Ubiquitination of Keap1, a BTB-Kelch substrate adaptor protein for Cul3, targets Keap1 for degradation by a proteasome-independent pathway (Q24306215)

Cullin 3

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Kelch like ECH associated protein 1

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Nuclear factor, erythroid 2 like 2

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Gigaxonin

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Ectodermal-neural cortex 1

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Ring-box 1

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protein ubiquitination

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Donna D Zhang

1

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Shih-Ching Lo

2

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Zheng Sun

3

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Geetha M Habib

4

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Michael W Lieberman

5

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Mark Hannink

Journal of Biological Chemistry

6

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language of work or name

English

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publication date

26 August 2005

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published in

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volume

280

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issue

34

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page(s)

30091-9

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The Keap1-BTB protein is an adaptor that bridges Nrf2 to a Cul3-based E3 ligase: oxidative stress sensing by a Cul3-Keap1 ligase

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Oxidative stress sensor Keap1 functions as an adaptor for Cul3-based E3 ligase to regulate proteasomal degradation of Nrf2

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Keap1 is a redox-regulated substrate adaptor protein for a Cul3-dependent ubiquitin ligase complex

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BTB protein Keap1 targets antioxidant transcription factor Nrf2 for ubiquitination by the Cullin 3-Roc1 ligase

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The gene encoding gigaxonin, a new member of the cytoskeletal BTB/kelch repeat family, is mutated in giant axonal neuropathy

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Gigaxonin is associated with the Golgi and dimerises via its BTB domain.

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Ubiquitination and degradation of the substrate recognition subunits of SCF ubiquitin-protein ligases

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7 January 2021

Intermediate filament aggregation in fibroblasts of giant axonal neuropathy patients is aggravated in non dividing cells and by microtubule destabilization

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Phytochemicals from cruciferous plants protect against cancer by modulating carcinogen metabolism

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Oxidants are a major contributor to aging

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Identifiers

DOI

10.1074/JBC.M501279200

1 reference

Consolidated OpenCitations Corpus – April 2017

4537709

4537709

1 reference

Consolidated OpenCitations Corpus – April 2017

Consolidated OpenCitations Corpus – April 2017

1 reference