Ca(2+)-dependent phosphorylation of the tail domain of myosin-V, a calmodulin-binding myosin in vertebrate brain
Braz. j. med. biol. res
;
26(5): 465-72, May 1993. ilus
Artigo
em Inglês
| LILACS
| ID: lil-148700
ABSTRACT
1. Myosin-V from vertebrate brain is a novel molecular motor with a myosin-like head domain, a calmodulin-binding neck region and a unique tail domain of unknown function. Previous studies showed brain myosin-V to be a phosphoprotein substrate for Ca2+/calmodulin-dependent protein kinase associated with actomyosin. In the present study we describe the preparation of a specific actin-cytoskeletal fraction which is enriched in brain myosin-V. 2. We show that Ca2+/calmodulin-dependent protein kinase activity is also associated with this preparation and phosphorylates brain myosin-V. 3. Calpain, a Ca(2+)-dependent protease, generates a M(r) 80,000 fragment from the COOH terminal region of brain myosin-V containing most or all of the phosphorylation sites. 4. These results suggest that the unique tail domain of this novel myosin is subject to Ca2+ control via phosphorylation by kinase activity associated with the actin cytoskeleton
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Índice:
LILACS (Américas)
Assunto principal:
Quinase de Cadeia Leve de Miosina
/
Calmodulina
/
Cérebro
Limite:
Animais
Idioma:
Inglês
Revista:
Braz. j. med. biol. res
Assunto da revista:
Biologia
/
Medicina
Ano de publicação:
1993
Tipo de documento:
Artigo
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