The otubain YOD1 is a deubiquitinating enzyme that associates with p97 to facilitate protein dislocation from the ER
Name
Ernst_Otubain.pdf
Size
271.32 KB
Format
Adobe PDF
Checksum (MD5)
8600d19e33bc957e4dc55ab8ba1c319c
Author(s)
Ploegh, Hidde
Mueller, Britta
Schlieker, Christian
Ernst, Robert
Date Issued
October 2009
Journal
Molecular Cell
Publisher
Elsevier Inc.
Citation
The Otubain YOD1 Is a Deubiquitinating Enzyme that Associates with p97 to Facilitate Protein Dislocation from the ER Ernst, Robert; Mueller, Britta; Ploegh, Hidde L.; Schlieker, Christian doi:10.1016/j.molcel.2009.09.016 (volume 36 issue 1 pp.28 - 38)
Version
Author's final manuscript
Abstract
YOD1 is a highly conserved deubiquitinating enzyme of the ovarian tumor (otubain) family, whose function has yet to be assigned in mammalian cells. YOD1 is a constituent of a multiprotein complex with p97 as its nucleus, suggesting a functional link to a pathway responsible for the dislocation of misfolded proteins from the endoplasmic reticulum. Expression of a YOD1 variant deprived of its deubiquitinating activity imposes a halt on the dislocation reaction, as judged by the stabilization of various dislocation substrates. Accordingly, we observe an increase in polyubiquitinated dislocation intermediates in association with p97 in the cytosol. This dominant-negative effect is dependent on the UBX and Zinc finger domains, appended to the N and C terminus of the catalytic otubain core domain, respectively. The assignment of a p97-associated ubiquitin processing function to YOD1 adds to our understanding of p97's role in the dislocation process.
MIT Department
Massachusetts Institute of Technology. Department of Biology
Whitehead Institute for Biomedical Research
Terms of Use
Article is made available in accordance with the publisher's policy and may be subject to US copyright law. Please refer to the publisher's site for terms of use.
Persistent DSpace Link
DOI of Published Version
https://doi.org/10.1016/j.molcel.2009.09.016
