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GoPubMed Proteins lists recent and important papers and reviews for proteins. Page last changed on 19 Aug 2016.

Arrestin, beta 1

beta-arrestin, beta-arrestin 1, arrestin-2, a beta-arrestin
Members of arrestin/beta-arrestin protein family are thought to participate in agonist-mediated desensitization of G-protein-coupled receptors and cause specific dampening of cellular responses to stimuli such as hormones, neurotransmitters, or sensory signals. Arrestin beta 1 is a cytosolic protein and acts as a cofactor in the beta-adrenergic receptor kinase (BARK) mediated desensitization of beta-adrenergic receptors. Besides the central nervous system, it is expressed at high levels in peripheral blood leukocytes, and thus the BARK/beta-arrestin system is believed to play a major role in regulating receptor-mediated immune functions. Alternatively spliced transcripts encoding different isoforms of arrestin beta 1 have been described. [provided by RefSeq, Jan 2011] (from NCBI)
Top mentioned proteins: IRBP, CAN, V1a, GPCR, beta-arrestin 2
Papers on beta-arrestin
Long Receptor Residence Time of C26 Contributes to Super Agonist Activity at the Human β2 Adrenoceptor.
Charlton et al., Nottingham, United Kingdom. In Mol Pharmacol, Feb 2016
We have further characterised the novel β2 adrenoceptor agonist C26 (7-[(R)-2-((1R,2R)-2-benzyloxycyclopentylamino)-1-hydroxyethyl]-4-hydroxybenzothiazolone), which displays higher intrinsic activity than the endogenous ligand adrenaline in cAMP accumulation, β-arrestin-2 recruitment and receptor internalization assays.
Topical Docosahexaenoic Acid (DHA) Accelerates Skin Wound Healing in Rats and Activates GPR120.
Araújo et al., Campinas, Brazil. In Biol Res Nurs, Feb 2016
Upon DHA topical treatment, wound healing was significantly accelerated and was accompanied by the molecular activation of GPR120, as determined by its association with β-arrestin-2.
Stalk-dependent and stalk-independent signaling by the adhesion G protein-coupled receptors GPR56 (ADGRG1) and BAI1 (ADGRB1).
Hall et al., United States. In J Biol Chem, Jan 2016
For G1, however, the results were mixed, with the SL mutant exhibiting robust activity in several signaling assays (including TGFα shedding, activation of NFAT luciferase and beta-arrestin recruitment) but reduced activity relative to ΔNT in a distinct assay (activation of SRF luciferase).
KISS1R signaling promotes invadopodia formation in human breast cancer cell via β-arrestin2/ERK.
Bhattacharya et al., London, Canada. In Cell Signal, Jan 2016
However, we have previously shown that in breast cancer cells lacking the estrogen receptor (ERα), kisspeptin-10 stimulates cell migration and invasion by cross-talking with the epidermal growth factor receptor (EGFR), via a β-arrestin-2-dependent mechanism.
Regulation of N-Formyl Peptide Receptor Signaling and Trafficking by Arrestin-Src Kinase Interaction.
Prossnitz et al., Albuquerque, United States. In Plos One, Dec 2015
To better understand the role of Src kinase in this process, in the current study we employed a previously described arrestin-2 (arr2) mutant deficient in Src kinase binding (arr2-P91G/P121E).
Treatment of acromegaly in the era of personalized and predictive medicine.
Puig Domingo, Badalona, Spain. In Clin Endocrinol (oxf), Jul 2015
This review will discuss the development of a potential treatment algorithm for acromegaly addressing the biochemical control of the disease as well of its associated comorbidities, under a personalized approach based upon markers of prognostic and predictive significance, such as tumour size, MRI adenoma signal, GH value after acute octreotide test, granular adenoma pattern, Ki-67, somatostatin receptor phenotype, aryl hydrocarbon-interacting protein expression, gsp mutations, RAF kinase activity, E-cadherin and beta-arrestin-1.
Activated protein C: biased for translation.
Mosnier et al., Los Angeles, United States. In Blood, Jun 2015
For these beneficial effects, APC alters cell signaling networks and gene expression profiles by activating protease-activated receptors 1 and 3. APC's activation of these G protein-coupled receptors differs completely from thrombin's activation mechanism due to biased signaling via either G proteins or β-arrestin-2.
Molecular Physiology of Enteric Opioid Receptors.
Akbarali et al., Lansing, United States. In Am J Gastroenterol, 2014
This may be due to differential β-arrestin-2-dependent opioid receptor desensitization and internalization in enteric nerves in the colon compared with the small intestine and in neuronal pain pathways.
Omega-3 Fatty Acids and FFAR4.
Walenta et al., San Diego, United States. In Front Endocrinol (lausanne), 2013
This makes FFAR4 to be capable of interacting with β-arrestin-2, which in turn, results in association of β-arrestin-2 with TAB1.
β-arrestins and G protein-coupled receptor trafficking.
Benovic et al., Philadelphia, United States. In Handb Exp Pharmacol, 2013
Nonvisual arrestins (β-arrestin-1 and β-arrestin-2) are adaptor proteins that function to regulate G protein-coupled receptor (GPCR) signaling and trafficking.
Omega-3 fatty acids prevent inflammation and metabolic disorder through inhibition of NLRP3 inflammasome activation.
Zhou et al., Hefei, China. In Immunity, 2013
In addition, G protein-coupled receptor 120 (GPR120) and GPR40 and their downstream scaffold protein β-arrestin-2 were shown to be involved in inflammasome inhibition induced by ω-3 FAs.
Structure of active β-arrestin-1 bound to a G-protein-coupled receptor phosphopeptide.
Lefkowitz et al., Durham, United States. In Nature, 2013
Here we report the crystal structure of β-arrestin-1 (also called arrestin-2) in complex with a fully phosphorylated 29-amino-acid carboxy-terminal peptide derived from the human V2 vasopressin receptor (V2Rpp).
Fluorescence correlation spectroscopy, combined with bimolecular fluorescence complementation, reveals the effects of β-arrestin complexes and endocytic targeting on the membrane mobility of neuropeptide Y receptors.
Holliday et al., Nottingham, United Kingdom. In Biochim Biophys Acta, 2012
The influence of beta-arrestin adaptors and endocytosis mechanisms on plasma membrane diffusion and particle brightness of GFP-tagged neuropeptide Y (NPY) receptors, was investigated.
β-arrestin-1 participates in thrombosis and regulates integrin aIIbβ3 signalling without affecting P2Y receptors desensitisation and function.
Mangin et al., Strasbourg, France. In Thromb Haemost, 2012
beta-arr1 has a role in promoting thrombus formation, in part through its participation in alphaIIbbeta3 signalling, but neither beta-arr1 or beta-arr2 have a role in agonist-induced platelet activation and P2Y receptors desensitisation
Identification of a nuclear localization sequence in β-arrestin-1 and its functional implications.
Ye et al., Chicago, United States. In J Biol Chem, 2012
Lys(157) within the putative nuclear localization sequence is critical to nuclear localization of beta-arrestin-1.
ßarrestin1-biased agonism at human δ-opioid receptor by peptidic and alkaloid ligands.
Allouche et al., Caen, France. In Cell Signal, 2012
Beta arrestin1 is differentially involved during receptor desensitization and endocytosis depending on the ligand.
Activated protein C promotes protease-activated receptor-1 cytoprotective signaling through β-arrestin and dishevelled-2 scaffolds.
Trejo et al., San Diego, United States. In Proc Natl Acad Sci U S A, 2012
These findings identify a role for beta-arrestin and Dvl-2 scaffolds in APC-activated PAR1 cytoprotective signaling in human endothelial cells.
Teaching old receptors new tricks: biasing seven-transmembrane receptors.
Lefkowitz et al., Durham, United States. In Nat Rev Drug Discov, 2010
Originally identified as mediators of 7TMR desensitization, beta-arrestins (arrestin 2 and arrestin 3) are now recognized as true adaptor proteins that transduce signals to multiple effector pathways.
Beta-arrestin1 regulates zebrafish hematopoiesis through binding to YY1 and relieving polycomb group repression.
Pei et al., Shanghai, China. In Cell, 2009
Beta-arrestin1 is a multifunctional protein critically involved in signal transduction.
Insulin action under arrestin.
James et al., Australia. In Cell Metab, 2009
In mouse models, beta-arrestin-2 controls whole-body insulin action by regulating assembly of a complex containing insulin receptor, c-Src, and Akt.
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