N-formyl peptide receptor phosphorylation domains differentially regulate arrestin and agonist affinity (Q44211079)

30 November 2017

N-formyl peptide receptor phosphorylation domains differentially regulate arrestin and agonist affinity (English)

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30 November 2017

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30 November 2017

5

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30 November 2017

4

Larry A Sklar

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30 November 2017

T Alexander Key

1

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PubMed ID

12424254

30 November 2017

Terry D Foutz

series ordinal

2

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PubMed ID

12424254

30 November 2017

language of work or name

English

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publication date

6 November 2002

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Journal of Biological Chemistry

30 November 2017

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30 November 2017

278

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30 November 2017

6

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30 November 2017

4041-4047

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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)

30 November 2017

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M204687200

G-protein-coupled receptor regulation: role of G-protein-coupled receptor kinases and arrestins

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M204687200

G protein-coupled receptor kinases

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M204687200

Phosphorylation modulates the affinity of light-activated rhodopsin for G protein and arrestin.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M204687200

Regulation of formyl peptide receptor agonist affinity by reconstitution with arrestins and heterotrimeric G proteins

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M204687200

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M204687200

beta-Arrestin1 modulates lymphoid enhancer factor transcriptional activity through interaction with phosphorylated dishevelled proteins

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M204687200

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M204687200

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M204687200

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M204687200

Classical and new roles of beta-arrestins in the regulation of G-protein-coupled receptors

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M204687200

A central role for beta-arrestins and clathrin-coated vesicle-mediated endocytosis in beta2-adrenergic receptor resensitization. Differential regulation of receptor resensitization in two distinct cell types

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M204687200

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M204687200

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.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M204687200

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M204687200

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M204687200

How does arrestin respond to the phosphorylated state of rhodopsin?

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M204687200

Agonist-receptor-arrestin, an alternative ternary complex with high agonist affinity.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M204687200

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M204687200

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M204687200

Molecular determinants underlying the formation of stable intracellular G protein-coupled receptor-beta-arrestin complexes after receptor endocytosis*

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M204687200

Functional differences in the interaction of arrestin and its splice variant, p44, with rhodopsin

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M204687200

Kinetics, binding constant, and activation energy of the 48-kDa protein-rhodopsin complex by extra-metarhodopsin II.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M204687200

Arrestin binding to the G protein-coupled N-formyl peptide receptor is regulated by the conserved "DRY" sequence

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M204687200

Internalization of the human N-formyl peptide and C5a chemoattractant receptors occurs via clathrin-independent mechanisms

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M204687200

Differential phosphorylation paradigms dictate desensitization and internalization of the N-formyl peptide receptor

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M204687200

Real-time analysis of G protein-coupled receptor reconstitution in a solubilized system.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M204687200

Partial phosphorylation of the N-formyl peptide receptor inhibits G protein association independent of arrestin binding.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M204687200

Real-time analysis of the assembly of ligand, receptor, and G protein by quantitative fluorescence flow cytometry

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M204687200

Desensitization and internalization of the m2 muscarinic acetylcholine receptor are directed by independent mechanisms.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M204687200

Two homologous phosphorylation domains differentially contribute to desensitization and internalization of the m2 muscarinic acetylcholine receptor

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M204687200

Removal of phosphorylation sites from the β2-adrenergic receptor delays onset of agonist-promoted desensitization

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M204687200

The role of receptor kinases and arrestins in G protein-coupled receptor regulation

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M204687200

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M204687200

Arrestin Variants Display Differential Binding Characteristics for the PhosphorylatedN-Formyl Peptide Receptor Carboxyl Terminus

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M204687200

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M204687200

21 January 2018

Identifiers

DOI

10.1074/JBC.M204687200

1 reference

30 November 2017

1 reference

PubMed ID

12424254