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Expanding SUMO and ubiquitin-mediated signaling through hybrid SUMO-ubiquitin chains and their receptors

机译：通过杂合SUMO-泛素链及其受体扩展SUMO和泛素介导的信号传导

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Monomeric and polymeric forms of SUMO and ubiquitin are covalently attached to substrates and recognized by effector proteins containing SUMO-interacting motifs (SIMs) or ubiquitin-interacting motifs (UIMs), thereby triggering a wide range of biological responses. SUMO and ubiquitin were thought to represent distinct homotypic signals, until recent studies revealed the presence of hybrid SUMO-Ub chains. Synthesis of SUMO-Ub chains is dependent on the activity of SUMO-targeted ubiquitin ligases (STUbLs) that specifically recognize and ubiquitinate SUMO chains on substrates (Fig. 1A). SUMO-Ub chains were originally identified on proteins destined for proteasomal degradation. As exemplified in humans, SUMO-Ub chains synthesized by RNF4 target PML (promyelocytic leukemia protein) for proteasomal degradation. However, it remained unclear whether SUMO-Ub chains are recognized as distinct signals by hybrid chain-specific receptors or by receptors recognizing ubiquitin alone.
机译：SUMO和泛素的单体形式和聚合形式共价附着于底物，并被含有SUMO相互作用基序（SIM）或泛素相互作用基序（UIM）的效应蛋白识别，从而引发广泛的生物学反应。 SUMO和泛素被认为代表不同的同型信号，直到最近的研究表明存在杂化SUMO-Ub链。 SUMO-Ub链的合成取决于以SUMO为靶标的泛素连接酶（STUbLs）的活性，该酶特异性识别和泛化底物上的SUMO链（图1A）。 SUMO-Ub链最初是在用于蛋白酶体降解的蛋白质上鉴定的。如在人类中所举例说明的那样，由RNF4合成的SUMO-Ub链靶向PML（早幼粒细胞白血病蛋白）以进行蛋白酶体降解。然而，尚不清楚SUMO-Ub链是否被杂合链特异性受体或单独识别泛素的受体识别为不同的信号。

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