title: The human phosphatase interactome: An intricate family portrait.
abstract: The concerted activities of kinases and phosphatases modulate the phosphorylation levels of proteins, lipids and carbohydrates in eukaryotic cells. Despite considerable effort, we are still missing a holistic picture representing, at a proteome level, the functional relationships between kinases, phosphatases and their substrates. Here we focus on phosphatases and we review and integrate the available information that helps to place the members of the protein phosphatase superfamilies into the human protein interaction network. In addition we show how protein interaction domains and motifs, either covalently linked to the phosphatase domain or in regulatory/adaptor subunits, play a prominent role in substrate selection.
authors.affiliation: Department of Biology, University of Rome Tor Vergata, Rome, Italy.
authors.forename: Francesca
authors.initials: F
authors.lastname: Sacco
authors.forename: Livia
authors.initials: L
authors.lastname: Perfetto
authors.forename: Luisa
authors.initials: L
authors.lastname: Castagnoli
authors.forename: Gianni
authors.initials: G
authors.lastname: Cesareni
mesh_terms: D020816:Amino Acid Motifs; D001665:Binding Sites; D020134:Catalytic Domain; D006801:Humans; D010455:Peptides / Q000737:chemistry; D010744:Phosphoric Monoester Hydrolases / Q000737:chemistry* / Q000502:physiology; D010766:Phosphorylation; D010802:Phylogeny; D011485:Protein Binding; D025941:Protein Interaction Mapping / Q000379:methods*; D017434:Protein Structure, Tertiary; D013379:Substrate Specificity; D014443:Tyrosine / Q000737:chemistry
chemical_list: D010455:Peptides; D014443:Tyrosine; D010744:Phosphoric Monoester Hydrolases