Dictyostelium myosin heavy chain phosphorylation sites regulate myosin filament assembly and localization in vivo.
Cell
; 75(2): 363-71, 1993 Oct 22.
Article
en En
| MEDLINE
| ID: mdl-7691416
Three threonine residues in the tail region of Dictyostelium myosin II heavy chain have been implicated previously in control of myosin filament formation. Here we report the in vitro and in vivo consequences of converting these sites to alanine residues, which eliminates phosphorylation at these positions, or to aspartate residues, which mimics the negative charge state of the phosphorylated molecule. Alanine substitution allows in vitro assembly and in vivo contractile activity, although this myosin shows substantial over-assembly in vivo. Aspartate substitution eliminates filament assembly in vitro and renders the myosin unable to drive any tested contractile event in vivo. These results demonstrate that heavy chain phosphorylation plays a key modulatory role in controlling myosin function in vivo.
Buscar en Google
Colección:
01-internacional
Base de datos:
MEDLINE
Asunto principal:
Citoesqueleto de Actina
/
Compartimento Celular
/
Secuencias Reguladoras de Ácidos Nucleicos
/
Miosinas
/
Dictyostelium
Límite:
Animals
Idioma:
En
Revista:
Cell
Año:
1993
Tipo del documento:
Article
Pais de publicación:
Estados Unidos