title: Reading protein modifications with interaction domains.
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.
authors.affiliation: Samuel Lunenfeld Research Institute, Mount Sinai Hospital, 600 University Avenue, Toronto, Ontario M5G 1X5, Canada.
authors.forename: Bruce T
authors.initials: BT
authors.lastname: Seet
authors.forename: Ivan
authors.initials: I
authors.lastname: Dikic
authors.forename: Ming-Ming
authors.initials: MM
authors.lastname: Zhou
authors.forename: Tony
authors.initials: T
authors.lastname: Pawson
mesh_terms: D020816:Amino Acid Motifs; D002468:Cell Physiological Phenomena; D008958:Models, Molecular; D015394:Molecular Structure; D011485:Protein Binding; D011487:Protein Conformation; D011499:Protein Processing, Post-Translational; D011506:Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*
chemical_list: D011506:Proteins