JCB logo
Accuri Cytometers
  Home | Help | Feedback | Subscriptions | Archive | Search | Table of Contents
Published online 10 July 2000. doi:10.1083/jcb.150.1.77
This Article
Right arrow Full Text
Right arrow Full Text (PDF, 280K)
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 Ng, D. T.W.
Right arrow Articles by Walter, P.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Ng, D. T.W.
Right arrow Articles by Walter, P.
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?

© The Rockefeller University Press, 0021-9525/2000//77 $5.00
The Journal of Cell Biology, Volume 150, Number 1, , 2000 77-88

Original Article

The Unfolded Protein Response Regulates Multiple Aspects of Secretory and Membrane Protein Biogenesis and Endoplasmic Reticulum Quality Control



Davis T.W. Nga, Eric D. Speara, and Peter Walterb,c

a Department of Biochemistry and Molecular Biology, Pennsylvania State University, University Park, Pennsylvania 16802
b Howard Hughes Medical Institute, University of California School of Medicine, San Francisco, California 94143-0448
c Department of Biochemistry and Biophysics, University of California School of Medicine, San Francisco, California 94143-0448
Department of Biochemistry and Molecular Biology, Pennsylvania State University, University Park, PA 16802.(814) 863-5876(814) 863-5686

dtn1{at}psu.edu

The unfolded protein response (UPR) is an intracellular signaling pathway that relays signals from the lumen of the ER to activate target genes in the nucleus. We devised a genetic screen in the yeast Saccharomyces cerevisiae to isolate mutants that are dependent on activation of the pathway for viability. Using this strategy, we isolated mutants affecting various aspects of ER function, including protein translocation, folding, glycosylation, glycosylphosphatidylinositol modification, and ER-associated protein degradation (ERAD). Extending results gleaned from the genetic studies, we demonstrate that the UPR regulates trafficking of proteins at the translocon to balance the needs of biosynthesis and ERAD. The approach also revealed connections of the UPR to other regulatory pathways. In particular, we identified SON1/RPN4, a recently described transcriptional regulator for genes encoding subunits of the proteasome. Our genetic strategy, therefore, offers a powerful means to provide insight into the physiology of the UPR and to identify novel genes with roles in many aspects of secretory and membrane protein biogenesis.

Key Words: protein translocation • protein maturation • gene regulation • glycosylation • protein degradation

© 2000 The Rockefeller University Press

Abbreviations used in this paper: CPY, carboxypeptidase Y; ERAD, ER-associated protein degradation; GPI, glycosylphosphatidylinositol; PER, protein processing in the ER gene; UPR, unfolded protein response; UPRE, unfolded protein response element.


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?


This article has been cited by other articles:



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