(Q53178691)

12 May 2018

title

FAT10 and NUB1L bind to the VWA domain of Rpn10 and Rpn1 to enable proteasome-mediated proteolysis. (English)

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12 May 2018

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Neha Rani

1

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12 May 2018

Annette Aichem

2

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12 May 2018

Gunter Schmidtke

3

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12 May 2018

Stefan G Kreft

4

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12 May 2018

Marcus Groettrup

5

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12 May 2018

language of work or name

English

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publication date

20 March 2012

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12 May 2018

published in

Nature Communications

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12 May 2018

volume

3

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12 May 2018

page(s)

749

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12 May 2018

https://scigraph.springernature.com/pub.10.1038/ncomms1752

exact match

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Rad23 and Rpn10 serve as alternative ubiquitin receptors for the proteasome

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12 December 2020

Proteasome subunit Rpn1 binds ubiquitin-like protein domains

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A MHC-encoded ubiquitin-like protein (FAT10) binds noncovalently to the spindle assembly checkpoint protein MAD2

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The ubiquitin-like protein FAT10 forms covalent conjugates and induces apoptosis

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12 December 2020

The multiubiquitin-chain-binding protein Mcb1 is a component of the 26S proteasome in Saccharomyces cerevisiae and plays a nonessential, substrate-specific role in protein turnover.

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Together, Rpn10 and Dsk2 can serve as a polyubiquitin chain-length sensor

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USE1 is a bispecific conjugating enzyme for ubiquitin and FAT10, which FAT10ylates itself in cis.

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NEDD8 ultimate buster-1L interacts with the ubiquitin-like protein FAT10 and accelerates its degradation

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Multiubiquitin chain binding and protein degradation are mediated by distinct domains within the 26 S proteasome subunit Mcb1.

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12 December 2020

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Multiubiquitin chain receptors define a layer of substrate selectivity in the ubiquitin-proteasome system

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Budding yeast Dsk2p is a polyubiquitin-binding protein that can interact with the proteasome

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Rad23 links DNA repair to the ubiquitin/proteasome pathway

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12 December 2020

Identification of seven new humanMHC class I region genes around theHLA-F locus

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Crossref

https://api.crossref.org/works/10.1038%2FNCOMMS1752

7 January 2021

inferred from DOI database lookup

Additional modules for versatile and economical PCR-based gene deletion and modification in Saccharomyces cerevisiae

1 reference

Crossref

https://api.crossref.org/works/10.1038%2FNCOMMS1752

7 January 2021

inferred from DOI database lookup

Identifiers

DOI

10.1038/NCOMMS1752

1 reference

12 May 2018

0 references

1 reference

12 May 2018