Department of Vertebrate Genomics, Max Planck Institute for Molecular Genetics, Berlin, Germany.
Cell Div. 2012 Jul 16;7(1):17. doi: 10.1186/1747-1028-7-17.
This review provides a brief overview of the recent work on centrosome proteomics, protein complex identification and functional characterization with an emphasis on the literature of the last three years. Proteomics, genetic screens and comparative genomics studies in different model organisms have almost exhaustively identified the molecular components of the centrosome. However, much knowledge is still missing on the protein-protein interactions, protein modifications and molecular changes the centrosome undergoes throughout the cell cycle and development. The dynamic nature of this large multi-protein complex is reflected in the variety of annotated subcellular locations and biological processes of its proposed components. Some centrosomal proteins and complexes have been studied intensively in different organisms and provided detailed insight into centrosome functions. For example, the molecular, structural and functional characterization of the γ-Tubulin ring complex (γ-TuRC) and the the discovery of the Augmin/HAUS complex has advanced our understanding of microtubule (MT) capture, nucleation and organization. Surprising findings revealed new functions and localizations of proteins that were previously regarded as bona fide centriolar or centrosome components, e.g. at the kinetochore or in the nuclear pore complex regulating MT plus end capture or mRNA processing. Many centrosome components undergo posttranslational modifications such as phosphorylation, SUMOylation and ubiquitylation that are critical in modulating centrosome function and biology. A wealth of information has recently become available driven by new developments in technologies such as mass spectrometry, light and electron microscopy providing more detailed molecular and structural definition of the centrosome and particular roles of proteins throughout the cell cycle and development.
这篇综述简要概述了最近在中心体蛋白质组学、蛋白质复合物鉴定和功能特征方面的工作，重点介绍了过去三年的文献。蛋白质组学、遗传筛选和比较基因组学研究在不同的模式生物中几乎已经详尽地鉴定了中心体的分子组成。然而，关于中心体在细胞周期和发育过程中经历的蛋白质-蛋白质相互作用、蛋白质修饰和分子变化，我们仍然知之甚少。这个大型多蛋白复合物的动态性质反映在其注释的亚细胞位置和生物过程的多样性上，其提议的组成部分。一些中心体蛋白和复合物在不同的生物体中进行了深入研究，为中心体功能提供了详细的见解。例如，γ-微管蛋白环复合物（γ-TuRC）的分子、结构和功能特征以及 Augmin/HAUS 复合物的发现，提高了我们对微管（MT）捕获、成核和组织的理解。令人惊讶的发现揭示了以前被认为是真正的中心粒或中心体成分的蛋白质的新功能和定位，例如在动粒或核孔复合物中，调节 MT 加端捕获或 mRNA 处理。许多中心体成分经历翻译后修饰，如磷酸化、SUMO 化和泛素化，这些修饰在调节中心体功能和生物学方面至关重要。最近，新技术的发展，如质谱、光和电子显微镜，提供了更多关于中心体的分子和结构定义以及蛋白质在整个细胞周期和发育过程中的特定作用的详细信息，这方面的信息也变得非常丰富。
