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Advances in the analysis of dynamic protein complexes by proteomics and data processing

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Abstract

Signal transduction governs virtually every cellular function of multicellular organisms, and its deregulation leads to a variety of diseases. This intricate network of molecular interactions is mediated by proteins that are assembled into complexes within individual signaling pathways, and their composition and function is often regulated by different post-translational modifications. Proteomic approaches are commonly used to analyze biological complexes and networks, but often lack the specificity to address the dynamic and hence transient nature of the interactions and the influence of the multiple post-translational modifications that govern these processes. Here we review recent developments in proteomic research to address these limitations, and discuss several technologies that have been developed for this purpose. The synergy between these proteomic and computational tools, when applied together with global methods to the analysis of individual proteins, complexes and pathways, may allow researchers to unravel the underlying mechanisms of signaling networks in greater detail than previously possible.

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Acknowledgements

This work is funded by grants from the Canadian Institutes for Health Research (CIHR) and NSERC to J.K. P.S. is supported by a CIHR/HSFC postdoctoral fellowship. M.D.H. received a CGS scholarship from NSERC. Due to space limitations we regret that we were not able to acknowledge all contributions in this growing field.

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  1. The Biomedical Research Centre, University of British Columbia, 2222 Health Sciences Mall, Vancouver, BC, V6T 1Z3, Canada

    Peter Schubert, Michael D. Hoffman, Matthew J. Sniatynski & Juergen Kast

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  1. Peter Schubert
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  2. Michael D. Hoffman
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  3. Matthew J. Sniatynski
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  4. Juergen Kast
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Correspondence to Juergen Kast.

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Schubert, P., Hoffman, M.D., Sniatynski, M.J. et al. Advances in the analysis of dynamic protein complexes by proteomics and data processing. Anal Bioanal Chem 386, 482–493 (2006). https://doi.org/10.1007/s00216-006-0609-9

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  • DOI: https://doi.org/10.1007/s00216-006-0609-9

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