title: Molecular mechanisms of SH2- and PTB-domain-containing proteins in receptor tyrosine kinase signaling.
abstract: Intracellular signaling is mediated by reversible posttranslational modifications (PTMs) that include phosphorylation, ubiquitination, and acetylation, among others. In response to extracellular stimuli such as growth factors, receptor tyrosine kinases (RTKs) typically dimerize and initiate signaling through phosphorylation of their cytoplasmic tails and downstream scaffolds. Signaling effectors are recruited to these phosphotyrosine (pTyr) sites primarily through Src homology 2 (SH2) domains and pTyr-binding (PTB) domains. This review describes how these conserved domains specifically recognize pTyr residues and play a major role in mediating precise downstream signaling events.
authors.affiliation: Lunenfeld Tanenbaum Research Institute, Mount Sinai Hospital, Toronto, Ontario M5G 1X5, Canada.
authors.forename: Melany J
authors.initials: MJ
authors.lastname: Wagner
authors.forename: Melissa M
authors.initials: MM
authors.lastname: Stacey
authors.forename: Bernard A
authors.initials: BA
authors.lastname: Liu
authors.forename: Tony
authors.initials: T
authors.lastname: Pawson
mesh_terms: D020816:Amino Acid Motifs; D001665:Binding Sites; D006801:Humans; D008958:Models, Molecular; D010766:Phosphorylation; D019000:Phosphotyrosine / Q000378:metabolism*; D011485:Protein Binding; D020794:Receptor Protein-Tyrosine Kinases / Q000378:metabolism*; D015398:Signal Transduction; D018909:src Homology Domains
chemical_list: D019000:Phosphotyrosine; D020794:Receptor Protein-Tyrosine Kinases