TY - JOUR
T1 - Mechanisms determining the morphology of the peripheral ER
AU - Shibata, Yoko
AU - Shemesh, Tom
AU - Prinz, William A.
AU - Palazzo, Alexander F.
AU - Kozlov, Michael M.
AU - Rapoport, Tom A.
N1 - Funding Information:
We thank C. Denison, J. Minsteris, and S. Gygi for mass spectrometry analysis; J. Baughman for microarray analysis; A. Condon and A. Boye-Doe for technical assistance; J. Iwasa for help with illustrations; G. Kreibich, K. Ogawa-Goto, L. Lu, and R. Yan for materials; the Nikon Imaging Center and the Electron Microscopy facility at HMS for microscopy assistance; and R. Klemm and A. Osborne for critical reading of the manuscript. Y.S. was supported by the American Heart Association and is a Howard Hughes Medical Institute postdoctoral fellow. W.A.P. is supported by the Intramural Research Program of the National Institute of Diabetes and Digestive and Kidney Diseases. T.A.R. is a Howard Hughes Medical Institute Investigator. M.M.K. is supported by the Israel Science Foundation (ISF) and the Marie Curie network “Virus Entry.”
PY - 2010/11/24
Y1 - 2010/11/24
N2 - The endoplasmic reticulum (ER) consists of the nuclear envelope and a peripheral network of tubules and membrane sheets. The tubules are shaped by the curvature-stabilizing proteins reticulons and DP1/Yop1p, but how the sheets are formed is unclear. Here, we identify several sheet-enriched membrane proteins in the mammalian ER, including proteins that translocate and modify newly synthesized polypeptides, as well as coiled-coil membrane proteins that are highly upregulated in cells with proliferated ER sheets, all of which are localized by membrane-bound polysomes. These results indicate that sheets and tubules correspond to rough and smooth ER, respectively. One of the coiled-coil proteins, Climp63, serves as a "luminal ER spacer" and forms sheets when overexpressed. More universally, however, sheet formation appears to involve the reticulons and DP1/Yop1p, which localize to sheet edges and whose abundance determines the ratio of sheets to tubules. These proteins may generate sheets by stabilizing the high curvature of edges.
AB - The endoplasmic reticulum (ER) consists of the nuclear envelope and a peripheral network of tubules and membrane sheets. The tubules are shaped by the curvature-stabilizing proteins reticulons and DP1/Yop1p, but how the sheets are formed is unclear. Here, we identify several sheet-enriched membrane proteins in the mammalian ER, including proteins that translocate and modify newly synthesized polypeptides, as well as coiled-coil membrane proteins that are highly upregulated in cells with proliferated ER sheets, all of which are localized by membrane-bound polysomes. These results indicate that sheets and tubules correspond to rough and smooth ER, respectively. One of the coiled-coil proteins, Climp63, serves as a "luminal ER spacer" and forms sheets when overexpressed. More universally, however, sheet formation appears to involve the reticulons and DP1/Yop1p, which localize to sheet edges and whose abundance determines the ratio of sheets to tubules. These proteins may generate sheets by stabilizing the high curvature of edges.
UR - http://www.scopus.com/inward/record.url?scp=79251471434&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=79251471434&partnerID=8YFLogxK
U2 - 10.1016/j.cell.2010.11.007
DO - 10.1016/j.cell.2010.11.007
M3 - Article
C2 - 21111237
AN - SCOPUS:79251471434
SN - 0092-8674
VL - 143
SP - 774
EP - 788
JO - Cell
JF - Cell
IS - 5
ER -