An Akt/β-Arrestin 2/PP2A Signaling Complex Mediates Dopaminergic Neurotransmission and Behavior
Jean-Martin Beaulieu,Tatyana D. Sotnikova,Sébastien Marion,Robert J. Lefkowitz,Raul R. Gainetdinov,Marc G. Caron +5 more
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TLDR
It is demonstrated that, apart from its classical function in receptor desensitization, beta-arrestin 2 also acts as a signaling intermediate through a kinase/phosphatase scaffold, thus implicating beta-arsenin 2 as a positive mediator of dopaminergic synaptic transmission and a potential pharmacological target for dopamine-related psychiatric disorders.About:
This article is published in Cell.The article was published on 2005-07-29 and is currently open access. It has received 950 citations till now. The article focuses on the topics: Protein kinase B & Protein phosphatase 2.read more
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The Physiology, Signaling, and Pharmacology of Dopamine Receptors
TL;DR: D dopamine receptor classification, their basic structural and genetic organization, their distribution and functions in the brain and the periphery, and their regulation and signal transduction mechanisms are discussed.
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β-Arrestins and Cell Signaling
TL;DR: The signaling capacities of these versatile adapter molecules are reviewed and the possible implications for cellular processes such as chemotaxis and apoptosis are discussed.
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Neurogenesis-Dependent and -Independent Effects of Fluoxetine in an Animal Model of Anxiety/Depression
Denis J. David,Benjamin Adam Samuels,Quentin Rainer,Jingwen Wang,Douglas Marsteller,Indira Mendez,Michael R. Drew,Douglas A. Craig,Bruno P. Guiard,Jean-Philippe Guilloux,Roman Artymyshyn,Alain M. Gardier,Christophe P. G. Gerald,Irina Antonijevic,E. David Leonardo,René Hen +15 more
TL;DR: A mouse model of an anxiety/depressive-like state induced by chronic corticosterone treatment is described, and mice deficient in one of these genes, beta-arrestin 2, displayed a reduced response to fluoxetine in multiple tasks, suggesting that beta-Arrestin signaling is necessary for the antidepressant effects of fluoxettine.
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Glycogen synthase kinase-3 (GSK3): Regulation, actions, and diseases
TL;DR: Glycogen synthase kinase-3 (GSK3) must be particularly adaptable for incorporating new substrates into its repertoire, and the distinct properties of GSK3 that may contribute to its capacity to fulfill its roles in multiple signaling pathways are discussed.
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Teaching old receptors new tricks: biasing seven-transmembrane receptors
TL;DR: Seven-transmembrane receptors are the largest class of receptors in the human genome and are common targets for therapeutics, and several biased ligands and receptors have been identified that preferentially signal through either G protein- or β-arrestin-mediated pathways.
References
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Journal ArticleDOI
Inhibition of glycogen synthase kinase-3 by insulin mediated by protein kinase B.
TL;DR: It is shown that agents which prevent the activation of both MAPKAP kinase-1 and p70S6k by insulin in vivo do not block the phosphorylation and inhibition of GSK3, and it is demonstrated that PKB is the product of the proto-oncogene protein kinase B (PKB, also known as Akt/RAC).
Journal ArticleDOI
Dopamine Receptors: From Structure to Function
TL;DR: Target deletion of several of these dopamine receptor genes in mice should provide valuable information about their physiological functions and provide unequivocal evidence for the involvement of one of these receptors in the etiology of various central nervous system disorders.
Journal ArticleDOI
Characterization of a 3-phosphoinositide-dependent protein kinase which phosphorylates and activates protein kinase Bα
Dario R. Alessi,Stephen R. James,C. Peter Downes,Andrew B. Holmes,Piers R. J. Gaffney,Colin B. Reese,Philip Cohen +6 more
TL;DR: In this paper, a protein kinase that phosphorylates PKB α at Thr308 and increases its activity over 30-fold was found to play a key role in mediating the activation of PKB by insulin and growth factors.
Mechanism of activation of protein kinase B by insulin and IGF-1. EMBO J 15 (23):6541-6551
TL;DR: It is demonstrated that activation of PKBalpha by insulin or insulin‐like growth factor‐1 (IGF‐1) results from phosphorylation of both Thr308 and Ser473, that phosphorylate of both residues is critical to generate a high level of P KBalpha activity and that the phosphorylated of Thr308 in vivo is not dependent on phosphorylations of Ser473 or vice versa.
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Mechanism of activation of protein kinase B by insulin and IGF-1.
Dario R. Alessi,Mirjana Andjelkovic,Barry Caudwell,Peter Cron,Nick Morrice,Philip Cohen,Brian A. Hemmings +6 more
TL;DR: In this paper, the activation of PKBalpha was accompanied by its phosphorylation at Thr308 and Ser473 and, like activation, likeactivation was prevented by the phosphatidylinositol 3-kinase inhibitor wortmannin.