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Titolo:
Targeting of an a kinase-anchoring protein, AKAP79, to an inwardly rectifying potassium channel, Kir2.1
Autore:
Dart, C; Leyland, ML;
Indirizzi:
Univ Leicester, Dept Cell Physiol & Pharmacol, Leicester LE1 9HN, Leics, England Univ Leicester Leicester Leics England LE1 9HN er LE1 9HN, Leics, England Univ Leicester, Dept Biochem, Leicester LE1 9HN, Leics, England Univ Leicester Leicester Leics England LE1 9HN er LE1 9HN, Leics, England
Titolo Testata:
JOURNAL OF BIOLOGICAL CHEMISTRY
fascicolo: 23, volume: 276, anno: 2001,
pagine: 20499 - 20505
SICI:
0021-9258(20010608)276:23<20499:TOAAKP>2.0.ZU;2-B
Fonte:
ISI
Lingua:
ENG
Soggetto:
RECTIFIER K+ CHANNELS; PHOSPHORYLATION; EXPRESSION; RECEPTORS; COMPLEX; RII; CYTOSKELETON; CONDUCTANCE; ASSOCIATION; INHIBITION;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
38
Recensione:
Indirizzi per estratti:
Indirizzo: Dart, C Univ Leicester, Dept Cell Physiol & Pharmacol, POB 138, Leicester LE1 9HN,Leics, England Univ Leicester POB 138 Leicester Leics England LE1 9HN cs, England
Citazione:
C. Dart e M.L. Leyland, "Targeting of an a kinase-anchoring protein, AKAP79, to an inwardly rectifying potassium channel, Kir2.1", J BIOL CHEM, 276(23), 2001, pp. 20499-20505

Abstract

Protein kinase A (PKA) is targeted to discrete subcellular locations closeto its intended substrates through interaction with A kinase-anchoring proteins (AKAPs), Ion channels represent a diverse and important group of kinase substrates, and it has been shown that membrane targeting of PKA throughassociation with AKAPs facilitates PKA-mediated phosphorylation and regulation of several classes of ion channel. Here, we investigate the effect of AKAP79, a membrane associated multivalent-anchoring protein, upon the function and modulation of the strong inwardly rectifying potassium channel, Kir2.1. Functionally, the presence of AKAP79 enhanced the response of Kir2.1 to elevated intracellular cAMP, suggesting a requirement for a pool of PKA anchored close to the channel. Antibodies directed against a hemagglutinin epitope tag on Kir2.1 coimmunoprecipitated AKAP79, indicating that the two proteins exist together in a complex within intact cells. In support of this, glutathione S-transferase fusion proteins of both the intracellular N andC domains of Kir2.1 isolated AKAP79 from cell lysates, while glutathione S-transferase alone failed to interact with AKAP79. Together, these findingssuggest that AKAP79 associates directly with the Kir2.1 ion channel and may serve to anchor kinase enzymes in close proximity to key channel phosphorylation sites.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 30/11/20 alle ore 16:17:25