title: Characterization of p29, an estrogen-receptor associated tumor marker.
abstract: Monoclonal antibody D5, raised against cytosolic human estrogen receptor (ER) reacts with p29, a receptor-associated cytoplasmic serine phosphoprotein which does not bind steroid, While p29 selectively binds GTP and to a lesser extent ATP, in vitro GTP binding does not result in p29 phosphorylation. Under ER activating conditions, p29 associates with cytosolic ER; GTP, ATP and sodium molybdate block formation of immunoprecipitable p29-ER complexes. Nucleotide binding data suggest a role for p29 in the estrogen response machinery, possibly at the level of phosphate or nucleotide metabolism.
authors.affiliation: Department of Hormone Biochemistry, Imperial Cancer Research Fund, London, England.
authors.forename: A I
authors.initials: AI
authors.lastname: Coffer
authors.forename: R J
authors.initials: RJ
authors.lastname: King
mesh_terms: D000255:Adenosine Triphosphate / Q000378:metabolism; D014408:Biomarkers, Tumor / Q000032:analysis*; D001943:Breast Neoplasms / Q000032:analysis; D002460:Cell Line; D005260:Female; D006160:Guanosine Triphosphate / Q000378:metabolism; D006360:Heat-Shock Proteins; D006801:Humans; D009215:Myometrium / Q000032:analysis; D010750:Phosphoproteins / Q000032:analysis*; D010766:Phosphorylation; D011960:Receptors, Estrogen / Q000378:metabolism*
chemical_list: D014408:Biomarkers, Tumor; D006360:Heat-Shock Proteins; D010750:Phosphoproteins; D011960:Receptors, Estrogen; D006160:Guanosine Triphosphate; D000255:Adenosine Triphosphate