Institute for Transformative Molecular Medicine, Case Western Reserve University School of Medicine and University Hospitals, Cleveland, OH 44106, USA.
Curr Opin Chem Biol. 2011 Feb;15(1):129-36. doi: 10.1016/j.cbpa.2010.10.012. Epub 2010 Nov 17.
Cell signaling is a complex and highly regulated process. Post-translational modifications of proteins serve to sense and transduce cellular signals in a precisely coordinated manner. It is increasingly recognized that protein S-nitrosylation, the addition of a nitric oxide group to cysteine thiols, serves an important role in a wide range of signaling pathways. In spite of the large number of SNO-proteins now identified (∼1000), the observed specificity of S-nitrosylation in terms of target proteins and specific cysteines within modified proteins is incompletely understood. Here we review the progress made in S-nitrosylation detection methods that have facilitated the study of the SNO-proteome under physiological and pathophysiological conditions, and some factors important in determining the SNO-proteome. Classification schemes for emergent denitrosylases and prospective 'protein S-nitrosylases' are provided.
细胞信号转导是一个复杂且高度调控的过程。蛋白质的翻译后修饰可用于以精确协调的方式感知和转导细胞信号。人们越来越认识到，蛋白质的 S-亚硝基化（将一氧化氮基团添加到半胱氨酸巯基上）在广泛的信号通路中起着重要作用。尽管现在已经鉴定出了大量的 SNO-蛋白（约 1000 个），但在修饰蛋白质中的靶蛋白和特定半胱氨酸方面，S-亚硝基化的观察到的特异性仍不完全清楚。在这里，我们回顾了在生理和病理生理条件下促进 SNO-蛋白质组研究的 S-亚硝基化检测方法的进展，以及一些决定 SNO-蛋白质组的重要因素。还提供了新兴的去亚硝酰酶和预期的“蛋白质 S-亚硝酰酶”的分类方案。
