MIT Libraries logoDSpace@MIT

MIT
View Item 
  • DSpace@MIT Home
  • MIT Open Access Articles
  • MIT Open Access Articles
  • View Item
  • DSpace@MIT Home
  • MIT Open Access Articles
  • MIT Open Access Articles
  • View Item
JavaScript is disabled for your browser. Some features of this site may not work without it.

Enzymatic Blockade of the Ubiquitin-Proteasome Pathway

Author(s)
Ernst, Robert; Claessen, Jasper H. L.; Mueller, Britta; Sanyal, Sumana; Spooner, Eric; van der Veen, Annemarthe G.; Kirak, Oktay; Schlieker, Christian D.; Weihofen, Wilhelm A.; Ploegh, Hidde; ... Show more Show less
Thumbnail
DownloadErnst-2011-Enzymatic Blockade o.pdf (1.416Mb)
PUBLISHER_CC

Publisher with Creative Commons License

Creative Commons Attribution

Terms of use
Creative Commons Attribution http://creativecommons.org/licenses/by/2.5
Metadata
Show full item record
Abstract
Ubiquitin-dependent processes control much of cellular physiology. We show that expression of a highly active, Epstein-Barr virus-derived deubiquitylating enzyme (EBV-DUB) blocks proteasomal degradation of cytosolic and ER-derived proteins by preemptive removal of ubiquitin from proteasome substrates, a treatment less toxic than the use of proteasome inhibitors. Recognition of misfolded proteins in the ER lumen, their dislocation to the cytosol, and degradation are usually tightly coupled but can be uncoupled by the EBV-DUB: a misfolded glycoprotein that originates in the ER accumulates in association with cytosolic chaperones as a deglycosylated intermediate. Our data underscore the necessity of a DUB activity for completion of the dislocation reaction and provide a new means of inhibition of proteasomal proteolysis with reduced cytotoxicity.
Date issued
2011-03
URI
http://hdl.handle.net/1721.1/65337
Department
Massachusetts Institute of Technology. Department of Biology
Journal
PLoS Biology
Publisher
Public Library of Science
Citation
Ernst, Robert et al. “Enzymatic Blockade of the Ubiquitin-Proteasome Pathway.” Ed. Jonathan D. Ashwell. PLoS Biology 8.3 (2011) : e1000605.
Version: Final published version
ISSN
1544-9173
1545-7885

Collections
  • MIT Open Access Articles

Browse

All of DSpaceCommunities & CollectionsBy Issue DateAuthorsTitlesSubjectsThis CollectionBy Issue DateAuthorsTitlesSubjects

My Account

Login

Statistics

OA StatisticsStatistics by CountryStatistics by Department
MIT Libraries
PrivacyPermissionsAccessibilityContact us
MIT
Content created by the MIT Libraries, CC BY-NC unless otherwise noted. Notify us about copyright concerns.