Transduction of Receptor Signals by ß-Arrestins

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G protein coupled receptor structure and activation. (2007, background): “Moreover, there is a growing appreciation that GPCR regulation and signaling is much more complex than originally envisioned, and includes signalling through G protein independent pathways [2–4].”
Distinct Phosphorylation Sites on the β2-Adrenergic Receptor Establish a Barcode That Encodes Differential Functions of β-Arrestin (2011, background): “E-mail: lefko001@receptor-biol. duke.edu (R.J.L.); khxiao@receptor-biol.duke.edu (K.X.) ww (MAPK), the tyrosine kinase c-Src, and the Ser-Thr kinase Akt (3).”
Crystal Structure of the β2Adrenergic Receptor-Gs protein complex (2011, neutral): “More recently, sequencing of the human genome led to the identification of over expression and silencing of genes have revealed a complex network of cellular signaling and regulatory pathways including G protein-independent activation of cytosolic kinases 10,11 .”
Regulation of Notch signalling by non-visual β-arrestin (2005, background): “The mammalian non-visual arrestins, β-arrestin-1 and β-arrestin-2, have a major role in desensitization and endocytosis of G-protein-coupled receptors (GPCRs”