β-Arrestin Condensate: a New Paradigm for Spatiotemporal Regulation of GPCR Signaling
- VernacularTitle:β-制动蛋白聚集体调控G蛋白偶联受体信号的新机制
- Author:
Yuan-Xia WANG
1
;
De-Meng SUN
1
Author Information
- Publication Type:Journal Article
- Keywords: β-arrestin; liquid-liquid phase separation; biomolecular condensates; GPCR signaling
- From: Progress in Biochemistry and Biophysics 2026;53(10):2841-2845
- CountryChina
- Language:Chinese
- Abstract: β‑arrestin serves as a core functional effector governing signal transduction of G protein-coupled receptors (GPCRs), exerting dual roles as a signal terminator and molecular scaffold. However, the molecular mechanism underlying how β-arrestin responds to diverse GPCRs and interacts with hundreds of effector proteins to mediate a broad spectrum of physiological functions remains poorly understood. A landmark original study recently published in Nature overturned the conventional view of β‑arrestin as a static scaffold protein. Endogenously expressed β‑arrestin undergoes liquid-liquid phase separation (LLPS) to form highly dynamic biomolecular condensates, which orchestrate compartmentalized assembly and fine-tuning of GPCR signaling complexes. This work establishes a novel paradigm centered on β‑arrestin condensates for GPCR signal regulation and reshapes the molecular framework of hierarchically organized intracellular signaling networks.
