A Class of Membrane Proteins Shaping the Tubular Endoplasmic Reticulum.
From: Howard Hughes Medical Institute and Department of Cell Biology, Harvard Medical School, 240 Longwood Avenue, Boston, MA 02115, USA.
Cell
- Publish Date: Feb 2006
- ISSN: 0092-8674
- Volume: 124
- Issue: 3
- Pages: 573-86
- Medium: Print
- Language: English
- Citation (JAMA): Voeltz Gia K, Prinz William A, Shibata Yoko, et al. A Class of Membrane Proteins Shaping the Tubular Endoplasmic Reticulum.. Cell Feb 2006;124:573-86
Abstract
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.
Mesh Headings (Keywords): Animals, COS Cells, Calcium Signaling, Cercopithecus aethiops, Endoplasmic Reticulum, Female, Humans, Intracellular Signaling Peptides and Proteins, Membrane Proteins, Membrane Transport Proteins, Myelin Proteins, Oocytes, Rats, Recombinant Proteins, Saccharomyces cerevisiae, Saccharomyces cerevisiae Proteins, Transfection
Check for Full Text / PubMed Unique Identifier (PMID): 16469703
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