The Activation of Protein Kinase A by the Calcium-Binding Protein S100A1 Is Independent of Cyclic AMP.
Biochemistry
; 56(17): 2328-2337, 2017 05 02.
Article
en En
| MEDLINE
| ID: mdl-28409622
ABSTRACT
Biochemical and structural studies demonstrate that S100A1 is involved in a Ca2+-dependent interaction with the type 2α and type 2ß regulatory subunits of protein kinase A (PKA) (RIIα and RIIß) to activate holo-PKA. The interaction was specific for S100A1 because other calcium-binding proteins (i.e., S100B and calmodulin) had no effect. Likewise, a role for S100A1 in PKA-dependent signaling was established because the PKA-dependent subcellular redistribution of HDAC4 was abolished in cells derived from S100A1 knockout mice. Thus, the Ca2+-dependent interaction between S100A1 and the type 2 regulatory subunits represents a novel mechanism that provides a link between Ca2+ and PKA signaling, which is important for the regulation of gene expression in skeletal muscle via HDAC4 cytosolic-nuclear trafficking.
Texto completo:
1
Colección:
01-internacional
Base de datos:
MEDLINE
Asunto principal:
Proteínas S100
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Fibras Musculares Esqueléticas
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Señalización del Calcio
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Subunidad RIIalfa de la Proteína Quinasa Dependiente de AMP Cíclico
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Subunidad RIIbeta de la Proteína Quinasa Dependiente de AMP Cíclico
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Histona Desacetilasas
Límite:
Animals
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Humans
Idioma:
En
Revista:
Biochemistry
Año:
2017
Tipo del documento:
Article
País de afiliación:
Estados Unidos