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A class of membrane proteins shaping the tubular endoplasmic reticulum
A class of membrane proteins shaping the tubular endoplasmic reticulum.
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How is the characteristic shape of a membrane bound organelle achieved? We have used an in vitro system to address the mechanism by which the tubular network of the endoplasmic reticulum (ER) is generated and maintained. Based on the inhibitory effect of sulfhydryl reagents and antibodies, network formation in vitro requires the integral membrane protein Rtn4a/NogoA, a member of the ubiquitous reticulon family. Both in yeast and mammalian cells, the reticulons are largely restricted to the tubular ER and are excluded from the continuous sheets of the nuclear envelope and peripheral ER. Upon overexpression, the reticulons form tubular membrane structures. The reticulons interact with DP1/Yop1p, a conserved integral membrane protein that also localizes to the tubular ER. These proteins share an unusual hairpin topology in the membrane. The simultaneous absence of the reticulons and Yop1p in S. cerevisiae results in disrupted tubular ER. We propose that these morphogenic proteins partition into and stabilize highly curved ER membrane tubules.
Voeltz GK, Prinz WA, Shibata Y, Rist JM, Rapoport TA
Cell
2006-02-10 00:00
124
3
573-86
Animals,COS Cells,Calcium Signaling,Cercopithecus aethiops,Endoplasmic Reticulum,Female,Humans,Intracellular Signaling Peptides and Proteins,Membrane Proteins,Membrane Transport Proteins,Oocytes,Rats,Recombinant Proteins,Saccharomyces cerevisiae,Saccharomyces cerevisiae Proteins,Transfection,Intracellular Signaling Peptides and Proteins,Membrane Proteins,Membrane Transport Proteins,RTN4 protein, human,Recombinant Proteins,Saccharomyces cerevisiae Proteins,YOP1 protein, S cerevisiae
Howard Hughes Medical Institute and Department of Cell Biology, Harvard Medical School, 240 Longwood Avenue, Boston, MA 02115, USA
Cell
NIGMS GM052586
0092-8674
10.1016/j.cell.2005.11.047
S0092-8674(06)00067-5
1221
True
16469703
