Inducible degradation of IkappaBalpha by the proteasome requires interaction with the F-box protein h-betaTrCP. (Q50335887)

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12 November 2019

title

Inducible degradation of IkappaBalpha by the proteasome requires interaction with the F-box protein h-betaTrCP (English)

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Florence Margottin-Goguet

12 November 2019

author

2

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12 November 2019

Jean-Paul Concordet

6

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12 November 2019

Françoise Bachelerie

7

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author name string

M Kroll

1

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12 November 2019

A Kohl

3

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12 November 2019

P Renard

4

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12 November 2019

H Durand

5

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12 November 2019

F Arenzana-Seisdedos

8

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R Benarous

9

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12 November 2019

language of work or name

English

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publication date

1 March 1999

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Journal of Biological Chemistry

12 November 2019

published in

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volume

274

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12 November 2019

issue

12

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page(s)

7941-7945

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NF-kappa B: ten years after

12 November 2019

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Rapid proteolysis of I kappa B-alpha is necessary for activation of transcription factor NF-kappa B

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Proteolytic degradation of MAD3 (I kappa B alpha) and enhanced processing of the NF-kappa B precursor p105 are obligatory steps in the activation of NF-kappa B.

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Loss of IkappaB alpha-mediated control over nuclear import and DNA binding enables oncogenic activation of c-Rel

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Stimulation-dependent I kappa B alpha phosphorylation marks the NF-kappa B inhibitor for degradation via the ubiquitin-proteasome pathway

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Signal-induced degradation of I kappa B alpha requires site-specific ubiquitination

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Critical role for lysines 21 and 22 in signal-induced, ubiquitin-mediated proteolysis of I kappa B-alpha

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Identification and characterization of an IkappaB kinase

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IkappaB kinase-beta: NF-kappaB activation and complex formation with IkappaB kinase-alpha and NIK

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The IkappaB kinase complex (IKK) contains two kinase subunits, IKKalpha and IKKbeta, necessary for IkappaB phosphorylation and NF-kappaB activation

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NF-kappaB-inducing kinase activates IKK-alpha by phosphorylation of Ser-176

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Complementation cloning of NEMO, a component of the IkappaB kinase complex essential for NF-kappaB activation

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Ubiquitin: Roles in protein modification and breakdown

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The ubiquitin-proteasome proteolytic pathway

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Ubiquitin, proteasomes, and the regulation of intracellular protein degradation

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Site-specific phosphorylation of IkappaBalpha by a novel ubiquitination-dependent protein kinase activity

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SKP1 connects cell cycle regulators to the ubiquitin proteolysis machinery through a novel motif, the F-box

21 January 2018

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A Complex of Cdc4p, Skp1p, and Cdc53p/Cullin Catalyzes Ubiquitination of the Phosphorylated CDK Inhibitor Sic1p

21 January 2018

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Grr1 of Saccharomyces cerevisiae is connected to the ubiquitin proteolysis machinery through Skp1: coupling glucose sensing to gene expression and the cell cycle

21 January 2018

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F-Box Proteins Are Receptors that Recruit Phosphorylated Substrates to the SCF Ubiquitin-Ligase Complex

21 January 2018

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21 January 2018

Identifiers

DOI

10.1074/JBC.274.12.7941

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:10075690%20AND%20SRC:MED&resulttype=core&format=json

12 November 2019

1 reference