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A more recent version of this article appeared on May 1, 2002
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Submitted on October 22, 2001
Revised on January 28, 2002
Accepted on February 14, 2002
1 Department of Cell Biology, Harvard Medical School, Boston, MA 02115 (present address: Institute of Neuroscience, University of Oregon 1254, Eugene, OR 97403)
2 Center for C. elegans Anatomy, Department of Neuroscience, Albert Einstein College of Medicine, Bronx, NY 10461
3 Department of Pathology, Harvard Medical School, Boston, MA 02115
4 Light Microscopy Group and Cell Biophysics Programme, European Molecular Biology Laboratory, D-69117 Heidelberg, Germany
5 Department of Cell Biology, Harvard Medical School, Boston, MA 02115
* Corresponding author. E-mail address: tom_rapoport{at}hms.harvard.edu.
The endoplasmic reticulum (ER) is divided into rough and smooth domains (RER and SER). The two domains share most proteins, but RER is enriched in some membrane proteins by an unknown mechanism. We studied RER protein targeting by expressing fluorescent protein fusions to ER membrane proteins in C. elegans. In several cell types RER and general ER proteins co-localized, but in neurons RER proteins were concentrated in the cell body while general ER proteins were also found in neurites. Surprisingly RER membrane proteins diffused rapidly within the cell body indicating they are not localized by immobilization. Ribosomes were also concentrated in the cell body suggesting they may be in part responsible for targeting RER membrane proteins.
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