USA.
Int Rev Cell Mol Biol. 2011;288:167-83. doi: 10.1016/B978-0-12-386041-5.00004-2.
The covalent attachment of small ubiquition-like modifier (SUMO) polypeptides, or sumoylation, is an important regulator of the functional properties of many proteins. Among these are many proteins implicated in human diseases including cancer and Huntington's, Alzheimer's, and Parkinson's diseases, as well as spinocerebellar ataxia 1 and amyotrophic lateral sclerosis. The results of two more recent studies identify two additional human disease-associated proteins that are sumoylated, amyloid precursor protein (APP), and lamin A. APP sumoylation modulates Aβ peptide levels, suggesting a potential role in Alzheimer's disease, and decreased lamin A sumoylation due to mutations near its SUMO site has been implicated in causing some forms of familial dilated cardiomyopathy.
小分子泛素样修饰物（SUMO）多肽的共价连接，或称为 SUMO 化，是许多蛋白质功能特性的重要调节因子。这些蛋白质中有许多与人类疾病有关，包括癌症和亨廷顿氏病、阿尔茨海默病、帕金森病，以及脊髓小脑共济失调 1 型和肌萎缩性侧索硬化症。最近的两项研究结果确定了另外两种与人类疾病相关的 SUMO 化蛋白，即淀粉样前体蛋白（APP）和核纤层蛋白 A。APP 的 SUMO 化调节 Aβ 肽水平，提示其在阿尔茨海默病中的潜在作用，而其 SUMO 结合位点附近的突变导致的核纤层蛋白 A 的 SUMO 化减少与某些形式的家族性扩张型心肌病有关。
