Cdc48-Ufd2-Rad23: the road less ubiquitinated?

Targeting substrates to the proteasome is generally thought to depend on long polyubiquitin chains that form on the substrate. Recent work has led to the provocative proposal that some substrates may be targeted to the proteasome through smaller chains that contain only four to six ubiquitin molecul...

Full description

Saved in:
Bibliographic Details
Published inNature cell biology Vol. 7; no. 3; pp. 207 - 209
Main Authors Bazirgan, Omar A, Hampton, Randolph Y
Format Journal Article
LanguageEnglish
Published England Nature Publishing Group 01.03.2005
Subjects
Adenosine Triphosphatases
Cell Cycle Proteins - physiology
DNA-Binding Proteins - physiology
Fungal Proteins - chemistry
Fungal Proteins - physiology
Models, Biological
Physiological aspects
Proteasome Endopeptidase Complex - chemistry
Proteasome Endopeptidase Complex - metabolism
Protein Structure, Tertiary
Saccharomyces cerevisiae Proteins - physiology
Ubiquitin - chemistry
Ubiquitin - metabolism
Ubiquitin-Conjugating Enzymes
Ubiquitin-proteasome system
Valosin Containing Protein
United States
Online AccessGet full text

Cover

More Information
Summary:Targeting substrates to the proteasome is generally thought to depend on long polyubiquitin chains that form on the substrate. Recent work has led to the provocative proposal that some substrates may be targeted to the proteasome through smaller chains that contain only four to six ubiquitin molecules.
Bibliography:SourceType-Other Sources-1
ObjectType-News-1
content type line 66
ISSN:1465-7392
1476-4679
DOI:10.1038/ncb0305-207