Note to users. If you're seeing this message, it means that your browser cannot find this page's style/presentation instructions -- or possibly that you are using a browser that does not support current Web standards. Find out more about why this message is appearing, and what you can do to make your experience of our site the best it can be.

Subscribe

Logo for

J. Cell Biol. 167 (1): 23-25

Copyright © 2004 by the Rockefeller University Press.


Comment

Membrane biogenesis and the unfolded protein response

David Ron1, and Randolph Y. Hampton2

1 Skirball Institute of Biomolecular Medicine, School of Medicine, New York University, New York, NY 10016
2 Division of Biological Sciences, University of California, San Diego, La Jolla, CA 92093

Correspondence to David Ron: ron{at}saturn.med.nyu.edu; or Randolph Y. Hampton: rhampton{at}ucsd.edu

Abstract Back to Top

Abstract: In addition to serving as the entry point for newly translated polypeptides making their way through the secretory pathway, the endoplasmic reticulum (ER) also synthesizes many lipid components of the entire endomembrane system. A report published in this issue implicates a signaling pathway known to respond to ER unfolded protein load in the control of phospholipid biosynthesis by the organelle (Sriburi et al., 2004). The reasonable notion that demand for ER membrane is integrated with protein processing capacity was initially suggested by genetic analysis of yeast. The new data lend direct support for this idea and imply interesting mechanistic possibilities for how this coupling develops.

Abbreviations used in this paper: UPR, unfolded protein response; XBP1, X-box binding protein 1.


THIS ARTICLE HAS BEEN CITED BY OTHER ARTICLES:
Activation of the unfolded protein response pathway causes ceramide accumulation in yeast and INS-1E insulinoma cells.
S. Epstein, C. L. Kirkpatrick, G. A. Castillon, M. Muniz, I. Riezman, F. P. A. David, C. B. Wollheim, and H. Riezman (2012)
J. Lipid Res. 53, 412-420
   Abstract »    Full Text »    PDF »
Orm1 and Orm2 are conserved endoplasmic reticulum membrane proteins regulating lipid homeostasis and protein quality control.
S. Han, M. A. Lone, R. Schneiter, and A. Chang (2010)
PNAS 107, 5851-5856
   Abstract »    Full Text »    PDF »
Abnormal Expression of Collagen IV in Lens Activates Unfolded Protein Response Resulting in Cataract.
Z. Firtina, B. P. Danysh, X. Bai, D. B. Gould, T. Kobayashi, and M. K. Duncan (2009)
J. Biol. Chem. 284, 35872-35884
   Abstract »    Full Text »    PDF »
Airway Epithelial Inflammation-induced Endoplasmic Reticulum Ca2+ Store Expansion Is Mediated by X-box Binding Protein-1.
M. E. B. Martino, J. C. Olsen, N. B. Fulcher, M. C. Wolfgang, W. K. O'Neal, and C. M. P. Ribeiro (2009)
J. Biol. Chem. 284, 14904-14913
   Abstract »    Full Text »    PDF »
Analysis of Quality Control Substrates in Distinct Cellular Compartments Reveals a Unique Role for Rpn4p in Tolerating Misfolded Membrane Proteins.
M. B. Metzger and S. Michaelis (2009)
Mol. Biol. Cell 20, 1006-1019
   Abstract »    Full Text »    PDF »
Flavivirus Infection Activates the XBP1 Pathway of the Unfolded Protein Response To Cope with Endoplasmic Reticulum Stress.
C.-Y. Yu, Y.-W. Hsu, C.-L. Liao, and Y.-L. Lin (2006)
J. Virol. 80, 11868-11880
   Abstract »    Full Text »    PDF »
Multiple Endoplasmic Reticulum-to-Nucleus Signaling Pathways Coordinate Phospholipid Metabolism with Gene Expression by Distinct Mechanisms.
S. A. Jesch, P. Liu, X. Zhao, M. T. Wells, and S. A. Henry (2006)
J. Biol. Chem. 281, 24070-24083
   Abstract »    Full Text »    PDF »
Endoplasmic reticulum stress modulates the response of myelinating oligodendrocytes to the immune cytokine interferon-{gamma}.
W. Lin, H. P. Harding, D. Ron, and B. Popko (2005)
J. Cell Biol. 169, 603-612
   Abstract »    Full Text »    PDF »

To Advertise     Find Products


Science Signaling. ISSN 1937-9145 (online), 1945-0877 (print). Pre-2008: Science's STKE. ISSN 1525-8882