PKCβII inhibits the ubiquitination of β-arrestin2 in an autophosphorylation-dependent manner. (Q54235583)

26 May 2018

title

PKCβII inhibits the ubiquitination of β-arrestin2 in an autophosphorylation-dependent manner. (English)

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26 May 2018

main subject

protein ubiquitination

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Mei Zheng

1

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26 May 2018

Xiaohan Zhang

2

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26 May 2018

Shuohan Guo

3

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26 May 2018

Xiaowei Zhang

4

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26 May 2018

Hyun Jin Choi

5

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26 May 2018

Moo-Yeol Lee

6

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26 May 2018

Kyeong-Man Kim

7

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26 May 2018

language of work or name

English

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publication date

3 November 2015

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26 May 2018

number of pages

9

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based on heuristic

inferred from page(s)

published in

FEBS Letters

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26 May 2018

volume

589

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26 May 2018

issue

24 Pt B

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26 May 2018

page(s)

3929-3937

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26 May 2018

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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Desensitization of the isolated beta 2-adrenergic receptor by beta-adrenergic receptor kinase, cAMP-dependent protein kinase, and protein kinase C occurs via distinct molecular mechanisms

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Protein kinase C switches the Raf kinase inhibitor from Raf-1 to GRK-2

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Cross-regulation of VPAC(2) receptor desensitization by M(3) receptors via PKC-mediated phosphorylation of RKIP and inhibition of GRK2.

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Functional desensitization of the extracellular calcium-sensing receptor is regulated via distinct mechanisms: role of G protein-coupled receptor kinases, protein kinase C and beta-arrestins

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Heterologous activation of protein kinase C stimulates phosphorylation of delta-opioid receptor at serine 344, resulting in beta-arrestin- and clathrin-mediated receptor internalization

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Crucial roles for protein kinase C isoforms in tumor-specific killing by apoptin

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β-Arrestin2 Plays Permissive Roles in the Inhibitory Activities of RGS9-2 on G Protein-Coupled Receptors by Maintaining RGS9-2 in the Open Conformation

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Identifiers

DOI

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26 May 2018

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26 May 2018