JCB logo
Avanti Polar Lipids, Inc.
  Home | Help | Feedback | Subscriptions | Archive | Search | Table of Contents
Published online 4 April 2005. doi:10.1083/jcb.200411136
The Rockefeller University Press, 0021-9525 $8.00
JCB, Volume 169, Number 1, 73-82
This Article
Right arrow Full Text
Right arrow Full Text (PDF, 1318K)
Right arrow PPT slides of all figures
Right arrow Alert me when this article is cited
Right arrow Citation Map
Services
Right arrow Email this article
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new content in the JCB
Right arrow Download to citation manager
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via CrossRef
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Spear, E. D.
Right arrow Articles by Ng, D. T.W.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Spear, E. D.
Right arrow Articles by Ng, D. T.W.
Related Collections
Right arrowRelated Article
Social Bookmarking
Add to CiteULike   Add to Complore   Add to Connotea   Add to Del.icio.us   Add to Digg   Add to Facebook   Add to Reddit   Add to Technorati   Add to Twitter  
What's this?

Article

Single, context-specific glycans can target misfolded glycoproteins for ER-associated degradation



Eric D. Spear and Davis T.W. Ng

Department of Biochemistry and Molecular Biology, Pennsylvania State University, University Park, PA 16802

Correspondence to Davis T.W. Ng: dtn1{at}psu.edu

The endoplasmic reticulum (ER) maintains an environment essential for secretory protein folding. Consequently, the premature transport of polypeptides would be harmful to the cell. To avert this scenario, mechanisms collectively termed "ER quality control" prevent the transport of nascent polypeptides until they properly fold. Irreversibly misfolded molecules are sorted for disposal by the ER-associated degradation (ERAD) pathway. To better understand the relationship between quality control and ERAD, we studied a new misfolded variant of carboxypeptidase Y (CPY). The molecule was recognized and retained by ER quality control but failed to enter the ERAD pathway. Systematic analysis revealed that a single, specific N-linked glycan of CPY was required for sorting into the pathway. The determinant is dependent on the putative lectin-like receptor Htm1/Mnl1p. The discovery of a similar signal in misfolded proteinase A supported the generality of the mechanism. These studies show that specific signals embedded in glycoproteins can direct their degradation if they fail to fold.

E.D. Spear's current address is Dept. of Biology, Massachusetts Institute of Technology, Cambridge, MA 02139.

Abbreviations used in this paper: CPY, carboxypeptidase Y; ERAD, ER-associated degradation; GT, glucosyltransferase; UPR, unfolded protein response.


Add to CiteULike CiteULike   Add to Complore Complore   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us   Add to Digg Digg   Add to Facebook Facebook   Add to Reddit Reddit   Add to Technorati Technorati   Add to Twitter Twitter    What's this?

Related Article

Signal for ER-associated degradation
Rabiya S. Tuma
J. Cell Biol. 2005 169: 15. [Full Text] [PDF]



This article has been cited by other articles:



  Home | Help | Feedback | Subscriptions | Archive | Search | Table of Contents