Molecular Biology of the Cell Sign up for new MBC in Press e-TOCs!

Home Help [Feedback] [For Subscribers] [Archive] [Search] [Contents]
 QUICK SEARCH:   [advanced]


     


Originally published as MBC in Press, 10.1091/mbc.E03-05-0325 on November 14, 2003

Vol. 15, Issue 2, 447-455, February 2004

This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow All Versions of this Article:
E03-05-0325v1
15/2/447    most recent
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Le Gall, S.
Right arrow Articles by Rapoport, T.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Le Gall, S.
Right arrow Articles by Rapoport, T.

The Endoplasmic Reticulum Membrane Is Permeable to Small Molecules

Sylvie Le Gall, Andrea Neuhof, and Tom Rapoport *

Department of Cell Biology, Howard Hughes Medical Institute/Harvard Medical School, Boston, Massachusetts 02115-6091

Submitted May 22, 2003; Revised September 5, 2003; Accepted October 1, 2003
Monitoring Editor: Reid Gilmore

The lumen of the endoplasmic reticulum (ER) differs from the cytosol in its content of ions and other small molecules, but it is unclear whether the ER membrane is as impermeable as other membranes in the cell. Here, we have tested the permeability of the ER membrane to small, nonphysiological molecules. We report that isolated ER vesicles allow different chemical modification reagents to pass from the outside into the lumen with little hindrance. In permeabilized cells, the ER membrane allows the passage of a small, charged modification reagent that is unable to cross the plasma membrane or the lysosomal and trans-Golgi membranes. A larger polar reagent of ~5 kDa is unable to pass through the ER membrane. Permeation of the small molecules is passive because it occurs at low temperature in the absence of energy. These data indicate that the ER membrane is significantly more leaky than other cellular membranes, a property that may be required for protein folding and other functions of the ER.


Article published online ahead of print. Mol. Biol. Cell 10.1091/mbc.E03-05-0325. Article and publication date are available at www.molbiolcell.org/cgi/doi/10.1091/mbc.E03-05-0325.

* Corresponding author. E-mail address: tom_rapoport{at}hms.harvard.edu.




This article has been cited by other articles:


Home page
J. Virol.Home page
E. K. Rainey-Barger, B. Magnuson, and B. Tsai
A Chaperone-Activated Nonenveloped Virus Perforates the Physiologically Relevant Endoplasmic Reticulum Membrane
J. Virol., December 1, 2007; 81(23): 12996 - 13004.
[Abstract] [Full Text] [PDF]


Home page
Proc. Natl. Acad. Sci. USAHome page
L.-P. Sun, J. Seemann, J. L. Goldstein, and M. S. Brown
From the Cover: Sterol-regulated transport of SREBPs from endoplasmic reticulum to Golgi: Insig renders sorting signal in Scap inaccessible to COPII proteins
PNAS, April 17, 2007; 104(16): 6519 - 6526.
[Abstract] [Full Text] [PDF]


Home page
Am. J. Physiol. Cell Physiol.Home page
B. Lizak, I. Czegle, M. Csala, A. Benedetti, J. Mandl, and G. Banhegyi
Translocon pores in the endoplasmic reticulum are permeable to small anions
Am J Physiol Cell Physiol, September 1, 2006; 291(3): 511 - 517.
[Abstract] [Full Text] [PDF]


Home page
J. Cell Biol.Home page
M. L. Forster, K. Sivick, Y.-n. Park, P. Arvan, W. I. Lencer, and B. Tsai
Protein disulfide isomerase-like proteins play opposing roles during retrotranslocation
J. Cell Biol., June 19, 2006; 173(6): 853 - 859.
[Abstract] [Full Text] [PDF]


Home page
RNAHome page
R. S. Lerner and C. V. Nicchitta
mRNA translation is compartmentalized to the endoplasmic reticulum following physiological inhibition of cap-dependent translation
RNA, May 1, 2006; 12(5): 775 - 789.
[Abstract] [Full Text] [PDF]


Home page
J. Biol. Chem.Home page
K. L. McCormick, X. Wang, and G. J. Mick
Evidence That the 11 {beta}-Hydroxysteroid Dehydrogenase (11 {beta}-HSD1) Is Regulated by Pentose Pathway Flux: STUDIES IN RAT ADIPOCYTES AND MICROSOMES
J. Biol. Chem., January 6, 2006; 281(1): 341 - 347.
[Abstract] [Full Text] [PDF]


Home page
J. Biol. Chem.Home page
Z.-Y. Guo, S. Lin, J. A. Heinen, C. C. Y. Chang, and T.-Y. Chang
The Active Site His-460 of Human Acyl-coenzyme A:Cholesterol Acyltransferase 1 Resides in a Hitherto Undisclosed Transmembrane Domain
J. Biol. Chem., November 11, 2005; 280(45): 37814 - 37826.
[Abstract] [Full Text] [PDF]


Home page
J. Biol. Chem.Home page
C. E. Jessop and N. J. Bulleid
Glutathione Directly Reduces an Oxidoreductase in the Endoplasmic Reticulum of Mammalian Cells
J. Biol. Chem., December 31, 2004; 279(53): 55341 - 55347.
[Abstract] [Full Text] [PDF]


Home page
J. Biol. Chem.Home page
S. Chakravarthi and N. J. Bulleid
Glutathione Is Required to Regulate the Formation of Native Disulfide Bonds within Proteins Entering the Secretory Pathway
J. Biol. Chem., September 17, 2004; 279(38): 39872 - 39879.
[Abstract] [Full Text] [PDF]


Home page
J. Biol. Chem.Home page
Y. Li, M. Ge, L. Ciani, G. Kuriakose, E. J. Westover, M. Dura, D. F. Covey, J. H. Freed, F. R. Maxfield, J. Lytton, et al.
Enrichment of Endoplasmic Reticulum with Cholesterol Inhibits Sarcoplasmic-Endoplasmic Reticulum Calcium ATPase-2b Activity in Parallel with Increased Order of Membrane Lipids: IMPLICATIONS FOR DEPLETION OF ENDOPLASMIC RETICULUM CALCIUM STORES AND APOPTOSIS IN CHOLESTEROL-LOADED MACROPHAGES
J. Biol. Chem., August 27, 2004; 279(35): 37030 - 37039.
[Abstract] [Full Text] [PDF]




Home Help [Feedback] [For Subscribers] [Archive] [Search] [Contents]
Copyright © 2004 by The American Society for Cell Biology. Terms of copyright protection, warranties, and disclaimers.