NDLI: Divergent ß-arrestin-dependent signaling events are dependent upon sequences within G-protein-coupled receptor C termini.

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Divergent ß-arrestin-dependent signaling events are dependent upon sequences within G-protein-coupled receptor C termini.

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Divergent ß-arrestin-dependent signaling events are dependent upon sequences within G-protein-coupled receptor C termini.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Kumar, Puneet Pal, Kasturi Mathur, Maneesh Defea, Kathryn
Description	Author Affiliation: Pal K ( Cell Molecular Developmental Biology Program, University of California, Riverside, California 92521, USA.)
Abstract	ß-Arrestins are multifunctional adaptor proteins that, upon recruitment to an activated G-protein-coupled receptor, can promote desensitization of G-protein signaling and receptor internalization while simultaneously eliciting an independent signal. The result of ß-arrestin signaling depends upon the activating receptor. For example, activation of two G (q)-coupled receptors, protease-activated receptor-2 (PAR(2)) and neurokinin-1 receptor (NK1R), results in drastically different signaling events. PAR(2) promotes ß-arrestin-dependent membrane-sequestered extracellular signal-regulated kinase (ERK1/2) activation, cofilin activation, and cell migration, whereas NK1R promotes nuclear ERK1/2 activation and proliferation. Using bioluminescence resonance energy transfer to monitor receptor/ß-arrestin interactions in real time, we observe that PAR(2) has a higher apparent affinity for both ß-arrestins than does NK1R, recruits them at a faster rate, and exhibits more rapid desensitization of the G-protein signal. Furthermore, recruitment of ß-arrestins to PAR(2) does not require prior G (q) signaling events, whereas inhibition of G (q) signaling intermediates inhibits recruitment of ß-arrestins to NK1R. Using chimeric receptors in which the C terminus of PAR(2) is fused to the N terminus of NK1R and vice versa and a critical Ser/Thr mutant of PAR(2), we demonstrate that interactions between ß-arrestins and specific phosphoresidues in the C termini of each receptor are crucial for determining the rate and magnitude of ß-arrestin recruitment as well as the ultimate signaling outcome.
ISSN	00219258
e-ISSN	1083351X
Journal	Journal of Biological Chemistry
Issue Number	5
Volume Number	288
Language	English
Publisher	American Society for Biochemistry and Molecular Biology (United States)
Publisher Date	2013-02-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Arrestins Metabolism Receptor, PAR-2 Chemistry Receptors, Neurokinin-1 Signal Transduction Actin Depolymerizing Factors Amino Acid Sequence Animals CHO Cells Calcium Cell Movement Cricetinae Endocytosis Enzyme Activation Extracellular Signal-Regulated MAP Kinases GTP-Binding Protein Alpha Subunits, Gq-G11 HEK293 Cells Intracellular Space Kinetics Mice Mutant Proteins Neurokinin-1 Receptor Antagonists Phosphorylation Antagonists & Inhibitors Structure-Activity Relationship Subcellular Fractions Research Support, N.I.H., Extramural Biochemistry Molecular Biology
Content Type	Text
Resource Type	Article
Subject	Cell Biology Biochemistry Molecular Biology

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