Search Results - "Vishnivetskiy, Sergey A"
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Structural basis of arrestin-3 activation and signaling
Published in Nature communications (10-11-2017)“…A unique aspect of arrestin-3 is its ability to support both receptor-dependent and receptor-independent signaling. Here, we show that inositol…”
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Structural Basis of Arrestin Selectivity for Active Phosphorylated G Protein-Coupled Receptors
Published in International journal of molecular sciences (19-11-2021)“…Arrestins are a small family of proteins that bind G protein-coupled receptors (GPCRs). Arrestin binds to active phosphorylated GPCRs with higher affinity than…”
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Identification of Receptor Binding-induced Conformational Changes in Non-visual Arrestins
Published in The Journal of biological chemistry (25-07-2014)“…The non-visual arrestins, arrestin-2 and arrestin-3, belong to a small family of multifunctional cytosolic proteins. Non-visual arrestins interact with…”
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Involvement of distinct arrestin-1 elements in binding to different functional forms of rhodopsin
Published in Proceedings of the National Academy of Sciences - PNAS (15-01-2013)“…Solution NMR spectroscopy of labeled arrestin-1 was used to explore its interactions with dark-state phosphorylated rhodopsin (P-Rh), phosphorylated opsin…”
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G Protein-coupled Receptor Kinases of the GRK4 Protein Subfamily Phosphorylate Inactive G Protein-coupled Receptors (GPCRs)
Published in The Journal of biological chemistry (24-04-2015)“…G protein-coupled receptor (GPCR) kinases (GRKs) play a key role in homologous desensitization of GPCRs. It is widely assumed that most GRKs selectively…”
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An Eight Amino Acid Segment Controls Oligomerization and Preferred Conformation of the two Non-visual Arrestins
Published in Journal of molecular biology (19-02-2021)“…[Display omitted] •In the presence of IP6 arrestin-2 and arrestin-3 form different oligomers.•IP6 activates arrestin-3, but does not activate arrestin-2.•An…”
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Monomeric Rhodopsin Is Sufficient for Normal Rhodopsin Kinase (GRK1) Phosphorylation and Arrestin-1 Binding
Published in The Journal of biological chemistry (14-01-2011)“…G-protein-coupled receptor (GPCR) oligomerization has been observed in a wide variety of experimental contexts, but the functional significance of this…”
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Functional Role of Arrestin-1 Residues Interacting with Unphosphorylated Rhodopsin Elements
Published in International journal of molecular sciences (17-05-2023)“…Arrestin-1, or visual arrestin, exhibits an exquisite selectivity for light-activated phosphorylated rhodopsin (P-Rh*) over its other functional forms. That…”
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The Role of Arrestin-1 Middle Loop in Rhodopsin Binding
Published in International journal of molecular sciences (11-11-2022)“…Arrestins preferentially bind active phosphorylated G protein-coupled receptors (GPCRs). The middle loop, highly conserved in all arrestin subtypes, is…”
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Manipulation of Very Few Receptor Discriminator Residues Greatly Enhances Receptor Specificity of Non-visual Arrestins
Published in The Journal of biological chemistry (24-08-2012)“…Based on the identification of residues that determine receptor selectivity of arrestins and the analysis of the evolution in the arrestin family, we…”
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Biological Role of Arrestin-1 Oligomerization
Published in The Journal of neuroscience (14-10-2020)“…Members of the arrestin superfamily have great propensity of self-association, but the physiological significance of this phenomenon is unclear. To determine…”
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Conformation of receptor-bound visual arrestin
Published in Proceedings of the National Academy of Sciences - PNAS (06-11-2012)“…Arrestin-1 (visual arrestin) binds to light-activated phosphorylated rhodopsin (P-Rh*) to terminate G-protein signaling. To map conformational changes upon…”
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Metabolic effects of skeletal muscle-specific deletion of beta-arrestin-1 and -2 in mice
Published in PLoS genetics (17-10-2019)“…Type 2 diabetes (T2D) has become a major health problem worldwide. Skeletal muscle (SKM) is the key tissue for whole-body glucose disposal and utilization. New…”
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Arrestin-3 binds the MAP kinase JNK3α2 via multiple sites on both domains
Published in Cellular signalling (01-04-2014)“…Although arrestins bind dozens of non-receptor partners, the interaction sites for most signaling proteins remain unknown. Here we report the identification of…”
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G Protein-Coupled Receptor Kinase 2 (GRK2) and 5 (GRK5) Exhibit Selective Phosphorylation of the Neurotensin Receptor in Vitro
Published in Biochemistry (Easton) (21-07-2015)“…G protein-coupled receptor kinases (GRKs) play an important role in the desensitization of G protein-mediated signaling of G protein-coupled receptors (GPCRs)…”
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The functional cycle of visual arrestins in photoreceptor cells
Published in Progress in retinal and eye research (01-11-2011)“…Visual arrestin-1 plays a key role in the rapid and reproducible shutoff of rhodopsin signaling. Its highly selective binding to light-activated phosphorylated…”
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Role of Receptor-attached Phosphates in Binding of Visual and Non-visual Arrestins to G Protein-coupled Receptors
Published in The Journal of biological chemistry (16-03-2012)“…Arrestins are a small family of proteins that regulate G protein-coupled receptors (GPCRs). Arrestins specifically bind to phosphorylated active receptors,…”
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Differential manipulation of arrestin-3 binding to basal and agonist-activated G protein-coupled receptors
Published in Cellular signalling (01-08-2017)“…Non-visual arrestins interact with hundreds of different G protein-coupled receptors (GPCRs). Here we show that by introducing mutations into elements that…”
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Regulation of Arrestin Binding by Rhodopsin Phosphorylation Level
Published in The Journal of biological chemistry (02-11-2007)“…Arrestins ensure the timely termination of receptor signaling. The role of rhodopsin phosphorylation in visual arrestin binding was established more than 20…”
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Enhanced Mutant Compensates for Defects in Rhodopsin Phosphorylation in the Presence of Endogenous Arrestin-1
Published in Frontiers in molecular neuroscience (18-06-2018)“…We determined the effects of different expression levels of arrestin-1-3A mutant with enhanced binding to light-activated rhodopsin that is independent of…”
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