Expanding roles for beta-arrestins as scaffolds and adapters in GPCR signaling and trafficking. (Q34180619)

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scientific article

Language	Label	Description	Also known as
English	Expanding roles for beta-arrestins as scaffolds and adapters in GPCR signaling and trafficking.	scientific article

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Europe PubMed Central

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5 November 2019

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Europe PubMed Central

Expanding roles for beta-arrestins as scaffolds and adapters in GPCR signaling and trafficking (English)

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https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:11248546%20AND%20SRC:MED&resulttype=core&format=json

5 November 2019

G protein-coupled receptor

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William E Miller

1

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5 November 2019

Robert Lefkowitz

2

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R J Lefkowitz

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5 November 2019

publication date

1 April 2001

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5 November 2019

Current Opinion in Cell Biology

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5 November 2019

13

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5 November 2019

2

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5 November 2019

139-145

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5 November 2019

G protein-coupled receptors. III. New roles for receptor kinases and beta-arrestins in receptor signaling and desensitization

1 reference

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The pathways connecting G protein-coupled receptors to the nucleus through divergent mitogen-activated protein kinase cascades

1 reference

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Endocytosis and recycling of G protein-coupled receptors

1 reference

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A beta-arrestin/green fluorescent protein biosensor for detecting G protein-coupled receptor activation

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7 January 2021

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G protein-coupled receptor kinases

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Phosphodiesterase activation by photoexcited rhodopsin is quenched when rhodopsin is phosphorylated and binds the intrinsic 48-kDa protein of rod outer segments

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Primary and secondary structure of bovine retinal S antigen (48-kDa protein).

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Functional desensitization of the isolated beta-adrenergic receptor by the beta-adrenergic receptor kinase: potential role of an analog of the retinal protein arrestin (48-kDa protein)

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beta-Arrestin: a protein that regulates beta-adrenergic receptor function

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beta-Arrestin1 knockout mice appear normal but demonstrate altered cardiac responses to beta-adrenergic stimulation

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Enhanced morphine analgesia in mice lacking beta-arrestin 2

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Mu-opioid receptor desensitization by beta-arrestin-2 determines morphine tolerance but not dependence

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Role of beta-arrestin in mediating agonist-promoted G protein-coupled receptor internalization

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

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7 January 2021

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Arrestin/clathrin interaction. Localization of the arrestin binding locus to the clathrin terminal domain

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Modulation of the arrestin-clathrin interaction in cells. Characterization of beta-arrestin dominant-negative mutants

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7 January 2021

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

1 reference

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7 January 2021

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Role of arrestins in G-protein-coupled receptor endocytosis.

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7 January 2021

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Clathrin-mediated endocytosis of the beta-adrenergic receptor is regulated by phosphorylation/dephosphorylation of beta-arrestin1

1 reference

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7 January 2021

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The beta2-adrenergic receptor/betaarrestin complex recruits the clathrin adaptor AP-2 during endocytosis

1 reference

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7 January 2021

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The interaction of beta-arrestin with the AP-2 adaptor is required for the clustering of beta 2-adrenergic receptor into clathrin-coated pits

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7 January 2021

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Identification of NSF as a beta-arrestin1-binding protein. Implications for beta2-adrenergic receptor regulation

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Signal transduction by the JNK group of MAP kinases

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Cardiac overexpression of a G(q) inhibitor blocks induction of extracellular signal-regulated kinase and c-Jun NH(2)-terminal kinase activity in in vivo pressure overload

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

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7 January 2021

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Signal transduction: hanging on a scaffold.

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7 January 2021

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Structural organization of MAP-kinase signaling modules by scaffold proteins in yeast and mammals

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Scaffold proteins may biphasically affect the levels of mitogen-activated protein kinase signaling and reduce its threshold properties

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Ste5 tethers multiple protein kinases in the MAP kinase cascade required for mating in S. cerevisiae

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JSAP1, a novel jun N-terminal protein kinase (JNK)-binding protein that functions as a Scaffold factor in the JNK signaling pathway

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The JIP group of mitogen-activated protein kinase scaffold proteins

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A cytoplasmic inhibitor of the JNK signal transduction pathway

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A mammalian scaffold complex that selectively mediates MAP kinase activation

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MP1: a MEK binding partner that enhances enzymatic activation of the MAP kinase cascade

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Role of c-Src tyrosine kinase in G protein-coupled receptor- and Gbetagamma subunit-mediated activation of mitogen-activated protein kinases

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

1 reference

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beta-arrestin1 interacts with the catalytic domain of the tyrosine kinase c-SRC. Role of beta-arrestin1-dependent targeting of c-SRC in receptor endocytosis

1 reference

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Src-mediated tyrosine phosphorylation of dynamin is required for beta2-adrenergic receptor internalization and mitogen-activated protein kinase signaling

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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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Regulation of tyrosine kinase activation and granule release through beta-arrestin by CXCRI

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beta-arrestin-dependent endocytosis of proteinase-activated receptor 2 is required for intracellular targeting of activated ERK1/2

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beta-arrestins regulate mitogenic signaling and clathrin-mediated endocytosis of the insulin-like growth factor I receptor

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

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

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Identifiers

10.1016/S0955-0674(00)00190-3

1 reference

Europe PubMed Central

PubMed publication ID

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:11248546%20AND%20SRC:MED&resulttype=core&format=json

5 November 2019

PubMed publication ID

1 reference

Europe PubMed Central

PubMed publication ID

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:11248546%20AND%20SRC:MED&resulttype=core&format=json

5 November 2019

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