Seven-Transmembrane Receptor Signaling Through β-Arrestin
By Sudha K. Shenoy, R. J. Lefkowitz. Science's STKE, 2005
158 citations recorded by the source corpus.
Subfields: Cellular and Molecular Neuroscience, Molecular Biology
View Paper: https://www.semanticscholar.org/paper/17cc0c558496d2671399a52668cddd7d396f692a
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In Cellular and Molecular Neuroscience
- R. J. Lefkowitz
- Sudha K. Shenoy
- Seungkirl Ahn
- S. Rajagopal
- R. Gainetdinov
- J. Beaulieu
- A. Shukla
- Éric Reiter
In Molecular Biology
- R. J. Lefkowitz
- Sudha K. Shenoy
- Seungkirl Ahn
- S. Rajagopal
- R. Gainetdinov
- A. Shukla
- J. Beaulieu
- Kunhong Xiao
Citations in the corpus
- Distinct Phosphorylation Sites on the β2-Adrenergic Receptor Establish a Barcode That Encodes Differential Functions of β-Arrestin (2011, background): “b-Arrestin binding uncouples the receptor from the G protein, thus terminating or attenuating G protein–mediated signaling (desensitization), and facilitates clathrin-mediated endocytosis (internalization) of the receptor (2).”
- The Physiology, Signaling, and Pharmacology of Dopamine Receptors (2011, background): “…the scaffolding of a wide variety of signaling proteins, such as mitogen-activated protein kinases (MAP kinases), c-Src, Mdm2, N-ethylmaleimide-sensitive factor, Akt, and others (Luttrell and Lefkowitz, 2002; Shenoy and Lefkowitz, 2003, 2005; Beaulieu et al., 2009; Luttrell and Gesty-Palmer, 2010).”
- Stress-Induced p38 Mitogen-Activated Protein Kinase Activation Mediates κ-Opioid-Dependent Dysphoria (2007, background): “The role of G-protein-coupled receptor phosphorylation by GRK in signaling has recently gained attention, because it has been shown that sustained agonist occupation and subsequent phosphorylation of the receptor can alter coupling to the MAPK signaling cassette in vitro (Shenoy and Lefkowitz, 2005;”