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.

Science 29 February 2008:
Vol. 319. no. 5867, pp. 1247 - 1250
DOI: 10.1126/science.1153634
Prev | Table of Contents | Next

Reports

Membrane Proteins of the Endoplasmic Reticulum Induce High-Curvature Tubules

Junjie Hu,1 Yoko Shibata,1 Christiane Voss,2 Tom Shemesh,3 Zongli Li,4 Margaret Coughlin,5 Michael M. Kozlov,3 Tom A. Rapoport,1* William A. Prinz2*

The tubular structure of the endoplasmic reticulum (ER) appears to be generated by integral membrane proteins, the reticulons and a protein family consisting of DP1 in mammals and Yop1p in yeast. Here, individual members of these families were found to be sufficient to generate membrane tubules. When we purified yeast Yop1p and incorporated it into proteoliposomes, narrow tubules (~15 to 17 nanometers in diameter) were generated. Tubule formation occurred with different lipids; required essentially only the central portion of the protein, including its two long hydrophobic segments; and was prevented by mutations that affected tubule formation in vivo. Tubules were also formed by reconstituted purified yeast Rtn1p. Tubules made in vitro were narrower than normal ER tubules, due to a higher concentration of tubule-inducing proteins. The shape and oligomerization of the "morphogenic" proteins could explain the formation of the tubular ER.

1 Howard Hughes Medical Institute and Department of Cell Biology, Harvard Medical School, 240 Longwood Avenue, Boston, MA 02115, USA.
2 Laboratory of Cell Biochemistry and Biology, National Institute of Diabetes and Digestive and Kidney Disorders (NIDDK), National Institutes of Health, Bethesda, MD 20892, USA.
3 Department of Physiology and Pharmacology, Sackler Faculty of Medicine, Tel Aviv University, Ramat Aviv, 69978 Tel Aviv, Israel.
4 Department of Cell Biology, Harvard Medical School, 240 Longwood Avenue, Boston, MA 02115, USA.
5 Department of Systems Biology, Harvard Medical School, 240 Longwood Avenue, Boston, MA 02115, USA.

* To whom correspondence should be addressed. E-mail: tom_rapoport{at}hms.harvard.edu (T.A.R.); wprinz{at}helix.nih.gov (W.A.P.)

Read the Full Text


THIS ARTICLE HAS BEEN CITED BY OTHER ARTICLES:
Massive Formation of Intracellular Membrane Vesicles in Escherichia coli by a Monotopic Membrane-bound Lipid Glycosyltransferase.
H. M. Eriksson, P. Wessman, C. Ge, K. Edwards, and A. Wieslander (2009)
J. Biol. Chem. 284, 33904-33914
   Abstract »    Full Text »    PDF »
Membrane expansion alleviates endoplasmic reticulum stress independently of the unfolded protein response.
S. Schuck, W. A. Prinz, K. S. Thorn, C. Voss, and P. Walter (2009)
J. Cell Biol. 187, 525-536
   Abstract »    Full Text »    PDF »
Transmembrane Protein-free Membranes Fuse into Xenopus Nuclear Envelope and Promote Assembly of Functional Pores.
E. R. Rafikova, K. Melikov, C. Ramos, L. Dye, and L. V. Chernomordik (2009)
J. Biol. Chem. 284, 29847-29859
   Abstract »    Full Text »    PDF »
Molecular mechanism of membrane constriction and tubulation mediated by the F-BAR protein Pacsin/Syndapin.
Q. Wang, M. V. A. S. Navarro, G. Peng, E. Molinelli, S. Lin Goh, B. L. Judson, K. R. Rajashankar, and H. Sondermann (2009)
PNAS 106, 12700-12705
   Abstract »    Full Text »    PDF »
Cisternal Organization of the Endoplasmic Reticulum during Mitosis.
L. Lu, M. S. Ladinsky, and T. Kirchhausen (2009)
Mol. Biol. Cell 20, 3471-3480
   Abstract »    Full Text »    PDF »
Many variations on a few themes: a broader look at development of iridescent scales (and feathers).
H. T Ghiradella and M. W Butler (2009)
J R Soc Interface 6, S243-S251
   Abstract »    Full Text »    PDF »
ER membrane-bending proteins are necessary for de novo nuclear pore formation.
T. R. Dawson, M. D. Lazarus, M. W. Hetzer, and S. R. Wente (2009)
J. Cell Biol. 184, 659-675
   Abstract »    Full Text »    PDF »
Reshaping of the endoplasmic reticulum limits the rate for nuclear envelope formation.
D. J. Anderson and M. W. Hetzer (2008)
J. Cell Biol. 182, 911-924
   Abstract »    Full Text »    PDF »
An Abscisic Acid-Induced Protein, HVA22, Inhibits Gibberellin-Mediated Programmed Cell Death in Cereal Aleurone Cells.
W.-J. Guo and T.-H. David Ho (2008)
Plant Physiology 147, 1710-1722
   Abstract »    Full Text »    PDF »
The Reticulon and Dp1/Yop1p Proteins Form Immobile Oligomers in the Tubular Endoplasmic Reticulum.
Y. Shibata, C. Voss, J. M. Rist, J. Hu, T. A. Rapoport, W. A. Prinz, and G. K. Voeltz (2008)
J. Biol. Chem. 283, 18892-18904
   Abstract »    Full Text »    PDF »
How the ER gets its shape.
R. Robinson (2008)
J. Cell Biol. 180, 1055
   Full Text »    PDF »


To Advertise     Find Products

Science. ISSN 0036-8075 (print), 1095-9203 (online)