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蛋白质翻译后修饰(PTM)修饰的蛋白质相互作用网络和复合物的生物信息学分析

Bioinformatics Analysis of PTM-Modified Protein Interaction Networks and Complexes.

作者信息

Woodsmith Jonathan, Stelzl Ulrich, Vinayagam Arunachalam

机构信息

Otto-Warburg Laboratory, Max-Planck Institute for Molecular Genetics (MPIMG), Ihnestrasse 63-73, Berlin, Germany.

Department of Pharmaceutical Chemistry, Institute of Pharmaceutical Sciences, University of Graz, Universitätsplatz 1, Graz, Austria.

出版信息

Methods Mol Biol. 2017;1558:321-332. doi: 10.1007/978-1-4939-6783-4_15.

Abstract

Normal cellular functioning is maintained by macromolecular machines that control both core and specialized molecular tasks. These machines are in large part multi-subunit protein complexes that undergo regulation at multiple levels, from expression of requisite components to a vast array of post-translational modifications (PTMs). PTMs such as phosphorylation, ubiquitination, and acetylation currently number more than 200,000 in the human proteome and function within all molecular pathways. Here we provide a framework for systematically studying these PTMs in the context of global protein-protein interaction networks. This analytical framework allows insight into which functions specific PTMs tend to cluster in, and furthermore which complexes either single or multiple PTM signaling pathways converge on.

摘要

正常细胞功能由控制核心和特定分子任务的大分子机器维持。这些机器在很大程度上是多亚基蛋白质复合物,它们在多个水平上受到调控,从必需成分的表达到大量的翻译后修饰(PTM)。诸如磷酸化、泛素化和乙酰化等PTM目前在人类蛋白质组中的数量超过200,000种,并且在所有分子途径中发挥作用。在这里,我们提供了一个框架,用于在全球蛋白质-蛋白质相互作用网络的背景下系统地研究这些PTM。这个分析框架能够深入了解特定PTM倾向于聚集在哪些功能中,以及单个或多个PTM信号通路会汇聚到哪些复合物上。

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