Reading protein modifications with interaction domains.

 Seet, B. T., Dikic, I., Zhou, M.-M. & Pawson, T.

 Nature Rev. Mol. Cell Biol. 7, 473-483 (2006).

doi:10.1038/nrm1960

Proteins are controlled by a vast and dynamic array of post-translational modifications, many of which create binding sites for specific protein-interaction domains. We propose that these domains, working together, read the state of the proteome and therefore couple post-translational modifications to cellular organization. We also identify common strategies through which modification-dependent interactions synergize to regulate cell behaviour.

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