Benson Mark, Iñiguez-Lluhí Jorge A, Martens Jeffrey
Department of Pharmacology, University of Michigan, Ann Arbor, MI, USA.
Adv Exp Med Biol. 2017;963:127-141. doi: 10.1007/978-3-319-50044-7_8.
Recently, a role for SUMO modification outside of the nucleus has emerged. Although the number of extranuclear proteins known to be sumoylated is comparatively small, ion channels represent one important new class of these proteins. Ion channels are responsible for the control of membrane excitability and therefore are critical for fundamental physiological processes such as muscle contraction, neuronal firing, and cellular homeostasis. As such, these ion-conducting proteins are subject to precise regulation. Recently, several studies have identified sumoylation as a novel mechanism of modulating ion channel function. These studies expand the list of known functions of sumoylation and reveal that, in addition to its more established role in the regulation of nuclear proteins, this modification plays important roles at the cytoplasmic face of membranes.
最近,小泛素样修饰蛋白(SUMO)在细胞核外的作用已逐渐显现。虽然已知发生SUMO化修饰的核外蛋白数量相对较少,但离子通道是这类蛋白中的一个重要新类别。离子通道负责控制膜兴奋性,因此对于肌肉收缩、神经元放电和细胞内稳态等基本生理过程至关重要。正因如此,这些离子传导蛋白受到精确调控。最近,多项研究已确定SUMO化修饰是调节离子通道功能的一种新机制。这些研究扩展了已知的SUMO化修饰功能列表,并揭示出,除了在调节核蛋白方面已确立的作用外,这种修饰在细胞膜的胞质面也发挥重要作用。