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首页> 外文期刊>Molecular & cellular proteomics: MCP >Gold for ubiquitin in Vancouver: First Conference on Proteomics of Protein Degradation and Ubiquitin Pathways held June 6-8, 2010 in Vancouver, University of British Columbia, organized By Lan Huang, Thibault Mayor, and Peipei Ping.
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Gold for ubiquitin in Vancouver: First Conference on Proteomics of Protein Degradation and Ubiquitin Pathways held June 6-8, 2010 in Vancouver, University of British Columbia, organized By Lan Huang, Thibault Mayor, and Peipei Ping.

机译:泛素在温哥华的金牌:蛋白质降解和泛素通路蛋白质组学第一次会议于2010年6月6日至8日在不列颠哥伦比亚大学温哥华举行,由黄煌,Thibault市长和Peipei Ping组织。

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摘要

The rise of proteomics has had tremendous influence on analysis and understanding of the role of post-translational modifications in biological processes. The covalent attachment of small proteins like ubiquitin, SUMO,(1) or other ubiquitin-like proteins (Ubls) is one class of post-translational modifications where proteomics has had notable impact. Various proteomics approaches, but in particular mass spectrometry-based analyses, have influenced the field and enabled significant advances over the past few years. The first meeting dedicated to proteomics of protein degradation and ubiquitin pathways showcased these advances and allowed a glimpse at future contributions of proteomics to this field. With its many attractive drug targets, the ubiquitin and proteasome system, as well as other proteolysis pathways, could offer new therapies for various human diseases including cancer and neurodegenerative disorders. The covalent linkage of ubiquitin to other proteins is catalyzed by the E1-E2-E3 cascade of enzymatic reactions whereby the many different E3 ubiquitin ligases provide substrate specificity to the process of protein ubiquitylation (1). Ubiquitylation is best known for targeting proteins for degradation by the proteasome, but other functions for ubiquitylation independent of proteolysis are also known. Likewise, modifications with SUMO or other Ubls generally do not regulate protein degradation but instead control subcellular localization, protein interactions, or change protein conformation and activity (2). The questions addressed by proteomics approaches to ubiquitylation and Ubl modifications are plentiful. They range from very specific, e.g. determination of the modified residue in a substrate protein, to complex, such as protein dynamics in proteome-wide ubiquitin (or Ubl) modification profiles (3). In either case, the rapid technological advancements (particularly in mass spectrometry instrumentation as well as quantitation and separation technologies) have allowed impressive progress, which was evident in the First Conference on Proteomics of Protein Degradation and Ubiquitin Pathways in Vancouver (http://ppdup.org/) (Fig. 1).
机译:蛋白质组学的兴起对分析和理解翻译后修饰在生物过程中的作用产生了巨大影响。小蛋白如泛素,SUMO(1)或其他泛素样蛋白(Ubls)的共价结合是蛋白质组学产生显着影响的一类翻译后修饰。各种蛋白质组学方法,特别是基于质谱的分析,已经影响了该领域,并在过去几年中取得了重大进展。第一次蛋白质降解和泛素途径的蛋白质组学会议展示了这些进展,并让人们瞥见了蛋白质组学在该领域的未来贡献。泛素和蛋白酶体系统以及许多蛋白水解途径具有许多吸引人的药物靶标,可以为包括癌症和神经退行性疾病在内的各种人类疾病提供新的疗法。泛素与其他蛋白质的共价键被酶促反应的E1-E2-E3级联催化,从而许多不同的E3泛素连接酶为蛋白质泛素化过程提供了底物特异性(1)。泛素化是最著名的靶向蛋白质被蛋白酶体降解的方法,但是与蛋白水解无关的泛素化的其他功能也是众所周知的。同样,用SUMO或其他Ubls修饰通常不调节蛋白质降解,而是控制亚细胞定位,蛋白质相互作用或改变蛋白质构象和活性(2)。蛋白质组学方法在泛素化和Ubl修饰中所解决的问题很多。它们的范围非常具体,例如确定底物蛋白质中修饰残基的复杂程度,例如蛋白质组范围内泛素(或Ubl)修饰谱中的蛋白质动力学(3)。无论哪种情况,快速的技术进步(特别是在质谱仪器以及定量和分离技术方面)都取得了令人瞩目的进展,这在温哥华举行的第一届蛋白质组学与蛋白质降解和泛素途径大会上很明显(http:// ppdup .org /)(图1)。

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