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Proteomic dissection of biological pathways/processes through profiling protein-protein interaction networks

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Abstract

Cellular functions, either under the normal or pathological conditions or under different stresses, are the results of the coordinated action of multiple proteins interacting in macromolecular complexes or assemblies. The precise determination of the specific composition of protein complexes, especially using scalable and high-throughput methods, represents a systematic approach toward revealing particular cellular biological functions. In this regard, the direct profiling protein-protein interactions (PPIs) represent an efficient way to dissect functional pathways for revealing novel protein functions. In this review, we illustrate the technological evolution for the large-scale and precise identification of PPIs toward higher physiologically relevant accuracy. These techniques aim at improving the efficiency of complex pull-down, the signal specificity and accuracy in distinguishing specific PPIs, and the accuracy of identifying physiological relevant PPIs. A newly developed streamline proteomic approach for mapping the binary relationship of PPIs in a protein complex is introduced.

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Authors and Affiliations

  1. Institutes for Biomedical Sciences, Fudan University, Shanghai, 200433, China

    Xian Chen

  2. Department of Biochemistry & Biophysics, School of Medicine, University of North Carolina-Chapel Hill, Chapel Hill, USA

    Xian Chen

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  1. Xian Chen
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Correspondence to Xian Chen.

Additional information

Support from the Shanghai Science and Technology Development Program (Grant Nos. 03DZ14024 & 07ZR14010) and the 863 High Technology Foundation of China (Grant No. 2006AA02A310), US NIH 1R01AI064806-01A2, 5R21DK082706, and U.S. Department of Energy, the Office of Science (BER) (Grant No. DE-FG02-07ER64422).

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Chen, X. Proteomic dissection of biological pathways/processes through profiling protein-protein interaction networks. Sci. China Chem. 53, 737–746 (2010). https://doi.org/10.1007/s11426-010-0136-6

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  • DOI: https://doi.org/10.1007/s11426-010-0136-6

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