These findings provide a model in which Nedd4 and beta-arrestin act together as a complex to regulate mGlu7 surface expression and function at presynaptic terminals.
The nuclear accumulation of beta-arrestin 1 following TLR2 activation promote H4 acetylation at specific target gene promoters and may thus affect transcription of target genes in BM CD34+ cells.
The beta-arrestin pathway-selective type 1A angiotensin receptor (AT1A) agonist [Sar1 Ile4 Ile8]angiotensin II regulates a robust G protein-independent signaling network.
Endogenous beta-arrestin1 functions exclusively in the phosphorylation-dependent receptor internalization whereas endogenous beta-arrestin2 but not beta-arrestin1 is required for the phosphorylation-independent receptor internalization.
both beta-arrestin1 recruitment and the presence of Ser/Thr residues in the distal half of the C-terminal domain were necessary for maximal agonist-induced internalization
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