Phosphorylation of Ryanodine Receptors

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...

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Autores principales:	DANILA,CRISTINA I, HAMILTON,SUSAN L
Lenguaje:	English
Publicado:	Sociedad de Biología de Chile 2004
Materias:	ryanodine receptor phosphorylation site protein kinase Ser-2809/Ser-2843 FK506-binding protein
Acceso en línea:	http://www.scielo.cl/scielo.php?script=sci_arttext&pid=S0716-97602004000400005
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spelling	oai:scielo:S0716-976020040004000052005-06-02Phosphorylation of Ryanodine ReceptorsDANILA,CRISTINA IHAMILTON,SUSAN L ryanodine receptor phosphorylation site protein kinase Ser-2809/Ser-2843 FK506-binding protein 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.info:eu-repo/semantics/openAccessSociedad de Biología de ChileBiological Research v.37 n.4 20042004-01-01text/htmlhttp://www.scielo.cl/scielo.php?script=sci_arttext&pid=S0716-97602004000400005en10.4067/S0716-97602004000400005
institution	Scielo Chile
collection	Scielo Chile
language	English
topic	ryanodine receptor phosphorylation site protein kinase Ser-2809/Ser-2843 FK506-binding protein
spellingShingle	ryanodine receptor phosphorylation site protein kinase Ser-2809/Ser-2843 FK506-binding protein DANILA,CRISTINA I HAMILTON,SUSAN L Phosphorylation of Ryanodine Receptors
description	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.
author	DANILA,CRISTINA I HAMILTON,SUSAN L
author_facet	DANILA,CRISTINA I HAMILTON,SUSAN L
author_sort	DANILA,CRISTINA I
title	Phosphorylation of Ryanodine Receptors
title_short	Phosphorylation of Ryanodine Receptors
title_full	Phosphorylation of Ryanodine Receptors
title_fullStr	Phosphorylation of Ryanodine Receptors
title_full_unstemmed	Phosphorylation of Ryanodine Receptors
title_sort	phosphorylation of ryanodine receptors
publisher	Sociedad de Biología de Chile
publishDate	2004
url	http://www.scielo.cl/scielo.php?script=sci_arttext&pid=S0716-97602004000400005
work_keys_str_mv	AT danilacristinai phosphorylationofryanodinereceptors AT hamiltonsusanl phosphorylationofryanodinereceptors
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Phosphorylation of Ryanodine Receptors

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