Affordable Access

Publisher Website

Ubiquitin Chain Elongation Enzyme Ufd2 Regulates a Subset of Doa10 Substrates*

Authors
Journal
Journal of Biological Chemistry
0021-9258
Publisher
American Society for Biochemistry and Molecular Biology
Publication Date
Volume
285
Issue
14
Identifiers
DOI: 10.1074/jbc.m110.110551
Keywords
  • Protein Synthesis And Degradation
  • Cell Biology
Disciplines
  • Biology

Abstract

Ufd2 is the founding member of E4 enzymes that are specifically involved in ubiquitin chain elongation but whose roles in proteolysis remain scarce. Here, using a genome-wide screen, we identified one cellular target of yeast Ufd2 as the membrane protein Pex29. The ubiquitin chains assembled on Pex29 in vivo by Ufd2 mainly contain Lys-48 linkages. We found that the ubiquitin-protein E3 ligase for overexpressed Pex29 is Doa10, which is known to be involved in protein quality control. Interestingly, not all Doa10 substrates are regulated by Ufd2, suggesting that E4 involvement is not specific to a particular E3, but may depend on the spatial arrangement of the E3-substrate interaction. Cells lacking UFD2 elicit an unfolded protein response, expanding the physiological function of Ufd2. Our results lead to novel insights into the biological role of Ufd2 and further underscore the significance of Ufd2 in proteolysis.

There are no comments yet on this publication. Be the first to share your thoughts.

Statistics

Seen <100 times
0 Comments

More articles like this

Ubiquitin chain elongation enzyme Ufd2 regulates a...

on Journal of Biological Chemistr... Apr 02, 2010

Definitive evidence for Ufd2-catalyzed elongation...

on Biochemical and Biophysical Re... Jan 01, 2004

Definitive evidence for Ufd2-catalyzed elongation...

on Biochemical and Biophysical Re... Jul 30, 2004

An unusual transmembrane helix in the endoplasmic...

on Journal of Biological Chemistr... Jun 10, 2011
More articles like this..