title: Cyclic AMP-dependent phosphorylation of the actin-binding protein filamin.
abstract: Filamin is a high molecular weight protein that binds to actin filaments in cells. It is found in large amounts in several different cells and tissues, including smooth muscle, fibroblasts, platelets, and macrophages. It is immunologically related to the previously described macrophage high molecular weight actin-binding protein but clearly different from erythrocyte spectrin. Filamin is a phosphoprotein; it is phosphorylated in vivo in intact tissues and cells. It can be phosphorylated in vitro with endogenous kinases; cyclic AMP stimulates this phosohorylation. Furthermore, the purified protein can be phosphorylated by purified cyclic AMP-dependent protein kinase. In smooth muscle homogenates, the stimulation of filamin phosphorylation by cyclic AMP is specific. Cyclic GMP and Ca2+ do not increase its phosphorylation, although they do stimulate phosphorylation of other proteins.
mesh_terms: D000199:Actins / Q000378:metabolism*; D000818:Animals; D002118:Calcium / Q000494:pharmacology; D002352:Carrier Proteins / Q000378:metabolism*; D003285:Contractile Proteins / Q000378:metabolism*; D000242:Cyclic AMP / Q000494:pharmacology / Q000502:physiology*; D006152:Cyclic GMP / Q000494:pharmacology; D006801:Humans; D066298:In Vitro Techniques; D009130:Muscle, Smooth / Q000187:drug effects / Q000378:metabolism; D010750:Phosphoproteins / Q000378:metabolism*
chemical_list: D000199:Actins; D002352:Carrier Proteins; D003285:Contractile Proteins; D010750:Phosphoproteins; D000242:Cyclic AMP; D006152:Cyclic GMP; D002118:Calcium