title: SRC substrate surprise.
abstract: In this issue of Cancer Cell, Lowy and colleagues show that the SH2 domain of tensin-3 is regulated by phosphorylation by Src and that this phosphorylation promotes the oncogenic function of tensin-3. Phosphorylation of the SH2 domain represents a novel mechanism for the regulation of SH2 ligand binding.
authors.affiliation: Department of Molecular and Cell Biology and Cancer Research Laboratory, University of California, Berkeley, Berkeley, CA 94720, USA. gsm@berkeley.edu
authors.forename: G Steven
authors.initials: GS
authors.lastname: Martin
mesh_terms: D000818:Animals; D001665:Binding Sites / Q000235:genetics; D008024:Ligands; D051379:Mice; D008822:Mice, Transgenic; D008954:Models, Biological; D010749:Phosphoprotein Phosphatases / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D010766:Phosphorylation; D011485:Protein Binding / Q000235:genetics; D017434:Protein Structure, Tertiary / Q000235:genetics; D011993:Recombinant Fusion Proteins / Q000737:chemistry / Q000378:metabolism; D013379:Substrate Specificity / Q000235:genetics; D000070876:Tensins; D014443:Tyrosine / Q000378:metabolism; D018909:src Homology Domains / Q000235:genetics*
chemical_list: D008024:Ligands; D011993:Recombinant Fusion Proteins; D000070876:Tensins; D014443:Tyrosine; D010749:Phosphoprotein Phosphatases; C500779:Tns3 protein, mouse