Localization and identification of actin structures involved in the filamin – actin interaction
Catherine Méjean, Marie‐Christine Lebart, Mireille Boyer, Claude Roustan, Yves Benyamin
Abstract
Catherine Méjean, Marie‐Christine Lebart, Mireille Boyer, Claude Roustan, Yves Benyamin
Abstract
The interface between gizzard filamin and skeletal muscle actin was located on the actin monomer. Conserved sequences 105-120 and 360-372, in the actin subdomain 1 near the myosin binding sites, were involved in this interaction. The corresponding peptides for these sequences were each found to bind filamin and compete in the actin-filamin interaction. When these two peptides were used together in the presence of filamin and filamentous actin, they dissociated sedimentable complexes formed by these two proteins.
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The interface between gizzard filamin and skeletal muscle actin was located on the actin monomer. Conserved sequences 105-120 and 360-372, in the actin subdomain 1 near the myosin binding sites, were involved in this interaction. The corresponding peptides for these sequences were each found to bind filamin and compete in the actin-filamin interaction. When these two peptides were used together in the presence of filamin and filamentous actin, they dissociated sedimentable complexes formed by these two proteins.
Key concepts: Filamin, Actin, FLNA, Myosin, Actina, Cell biology, Actin-binding protein, Chemistry