Reading protein modifications with interaction domains.

Bruce T Seet; Ivan Dikic; Ming-Ming Zhou; Tony Pawson

doi:10.1038/nrm1960

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Reading protein modifications with interaction domains.

Bruce T Seet·Ivan Dikic·Ming-Ming Zhou·Tony Pawson

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Abstract

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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Amino Acid Motifs Cell Physiological Phenomena Models, Molecular Molecular Structure Protein Binding Protein Conformation Protein Processing, Post-Translational Proteins Journal Article Research Support, N.I.H., Extramural Research Support, Non-U.S. Gov't Review

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Bruce T Seet, Ivan Dikic, Ming-Ming Zhou, Tony Pawson. 2006. Reading protein modifications with interaction domains.. https://doi.org/10.1038/nrm1960

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