Phosphorylation of G Protein-Coupled Receptors: From the Barcode Hypothesis to the Flute Model

التفاصيل البيبلوغرافية
العنوان: Phosphorylation of G Protein-Coupled Receptors: From the Barcode Hypothesis to the Flute Model
المؤلفون: Fan Yang, Peng Xiao, Sun Jinpeng, Daolai Zhang, Zhixin Liu, Amy Lin, Xiao Yu, Chuan Liu, Zhao Yang
المصدر: Molecular Pharmacology. 92:201-210
بيانات النشر: American Society for Pharmacology & Experimental Therapeutics (ASPET), 2017.
سنة النشر: 2017
مصطلحات موضوعية: 0301 basic medicine, Pharmacology, Protein Conformation, Kinase, Effector, Biology, Receptors, G-Protein-Coupled, Cell biology, 03 medical and health sciences, beta-Arrestin 1, 030104 developmental biology, Arrestin, Animals, Humans, Molecular Medicine, Phosphorylation, Arrestin beta 2, Arrestin beta 1, Receptor, Signal Transduction, G protein-coupled receptor
الوصف: Seven transmembrane G protein-coupled receptors (GPCRs) are often phosphorylated at the C terminus and on intracellular loops in response to various extracellular stimuli. Phosphorylation of GPCRs by GPCR kinases and certain other kinases can promote the recruitment of arrestin molecules. The arrestins critically regulate GPCR functions not only by mediating receptor desensitization and internalization, but also by redirecting signaling to G protein-independent pathways via interactions with numerous downstream effector molecules. Accumulating evidence over the past decade has given rise to the phospho-barcode hypothesis, which states that ligand-specific phosphorylation patterns of a receptor direct its distinct functional outcomes. Our recent work using unnatural amino acid incorporation and fluorine-19 nuclear magnetic resonance (19F-NMR) spectroscopy led to the flute model, which provides preliminary insight into the receptor phospho-coding mechanism, by which receptor phosphorylation patterns are recognized by an array of phosphate-binding pockets on arrestin and are translated into distinct conformations. These selective conformations are recognized by various effector molecules downstream of arrestin. The phospho-barcoding mechanism enables arrestin to recognize a wide range of phosphorylation patterns of GPCRs, contributing to their diverse functions.
تدمد: 1521-0111
0026-895X
URL الوصول: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::fa57443cd28acd9426d889b3f0539b6e
https://doi.org/10.1124/mol.116.107839
حقوق: OPEN
رقم الأكسشن: edsair.doi.dedup.....fa57443cd28acd9426d889b3f0539b6e
قاعدة البيانات: OpenAIRE