Solomon H. Snyder Department of Neuroscience, Johns Hopkins University School of Medicine, Baltimore, MD 21205, USA.
Trends Neurosci. 2010 Nov;33(11):493-502. doi: 10.1016/j.tins.2010.07.004. Epub 2010 Sep 16.
Covalent modifications of intracellular proteins, such as phosphorylation, are generally thought to occur as secondary or tertiary responses to neurotransmitters, following the intermediation of membrane receptors and second messengers such as cyclic AMP. By contrast, the gasotransmitter nitric oxide directly S-nitrosylates cysteine residues in diverse intracellular proteins. Recently, hydrogen sulfide has been acknowledged as a gasotransmitter, which analogously sulfhydrates cysteine residues in proteins. Cysteine residues are also modified by palmitoylation in response to neurotransmitter signaling, possibly in reciprocity with S-nitrosylation. Neurotransmission also elicits sumoylation and acetylation of lysine residues within diverse proteins. This review addresses how these recently appreciated protein modifications impact our thinking about ways in which neurotransmission regulates intracellular protein disposition.
细胞内蛋白质的共价修饰，如磷酸化，通常被认为是神经递质的二级或三级反应，在膜受体和第二信使如环 AMP 的介导下发生。相比之下，气体递质一氧化氮直接将半胱氨酸残基 S-亚硝化作用于各种细胞内蛋白质。最近，硫化氢被认为是一种气体递质，它类似地将半胱氨酸残基硫氢化作用于蛋白质。半胱氨酸残基也可通过神经递质信号转导的棕榈酰化作用进行修饰，可能与 S-亚硝化作用相互作用。神经传递也会引起各种蛋白质中赖氨酸残基的 SUMO 化和乙酰化。这篇综述讨论了这些新出现的蛋白质修饰如何影响我们对神经传递调节细胞内蛋白质分布方式的思考。
