Emerging paradigms of β-arrestin-dependent seven transmembrane receptor signaling.
β-Arrestins, originally discovered to desensitize activated seven transmembrane receptors (7TMRs; also known as G-protein-coupled receptors, GPCRs), are now well established mediators of receptor endocytosis, ubiquitylation and G protein-independent signaling. Recent global analyses of β-arrestin interactions and β-arrestin-dependent phosphorylation events have uncovered several previously unanticipated roles of β-arrestins in a range of cellular signaling events. These findings strongly suggest that the functional roles of β-arrestins are much broader than currently understood. Biophysical studies aimed at understanding multiple active conformations of the 7TMRs and the β-arrestins have begun to unravel the mechanistic basis for the diverse functional capabilities of β-arrestins in cellular signaling.
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- beta-Arrestins
- Ubiquitination
- Species Specificity
- Signal Transduction
- Receptors, G-Protein-Coupled
- Protein Transport
- Protein Conformation
- Phosphorylation
- Phosphoproteins
- Membrane Proteins
Citation
Published In
DOI
ISSN
Publication Date
Volume
Issue
Start / End Page
Location
Related Subject Headings
- beta-Arrestins
- Ubiquitination
- Species Specificity
- Signal Transduction
- Receptors, G-Protein-Coupled
- Protein Transport
- Protein Conformation
- Phosphorylation
- Phosphoproteins
- Membrane Proteins