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Titel:

Phosphorylation of Cav1.2 on S1928 uncouples the L-type Ca2+ channel from the ?2 adrenergic receptor.

Dokumenttyp:
Journal Article; Article
Autor(en):
Patriarchi, Tommaso; Qian, Hai; Di Biase, Valentina; Malik, Zulfiquar A; Chowdhury, Dhrubajyoti; Price, Jennifer L; Hammes, Erik A; Buonarati, Olivia R; Westenbroek, Ruth E; Catterall, William A; Hofmann, Franz; Xiang, Yang K; Murphy, Geoffrey G; Chen, Chao-Ye; Navedo, Manuel F; Hell, Johannes W
Abstract:
Agonist-triggered downregulation of ?-adrenergic receptors (ARs) constitutes vital negative feedback to prevent cellular overexcitation. Here, we report a novel downregulation of ?2AR signaling highly specific for Cav1.2. We find that ?2-AR binding to Cav1.2 residues 1923-1942 is required for ?-adrenergic regulation of Cav1.2. Despite the prominence of PKA-mediated phosphorylation of Cav1.2 S1928 within the newly identified ?2AR binding site, its physiological function has so far escaped identif...     »
Zeitschriftentitel:
EMBO J
Jahr:
2016
Band / Volume:
35
Heft / Issue:
12
Seitenangaben Beitrag:
1330-45
Sprache:
eng
Volltext / DOI:
doi:10.15252/embj.201593409
PubMed:
http://view.ncbi.nlm.nih.gov/pubmed/27103070
Print-ISSN:
0261-4189
TUM Einrichtung:
Institut für Pharmakologie und Toxikologie
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