X‐Arrestin: a new retinal arrestin mapping to the X chromosome

Murakami, Akira; Yajima, Toshihiro; Sakuma, Hitoshi; McLaren, M.; Inana, George

doi:10.1016/0014-5793(93)81712-9

Cited by 99 publications

(56 citation statements)

References 51 publications

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“…Our initial attempt to localize X-arrestin within the retina by in situ hybridization gave equivocal results [5]. Despite repeated attempts using a carefully chosen aSS-labeled riboprobe specific for X-arrestin, silver grains were heavily distributed over inner segments of both rods and cones in sections of human retina following liquid emulsion autoradiography.…”

Section: Discussionmentioning

confidence: 99%

Immunolocalization of X‐arrestin in human cone photoreceptors

et al. 1996

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X.arrestia is a recently identified retina-specific gene of unknown function. Affinity-purified anti-peptide antibody to human X-arrestin was prepared, and used in Western blot analysis of human retinal proteins and for immunohistoichemistry on human retinal sections. By Western blot analysis, the antibody specifically bound to an -47 kDa protein, and by indirect immunofluoresicenice specifiically labeled cone photoreceptors with greatest intensity in their outer segments. In single and double label experiments, the loicalization of X-arrestin immunoreaictivity was compared with immunolabeling patterns obtained with antibodies to red/green cone opsin, rhodopsin, and S.antigen. The results showed that X-arrestin is expressed in red-, green, and blue-sensitive cones in the human retina.

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Section: Discussionmentioning

confidence: 99%

Immunolocalization of X‐arrestin in human cone photoreceptors

et al. 1996

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“…β-Arrestin-1 and β-arrestin-2 (also called arrestin3) were subsequently identified and found to prevent activation of the β # -AR preferentially over rhodopsin [100,101]. Cone arrestin is similar in location and substrate specificity to arrestin [102,103]. There are several splice variants of the arrestins which sometimes show tissue-specific expression.…”

Section: Arrestin Familiesmentioning

confidence: 99%

Regulatory mechanisms that modulate signalling by G-protein-coupled receptors

Böhm

Grady

Bunnett

1997

Biochemical Journal

476

322

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The large and functionally diverse group of G-protein-coupled receptors includes receptors for many different signalling molecules, including peptide and non-peptide hormones and neurotransmitters, chemokines, prostanoids and proteinases. Their principal function is to transmit information about the extracellular environment to the interior of the cell by interacting with the heterotrimeric G-proteins, and they thereby participate in many aspects of regulation. Cellular responses to agonists of these receptors are usually rapidly attenuated. Mechanisms of signal attenuation include removal of agonists from the extracellular fluid, receptor desensitization, endocytosis and downregulation. Agonists are removed by dilution, uptake by transporters and enzymic degradation. Receptor desensitization is mediated by receptor phosphorylation by G-protein receptor kinases and second-messenger kinases, interaction of phosphorylated receptors with arrestins and receptor uncoupling from

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“…␤-Arrestin 1 (␤-arr1) and ␤-arrestin 2 (12) are widely expressed in many tissues, especially in the central nervous system, and both play important roles in the desensitization of several G s -and G i -coupled receptors (12,14,16,21). Conespecific arrestin, termed X-arrestin (22) or C-arrestin (23), a fourth member of the arrestin family, was cloned recently. Overexpression of ␤-arr1 and ␤-arrestin 2 attenuates cellular signaling events mediated by many GPCRs such as ␤ 2 -adenergic receptor (15), M 2 muscarinic receptors (24), and ␣ 1B -adrenergic receptor (25).…”

mentioning

confidence: 99%

Selective Interference of β-Arrestin 1 with κ and δ but Not μ Opioid Receptor/G Protein Coupling

Cheng

et al. 1998

Journal of Biological Chemistry

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The role of ␤-arrestin 1 (␤-arr1) in regulation of responsiveness of , ␦, and opioid receptors has been investigated in human embryonic kidney 293 cells cotransfected with opioid receptor and ␤-arr1. Expression of human ␤-arr1 attenuated and ␦ opioid receptor subtype-mediated inhibition of cAMP production and resulted in a 100-fold increase of EC 50 values for -agonist Opiates are effective analgesics. However, chronic use of opiates results in tolerance and dependence, which limit clinical application of opioid drugs. Opiates exert their effects in the central and peripheral nervous systems through interaction with , ␦, and , three major types of opioid receptors, which are structurally homologues and belong to the G protein-coupled receptor (GPCR) 1 family. It has been demonstrated clearly in opioid receptor gene knock-out experiments that analgesia, tolerance, and dependence induced by morphine are all mediated by the opioid receptor (1). However, the molecular mechanisms of opiate tolerance and dependence are not well understood. Desensitization of opioid receptors, the reduced responsiveness of opioid receptors upon agonist stimulation, has been implicated as one of the underlying mechanisms (2). Accumulating evidence indicates that desensitization of opioid receptors involves receptor phosphorylation. Protein kinase C (3-7) and GPCR kinases (GRKs) (8 -10) are shown to be involved in desensitization of , ␦, and opioid receptors. Agonist-stimulated phosphorylation of , ␦, and opioid receptors has been demonstrated recently (7-11). Receptor desensitization is accepted as one of ubiquitous regulatory mechanisms of GPCRs (12). Homologous desensitization of GPCRs are well characterized using the ␤ 2 -adrenergic receptor as a model, and GRKs and arrestins are involved (13). GRKs catalyze phosphorylation of agonist-occupied GPCRs, and their functional cofactor arrestins bind to the phosphorylated receptor subsequently, leading to quenching of G protein activation and reduction of GPCR-mediated responsiveness (12-18).Four members of the arrestin family have been cloned and characterized to date (12,14,19). Visual arrestin is predominantly localized in retina where it regulates phototransduction (20). ␤-Arrestin 1 (␤-arr1) and ␤-arrestin 2 (12) are widely expressed in many tissues, especially in the central nervous system, and both play important roles in the desensitization of several G s -and G i -coupled receptors (12,14,16,21). Conespecific arrestin, termed X-arrestin (22) or C-arrestin (23), a fourth member of the arrestin family, was cloned recently. Overexpression of ␤-arr1 and ␤-arrestin 2 attenuates cellular signaling events mediated by many GPCRs such as ␤ 2 -adenergic receptor (15), M 2 muscarinic receptors (24), and ␣ 1B -adrenergic receptor (25).Data suggesting the involvement of GRKs in phosphorylation and desensitization of opioid receptors have emerged recently. Overexpression of a dominant-negative mutant of ␤-adrenergic receptor kinase 1 (GRK2) blocks desensitization of opioid receptor (KOR) in COS...

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X‐Arrestin: a new retinal arrestin mapping to the X chromosome

Cited by 99 publications

References 51 publications

Immunolocalization of X‐arrestin in human cone photoreceptors

Immunolocalization of X‐arrestin in human cone photoreceptors

Regulatory mechanisms that modulate signalling by G-protein-coupled receptors

Selective Interference of β-Arrestin 1 with κ and δ but Not μ Opioid Receptor/G Protein Coupling

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