β-Arrestin Condensate: a New Paradigm for Spatiotemporal Regulation of GPCR Signaling
- 1Division of Life Sciences and Medicine, Hefei National Laboratory for Physical Sciences at the Microscale, University of Science and Technology of China, Hefei 230026, China
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.
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BibTeX
@article{yuanxia2026βarrestin,
title = {{β-Arrestin Condensate: a New Paradigm for Spatiotemporal Regulation of GPCR Signaling}},
author = {WANG Yuan-Xia and SUN De-Meng},
journal = {Shengwu huaxue yu shengwu wuli jinzhan},
year = {2026},
month = oct,
doi = {10.3724/j.pibb.2026.0337},
url = {https://doi.org/10.3724/j.pibb.2026.0337},
note = {CC BY-NC},
}
RIS
TY - JOUR
TI - β-Arrestin Condensate: a New Paradigm for Spatiotemporal Regulation of GPCR Signaling
AU - WANG Yuan-Xia
AU - SUN De-Meng
PY - 2026
DA - 2026/10/26
JO - Shengwu huaxue yu shengwu wuli jinzhan
DO - 10.3724/j.pibb.2026.0337
UR - https://doi.org/10.3724/j.pibb.2026.0337
AB - 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.
SN - 1000-3282
ER -