Schorova Lenka, Martin Stéphane
Institut de Pharmacologie Moléculaire et Cellulaire, Centre National de la Recherche Scientifique (UMR7275), University of Nice-Sophia-Antipolis, Laboratory of Excellence "Network for Innovation on Signal Transduction, Pathways in Life Sciences" Valbonne, France.
Front Synaptic Neurosci. 2016 Apr 28;8:9. doi: 10.3389/fnsyn.2016.00009. eCollection 2016.
Sumoylation has recently emerged as a key post-translational modification involved in many, if not all, biological processes. Small Ubiquitin-like Modifier (SUMO) polypeptides are covalently attached to specific lysine residues of target proteins through a dedicated enzymatic pathway. Disruption of the SUMO enzymatic pathway in the developing brain leads to lethality indicating that this process exerts a central role during embryonic and post-natal development. However, little is still known regarding how this highly dynamic protein modification is regulated in the mammalian brain despite an increasing number of data implicating sumoylated substrates in synapse formation, synaptic communication and plasticity. The aim of this review is therefore to briefly describe the enzymatic SUMO pathway and to give an overview of our current knowledge on the function and dysfunction of protein sumoylation at the mammalian synapse.
近年来，SUMO化已成为一种关键的翻译后修饰，即便不是涉及所有生物过程，也参与了许多生物过程。小泛素样修饰物（SUMO）多肽通过特定的酶促途径共价连接到靶蛋白的特定赖氨酸残基上。发育中的大脑中SUMO酶促途径的破坏会导致致死性，这表明该过程在胚胎期和出生后发育中发挥着核心作用。然而，尽管越来越多的数据表明SUMO化底物参与突触形成、突触通讯和可塑性，但对于这种高度动态的蛋白质修饰在哺乳动物大脑中是如何被调控的，我们仍然知之甚少。因此，本综述的目的是简要描述SUMO酶促途径，并概述我们目前对哺乳动物突触处蛋白质SUMO化的功能和功能障碍的认识。
