title: Caldesmon-induced polymerization of actin from profilactin.
abstract: We have investigated the effect of caldesmon, a Ca2+/calmodulin-regulated actin-binding protein, on the complex between profilin and G-actin (profilactin). We found that smooth muscle caldesmon dissociates this complex rapidly and induces the polymerization of the released actin. Native profilactin (e.g. the complex isolated from calf thymus) proved more resistant to the attack of caldesmon than a heterologous complex reconstituted from calf thymus profilin and skeletal muscle actin. The mode of caldesmon-induced profilactin dissociation was similar to that described for Mg2+, and 2 mM MgCl2 potentiated the caldesmon effect. Since both caldesmon and profilin have been found enriched in ruffling membranes of animal cells, our in vitro findings may be relevant to the regulation of actin filaments in living cells.
authors.affiliation: Department of Muscle Biochemistry, Nencki Institute of Experimental Biology, Warsaw, Poland.
authors.forename: B
authors.initials: B
authors.lastname: Gałazkiewicz
authors.forename: F
authors.initials: F
authors.lastname: Buss
authors.forename: B M
authors.initials: BM
authors.lastname: Jockusch
authors.forename: R
authors.initials: R
authors.lastname: Dabrowska
mesh_terms: D000199:Actins / Q000737:chemistry / Q000378:metabolism*; D000818:Animals; D002148:Calmodulin-Binding Proteins / Q000494:pharmacology*; D002462:Cell Membrane / Q000737:chemistry / Q000187:drug effects; D002645:Chickens; D066298:In Vitro Techniques; D007700:Kinetics; D015636:Magnesium Chloride / Q000494:pharmacology; D009132:Muscles / Q000737:chemistry / Q000187:drug effects / Q000378:metabolism*; D051304:Profilins; D011506:Proteins / Q000737:chemistry / Q000378:metabolism*; D014783:Viscosity
chemical_list: D000199:Actins; D002148:Calmodulin-Binding Proteins; D051304:Profilins; D011506:Proteins; C024782:profilactin; D015636:Magnesium Chloride