Coffer A I, King R J
Department of Hormone Biochemistry, Imperial Cancer Research Fund, London, England.
J Steroid Biochem. 1988 Nov;31(5):745-50. doi: 10.1016/0022-4731(88)90281-6.
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.
针对人胞质雌激素受体（ER）产生的单克隆抗体D5与p29发生反应，p29是一种不结合类固醇的受体相关胞质丝氨酸磷酸蛋白。虽然p29选择性结合GTP且在较小程度上结合ATP，但体外GTP结合不会导致p29磷酸化。在ER激活条件下，p29与胞质ER结合；GTP、ATP和钼酸钠会阻止可免疫沉淀的p29-ER复合物的形成。核苷酸结合数据表明p29在雌激素反应机制中发挥作用，可能在磷酸或核苷酸代谢水平。
