Diane Gesty-Palmer

TL;DR: The role of arrestin-dependent heptahelical G protein-coupled receptors in the human genome has been investigated in this article. But, the role of the arrestin binding is not yet fully understood.

TL;DR: The C-terminal tail of a GPCR, by determining the stability of the receptor-β-arrestin complex, controls the extent of β-Arrestin-bound ERK activation, and influences both the subcellular localization of activated ERK and the physiologic consequences of ERKactivation.

TL;DR: Surprisingly, phosphorylation-deficient mutants of the receptors are also capable of directing similar conformational changes in β-arrestin as is the wild-type receptor, indicating that distinct receptor conformations induced and/or stabilized by different ligands can promote distinct and functionally specific conformations inβ-argentin even in the absence of receptor phosphorylated.

TL;DR: The results in Gesty-Palmer et al. illustrate that, by activating exclusively the β-arrestin pathway downstream of the PTH receptor, a biased agonist can stimulate a desirable physiological outcome (bone growth) while minimizing an undesirable effect (bone degradation).

TL;DR: It is suggested that recurrent episodes of S. aureus bacteremia are primarily relapses and are associated with an indwelling foreign body, receiving vancomycin therapy, and hemodialysis dependence.