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Journal article

The catalytic activity of Ubp6 enhances maturation of the proteasomal regulatory particle.

Abstract:

The 26S proteasome is a 2.5 MDa macromolecular machine responsible for targeted protein degradation. Recently, four chaperones were identified that promote the assembly of the 19S regulatory particle (RP). Here, we probe the dynamic architecture of the proteasome by applying quantitative proteomics and mass spectrometry (MS) of intact complexes to provide a detailed characterization of how Ubp6 assists this assembly process. Our MS data demonstrate stoichiometric binding of chaperones and Ubp...

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Publication status:
Published

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Authors


Stengel, F More by this author
Fukunaga, K More by this author
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Journal:
Molecular cell
Volume:
42
Issue:
5
Pages:
637-649
Publication date:
2011-06-05
DOI:
EISSN:
1097-4164
ISSN:
1097-2765
URN:
uuid:77b31132-5900-4ee7-9dfc-84eded860d2a
Source identifiers:
159414
Local pid:
pubs:159414

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