Abstract
The dynamic interchange of information within a cell, which subsumes the regulation of protein function, activity and multiprotein complex membership, depends upon the flux of the sets of modifications of proteins present in a specific cell at defined times, and the actions of various modules recruited to the resulting interaction platforms. These modifications interact functionally with each other as agonists or antagonists. This intricate signaling network permits the cell to adapt to signals emanating from its environment, and creates multiple levels of complexity for investigations of any particular protein or set thereof. Here, we present an overview of some of the modules interacting with modified residues present in proteins. We also discuss several implications that this entails for both the control of protein function and the study of physiological processes.
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Acknowledgments
Space constraints render it impossible to acknowledge all of the contributions made to this field by the many key individuals and groups who have studied different aspects of this research area in detail, and have made it necessary to refer the reader to reviews in many cases where the primary literature is very large. This work was supported by a post-doctoral fellowship from the Research Institute of the McGill University Health Centre (to N.B.), as well as by operating grants from the Canadian Cancer Society and the Canadian Institutes of Health Research (to X.-J.Y. and M.P.). M.P. holds the Diane and Sal Guerrera Chair in Cancer Genetics at McGill University.
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Bertos, N.R., Sangwan, V., Yang, XJ., Park, M. (2011). Covalent Protein Modification as a Mechanism for Dynamic Recruitment of Specific Interactors. In: Vidal, C. (eds) Post-Translational Modifications in Health and Disease. Protein Reviews, vol 13. Springer, New York, NY. https://doi.org/10.1007/978-1-4419-6382-6_11
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