Bundling of actin filaments by myosin light chain kinase from smooth muscle.
Biochem Biophys Res Commun
; 199(2): 786-91, 1994 Mar 15.
Article
en En
| MEDLINE
| ID: mdl-8135824
Myosin light chain kinase has an inhibitory effect on the interaction of actin filaments with phosphorylated smooth muscle myosin. Myosin light chain kinase binds to actin filaments, and the inhibition is attributable to the actin-binding activity and not the kinase activity of myosin light chain kinase [Kohama et al. (1992) Biochem. Biophys. Res. Commun. 184, 1204-1211]. We now report that myosin light chain kinase is able to assemble actin filaments into thick bundles, which can be visualized by optical and electron microscopy and can be monitored by measuring the sedimentation and flow birefringence of actin filaments. The bundling activity of myosin light chain kinase is abolished by calmodulin in the presence of Ca2+. The possibility is discussed that myosin light chain kinase has multiple actin-binding sites through which it can cross-link actin filaments.
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Colección:
01-internacional
Base de datos:
MEDLINE
Asunto principal:
Quinasa de Cadena Ligera de Miosina
/
Actinas
/
Músculo Liso
/
Músculos
Límite:
Animals
Idioma:
En
Revista:
Biochem Biophys Res Commun
Año:
1994
Tipo del documento:
Article
País de afiliación:
Japón
Pais de publicación:
Estados Unidos