Diverse polyubiquitin interaction properties of ubiquitin-associated domains (Q46592679)

23 December 2017

title

Diverse polyubiquitin interaction properties of ubiquitin-associated domains (English)

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23 December 2017

author name string

Shahri Raasi

1

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23 December 2017

Ranjani Varadan

2

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23 December 2017

David Fushman

3

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23 December 2017

Cecile M Pickart

4

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23 December 2017

publication date

10 July 2005

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23 December 2017

Nature Structural & Molecular Biology

published in

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23 December 2017

volume

12

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23 December 2017

issue

8

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23 December 2017

page(s)

708-714

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23 December 2017

Polyubiquitin chains: polymeric protein signals

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Proteins containing the UBA domain are able to bind to multi-ubiquitin chains

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Ubiquitin-associated (UBA) domains in Rad23 bind ubiquitin and promote inhibition of multi-ubiquitin chain assembly

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

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Shp1 and Ubx2 are adaptors of Cdc48 involved in ubiquitin-dependent protein degradation

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The Ubx2 and Ubx3 cofactors direct Cdc48 activity to proteolytic and nonproteolytic ubiquitin-dependent processes

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Rad23 ubiquitin-associated domains (UBA) inhibit 26 S proteasome-catalyzed proteolysis by sequestering lysine 48-linked polyubiquitin chains

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Ubiquitin lys63 is involved in ubiquitination of a yeast plasma membrane protein

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SUMO modification of the ubiquitin-conjugating enzyme E2-25K

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Structure, dynamics and interactions of p47, a major adaptor of the AAA ATPase, p97.

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Loss of Ubiquitin-Binding Associated With Paget's Disease of Bone p62 (SQSTM1) Mutations

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Identification of a novel 29-linked polyubiquitin binding protein, Ufd3, using polyubiquitin chain analogues

31 March 2020

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31 March 2020

Identifiers

DOI

10.1038/NSMB962

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23 December 2017

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23 December 2017