Discrete GPCR-triggered endocytic modes enable β-arrestins to flexibly regulate cell signaling.

ABSTRACT: β-Arrestins are master regulators of cellular signaling that operate by desensitizing ligand-activated G-protein-coupled receptors (GPCRs) at the plasma membrane and promoting their subsequent endocytosis. The endocytic activity of β-arrestins is ligand dependent, triggered by GPCR binding, and increasingly recognized to have a multitude of downstream signaling and trafficking consequences that are specifically programmed by the bound GPCR. However, only one biochemical 'mode' for GPCR-mediated triggering of the endocytic activity is presently known - displacement of the β-arrestin C-terminus (CT) to expose clathrin-coated pit-binding determinants that are masked in the inactive state. Here, we revise this view by uncovering a second mode of GPCR-triggered endocytic activity that is indepe

SUBMITTER: Barsi-Rhyne B 

PROVIDER: S-EPMC9681205 | biostudies-literature | 2022 Oct

REPOSITORIES: biostudies-literature