Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

PKA-mediated phosphorylation of the beta1-adrenergic receptor promotes Gs/Gi switching.

Cellular signalling - 1 Dec 2004

Martin Negin P, Whalen Erin J, Zamah Musa A, Pierce Kristen L, Lefkowitz Robert J

Abstract excerpt

Recently, it has been shown that PKA-mediated phosphorylation of the beta(2)-adrenergic receptor (beta(2)-AR) by the cyclic AMP-dependent protein kinase (PKA) reduces its affinity for G(s) and increases its affinity for G(i). Here we demonstrate that, like the beta(2)-AR, the beta(1)-AR is also capable of "switching" its coupling from G(s) to G(i) in a PKA-dependent manner. The beta(1)-AR is capable of activating...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Adenylyl Cyclases
Share to CHO Cells
Share to Cyclic AMP

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to Cyclic AMP-Dependent Protein Kinases

Share to GTP-Binding Protein alpha Subunits, Gi-Go

Share to GTP-Binding Protein alpha Subunits, Gs

Share to Receptors, Adrenergic, beta-1

Share to Transcriptional Activation

Source

Identifiers

PMID: 15381255
DOI: 10.1016/j.cellsig.2004.05.002

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

PKA-mediated phosphorylation of the beta1-adrenergic receptor promotes Gs/Gi switching.PMID 15381255Read ↗

beta-arrestin-dependent, G protein-independent ERK1/2 activation by the beta2 adrenergic receptor.Semantic proximity Read ↗

Localization of the sites mediating desensitization of the beta(2)-adrenergic receptor by the GRK pathway.Semantic proximity Read ↗

Gi-biased β2AR signaling links GRK2 upregulation to heart failure.Semantic proximity Read ↗

Key amino acids for differential coupling of alpha1-adrenergic receptor subtypes to Gs.Semantic proximity Read ↗

Targeted transgenesis reveals discrete attenuator functions of GRK and PKA in airway beta2-adrenergic receptor physiologic signaling.Semantic proximity Read ↗

Cardiac β2-Adrenergic Receptor Phosphorylation at Ser355/356 Regulates Receptor Internalization and Functional Resensitization.Semantic proximity Read ↗

Role of the G protein-coupled receptor kinase site serine cluster in beta2-adrenergic receptor internalization, desensitization, and beta-arrestin translocation.Semantic proximity Read ↗

Signaling from β1‐ and β2‐adrenergic receptors is defined by differential interactions with PDE4Semantic proximity Read ↗

Ser/ Thr residues at α3/β5 loop of Gαs are important in morphine-induced adenylyl cyclase sensitization but not mitogen-activated protein kinase phosphorylation.Semantic proximity Read ↗

Inhibition of Galphaq-dependent PLC-beta1 activity by PKG and PKA is mediated by phosphorylation of RGS4 and GRK2.Semantic proximity Read ↗

Beta 2-adrenergic receptor mutants reveal structural requirements for the desensitization observed with long-term epinephrine treatment.Semantic proximity Read ↗

Phosphorylation of GRK2 by PKA augments GRK2-mediated phosphorylation, internalization, and desensitization of VPAC2 receptors in smooth muscle.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.