The active conformation of beta-arrestin1: direct evidence for the phosphate sensor in the N-domain and conformational differences in the active states of beta-arrestins1 and -2 (Q28570207)

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English	The active conformation of beta-arrestin1: direct evidence for the phosphate sensor in the N-domain and conformational differences in the active states of beta-arrestins1 and -2	scientific journal article

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scholarly article

1 reference

31 January 2017

The active conformation of beta-arrestin1: direct evidence for the phosphate sensor in the N-domain and conformational differences in the active states of beta-arrestins1 and -2 (English)

1 reference

31 January 2017

Robert Lefkowitz

5

object named as

Robert J. Lefkowitz

1 reference

31 January 2017

4

object named as

Terrence G. Oas

1 reference

31 January 2017

author name string

Kelly N. Nobles

1

1 reference

31 January 2017

Ziqiang Guan

2

1 reference

31 January 2017

Kunhong Xiao

3

1 reference

31 January 2017

language of work or name

0 references

publication date

20 July 2007

1 reference

31 January 2017

Journal of Biological Chemistry

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31 January 2017

282

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31 January 2017

29

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31 January 2017

21370–21381

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31 January 2017

Targeted construction of phosphorylation-independent beta-arrestin mutants with constitutive activity in cells.

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Activation-dependent conformational changes in {beta}-arrestin 2.

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The proliferative and antiapoptotic effects of substance P are facilitated by formation of a beta -arrestin-dependent scaffolding complex

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Conformational differences between arrestin2 and pre-activated mutants as revealed by hydrogen exchange mass spectrometry

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Visual arrestin binding to rhodopsin. Diverse functional roles of positively charged residues within the phosphorylation-recognition region of arrestin.

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beta-Arrestin 1 and Galphaq/11 coordinately activate RhoA and stress fiber formation following receptor stimulation

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Beta-arrestin acts as a clathrin adaptor in endocytosis of the beta2-adrenergic receptor

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Mechanism of phosphorylation-recognition by visual arrestin and the transition of arrestin into a high affinity binding state

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The solution structure and activation of visual arrestin studied by small-angle X-ray scattering

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Differential affinities of visual arrestin, beta arrestin1, and beta arrestin2 for G protein-coupled receptors delineate two major classes of receptors

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β-Arrestin1 Mediates Insulin-like Growth Factor 1 (IGF-1) Activation of Phosphatidylinositol 3-Kinase (PI3K) and Anti-apoptosis

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Activation and targeting of extracellular signal-regulated kinases by beta-arrestin scaffolds

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Beta-arrestin 2: a receptor-regulated MAPK scaffold for the activation of JNK3

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Transduction of receptor signals by beta-arrestins

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Arrestin interactions with G protein-coupled receptors. Direct binding studies of wild type and mutant arrestins with rhodopsin, beta 2-adrenergic, and m2 muscarinic cholinergic receptors.

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Kappa opioid receptor activation of p38 MAPK is GRK3- and arrestin-dependent in neurons and astrocytes

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Mapping the arrestin-receptor interface. Structural elements responsible for receptor specificity of arrestin proteins

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Transition of arrestin into the active receptor-binding state requires an extended interdomain hinge

1 reference

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Identification of a motif in the carboxyl terminus of beta -arrestin2 responsible for activation of JNK3

1 reference

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Distinct beta-arrestin- and G protein-dependent pathways for parathyroid hormone receptor-stimulated ERK1/2 activation.

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Independent beta-arrestin 2 and G protein-mediated pathways for angiotensin II activation of extracellular signal-regulated kinases 1 and 2.

1 reference

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Visual arrestin binding to microtubules involves a distinct conformational change

1 reference

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An additional phosphate-binding element in arrestin molecule. Implications for the mechanism of arrestin activation

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The new face of active receptor bound arrestin attracts new partners

1 reference

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Scaffolding functions of arrestin-2 revealed by crystal structure and mutagenesis

1 reference

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Synthetic phosphopeptide from rhodopsin sequence induces retinal arrestin binding to photoactivated unphosphorylated rhodopsin

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Beta-arrestin-dependent formation of beta2 adrenergic receptor-Src protein kinase complexes

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beta-Arrestin scaffolding of the ERK cascade enhances cytosolic ERK activity but inhibits ERK-mediated transcription following angiotensin AT1a receptor stimulation

1 reference

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Arrestin with a single amino acid substitution quenches light-activated rhodopsin in a phosphorylation-independent fashion

1 reference

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Beta-arrestins and cell signaling

1 reference

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X-ray crystal structure of arrestin from bovine rod outer segments

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G-protein-coupled receptor (GPCR) kinase phosphorylation and beta-arrestin recruitment regulate the constitutive signaling activity of the human cytomegalovirus US28 GPCR.

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How does arrestin respond to the phosphorylated state of rhodopsin?

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Crystal structure of cone arrestin at 2.3A: evolution of receptor specificity.

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The 2.8 A crystal structure of visual arrestin: a model for arrestin's regulation

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Reciprocal regulation of angiotensin receptor-activated extracellular signal-regulated kinases by beta-arrestins 1 and 2.

1 reference

11 October 2022

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The interaction with the cytoplasmic loops of rhodopsin plays a crucial role in arrestin activation and binding.

1 reference

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Visual and both non-visual arrestins in their "inactive" conformation bind JNK3 and Mdm2 and relocalize them from the nucleus to the cytoplasm

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The structural basis of arrestin-mediated regulation of G-protein-coupled receptors

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The molecular acrobatics of arrestin activation

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Crystal structure of beta-arrestin at 1.9 A: possible mechanism of receptor binding and membrane Translocation

1 reference

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Conservation of the phosphate-sensitive elements in the arrestin family of proteins.

1 reference

11 October 2022

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Arrestin/clathrin interaction. Localization of the clathrin binding domain of nonvisual arrestins to the carboxy terminus

1 reference

11 October 2022

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Identifiers

10.1074/JBC.M611483200

1 reference

Consolidated OpenCitations Corpus – April 2017

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OpenCitations bibliographic resource ID

1 reference

Consolidated OpenCitations Corpus – April 2017

OpenCitations bibliographic resource ID

1 reference

Consolidated OpenCitations Corpus – April 2017

OpenCitations bibliographic resource ID

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