Phosphorylation of ryanodine receptors
Biol. Res
; 37(4): 521-525, 2004.
Artigo
em Inglês
| LILACS
| ID: lil-437505
Biblioteca responsável:
CL1.1
ABSTRACT
Both cardiac and skeletal muscle ryanodine receptors (RyRs) are parts of large complexes that include a number of kinases and phosphatases. These RyRs have several potential phosphorylation sites in their cytoplasmic domains, but the functional consequences of phosphorylation and the identity of the enzymes responsible have been subjects of considerable controversy. Hyperphosphorylation of Ser-2809 in RyR2 (cardiac isoform) and Ser-2843 in RyR1 (skeletal isoform) has been suggested to cause the dissociation of the FK506-binding protein (FKBP) from RyRs, producing "leaky channels," but some laboratories find no relationship between phosphorylation and FKBP binding. Also debated is the identity of the kinases that phosphorylate these serines cAMP-dependent protein kinase (PKA) versus calmodulin kinase II (CaMKII). Phosphorylation of other targets of these kinases could also alter calcium homeostasis. For example, PKA also phosphorylates phospholamban (PLB), altering the Sarco-endoplasmic reticulum Ca2+ ATPase (SERCA) activity. This review summarizes the major findings and controversies associated with phosphorylation of RyRs.
Texto completo:
Disponível
Coleções:
Bases de dados internacionais
Base de dados:
LILACS
Assunto principal:
Fosfotransferases
/
Cálcio
/
Proteínas Quinases Dependentes de AMP Cíclico
/
Proteínas Quinases Dependentes de Cálcio-Calmodulina
/
Músculo Esquelético
/
Canal de Liberação de Cálcio do Receptor de Rianodina
Tipo de estudo:
Estudo prognóstico
Limite:
Animais
/
Humanos
Idioma:
Inglês
Revista:
Biol. Res
Assunto da revista:
Biologia
Ano de publicação:
2004
Tipo de documento:
Artigo
País de afiliação:
Estados Unidos
Instituição/País de afiliação:
Baylor College of Medicine/US