Recent advances in charting protein-protein interaction: mass spectrometry-based approaches

被引:91
|
作者
Gavin, Anne-Claude [1 ]
Maeda, Kenji [1 ]
Kuehner, Sebastian [1 ]
机构
[1] EMBL, D-69117 Heidelberg, Germany
关键词
CHEMICAL CROSS-LINKING; AFFINITY PURIFICATION; QUANTITATIVE PROTEOMICS; INTERACTION DATABASE; INTERACTION NETWORKS; BAC TRANSGENEOMICS; CELL-CYCLE; YEAST; COMPLEXES; REVEALS;
D O I
10.1016/j.copbio.2010.09.007
中图分类号
Q5 [生物化学];
学科分类号
071010 ; 081704 ;
摘要
Cellular functions are the result of the coordinated action of groups of proteins interacting in molecular assemblies or pathways. The systematic and unbiased charting of protein-protein networks in a variety of organisms has become an important challenge in systems biology. These protein-protein interaction networks contribute comprehensive cartographies of key pathways or biological processes relevant to health or disease by providing a molecular frame for the interpretation of genetic links. At a structural level protein-protein networks enabled the identification of the sequences, motifs and structural folds involved in the process of molecular recognition. A rapidly growing choice of technologies is available for the global charting of protein-protein interactions. In this review, we focus on recent developments in a suite of methods that enable the purification of protein complexes under native conditions and, in conjunction with protein mass spectrometry, identification of their constituents.
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页码:42 / 49
页数:8
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