The role of tropomyosin in the interactions of F-actin with caldesmon and actin-binding protein (or filamin).
The interactions of actin filaments with actin-binding protein (filamin) and caldesmon under the influence of tropomyosin were studied in detail using falling-ball viscometry, binding assay and electron microscopy. Caldesmon decreased the binding constant of filamin with F-actin. In contrast, the maximum binding ability of filamin to F-actin was decreased by tropomyosin. The filamin-induced gelation of actin filaments was inhibited by caldesmon. Tropomyosin also inhibited this gelation. The effect of caldesmon became stronger under the influence of tropomyosin. Furthermore, both caldesmon and tropomyosin additionally decreased the filamin binding to F-actin. From these results, caldesmon and tropomyosin appeared to influence filamin binding to F-actin with different modes of actin. In addition, there was no sign of direct interactions between filamin, caldesmon and tropomyosin as judged from gel filtration. Under the influence of caldesmon and tropomyosin, calmodulin conferred Ca2+ sensitivity on the filamin-induced gelation of actin filaments.
D000199:Actins / Q000378:metabolism*; D000818:Animals; D002118:Calcium / Q000378:metabolism; D002148:Calmodulin-Binding Proteins / Q000378:metabolism*; D002645:Chickens; D003285:Contractile Proteins / Q000378:metabolism*; D064448:Filamins; D008840:Microfilament Proteins / Q000378:metabolism*; D008854:Microscopy, Electron; D014335:Tropomyosin / Q000378:metabolism*; D014783:Viscosity
D000199:Actins; D002148:Calmodulin-Binding Proteins; D003285:Contractile Proteins; D064448:Filamins; D008840:Microfilament Proteins; D014335:Tropomyosin; D002118:Calcium