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首页> 外文期刊>Cell cycle >Cytoplasmic sumoylation by PIAS-type Siz1-SUMO ligase.
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Cytoplasmic sumoylation by PIAS-type Siz1-SUMO ligase.

机译：PIAS型Siz1-SUMO连接酶对细胞质的磺酰化作用。

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摘要

SUMO (small ubiquitin-related modifier), a 12 kDa protein with distant similarity to ubiquitin, covalently binds to many proteins in eukaryotic cells. In contrast to ubiquitination, which mainly regulates proteasome-dependent degradation and protein sorting, sumoylation is known to regulate assembly and disassembly of protein complexes, protein localization and stability, and so on. SUMO is primarily localized to the nucleus, and many SUMO substrates are nuclear proteins involved in DNA transaction. However, certain roles of SUMO conjugates have been shown outside the nucleus. Particularly in budding yeast, SUMO is also localized to the bud-neck in a cell cycle-dependent manner. The first and prominent SUMO substrates are septins, evolutionally conserved proteins required for cytokinesis in yeast. Recent analysis of human septin structure would greatly facilitate the study of the functions of these SUMO conjugates. SUMO modification of septins is regulated by cell cycle-dependent nuclear transport of PIAS-type Siz1 (SUMO E3) and Ulp1 desumoylation enzyme in yeast. Domains outside the SUMO-ligase core (SP-RING) of Siz1 ensure its regulations. Furthermore, newly discovered ubiquitin ligases that specifically recognize poly-SUMO conjugates could lead to degradation of SUMO conjugates. Thus, protein modifications seem to be regulated in an unexpectedly complex manner. In this review, we focus on various regulations in yeast septin sumoylation and discuss its possible functions.
机译：SUMO（小的泛素相关修饰物）是一种与泛素具有遥远相似性的12 kDa蛋白，可与真核细胞中的许多蛋白共价结合。与主要调节蛋白酶体依赖性降解和蛋白质分选的泛素化相反，已知磺酰化作用可调节蛋白质复合物的组装和拆卸，蛋白质定位和稳定性等。 SUMO主要位于细胞核，许多SUMO底物是涉及DNA交易的核蛋白。但是，SUMO偶联物的某些作用已在细胞核外显示。特别是在发芽酵母中，SUMO也以细胞周期依赖性方式定位于芽颈。 SUMO的第一个和最主要的底物是Septins，是酵母胞质分裂所需的进化保守蛋白。对人类septin结构的最新分析将极大地促进这些SUMO缀合物功能的研究。隔膜蛋白的SUMO修饰受酵母中PIAS型Siz1（SUMO E3）和Ulp1脱硫酶的细胞周期依赖性核转运的调节。 Siz1的SUMO-连接酶核心（SP-RING）以外的域确保其法规。此外，新发现的泛素连接酶可以特异性识别聚SUMO共轭物，从而导致SUMO共轭物的降解。因此，似乎以意想不到的复杂方式调节蛋白质修饰。在这篇综述中，我们着重介绍酵母Septin sumoylation中的各种法规，并讨论其可能的功能。

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