Dynamic regulation of cAMP synthesis through anchored PKA-adenylyl cyclase V/VI complexes.
Mol Cell
; 23(6): 925-31, 2006 Sep 15.
Article
em En
| MEDLINE
| ID: mdl-16973443
ABSTRACT
Spatiotemporal organization of cAMP signaling begins with the tight control of second messenger synthesis. In response to agonist stimulation of G protein-coupled receptors, membrane-associated adenylyl cyclases (ACs) generate cAMP that diffuses throughout the cell. The availability of cAMP activates various intracellular effectors, including protein kinase A (PKA). Specificity in PKA action is achieved by the localization of the enzyme near its substrates through association with A-kinase anchoring proteins (AKAPs). Here, we provide evidence for interactions between AKAP79/150 and ACV and ACVI. PKA anchoring facilitates the preferential phosphorylation of AC to inhibit cAMP synthesis. Real-time cellular imaging experiments show that PKA anchoring with the cAMP synthesis machinery ensures rapid termination of cAMP signaling upon activation of the kinase. This protein configuration permits the formation of a negative feedback loop that temporally regulates cAMP production.
Texto completo:
1
Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Adenilil Ciclases
/
Proteínas Quinases Dependentes de AMP Cíclico
/
AMP Cíclico
/
Isoenzimas
Limite:
Humans
Idioma:
En
Ano de publicação:
2006
Tipo de documento:
Article