|
|
|
|
|
|
|
|
|||||
| Home Help Feedback Subscriptions Archive Search Table of Contents | |||||
Journal of Cell Science, Vol 63, Issue 1 1-20, Copyright © 1983 by Company of Biologists
JOURNAL ARTICLES |
RG Anderson, L Orci, MS Brown, LM Garcia-Segura and JL Goldstein
The crystalloid endoplasmic reticulum (ER) consists of hexagonally packed membrane tubules that contain 3-hydroxy-3-methylglutaryl coenzyme A reductase (HMG CoA reductase), an intrinsic membrane protein that catalyses the rate-limiting step in cholesterol synthesis. The crystalloid ER appears in a clone of Chinese hamster ovary cells, designated UT-1, that contain high levels of HMG CoA reductase as a result of growth in the presence of compactin, a competitive inhibitor of the reductase. In the present studies, we have used ultrastructural morphometry to estimate that the crystalloid ER: (1) occupies about 15% of the volume of UT-1 cells; (2) contains 3.4-fold more membrane area than the plasma membrane; and (3) contains less than 700 subunits of HMG CoA reductase per micrometer2 of membrane surface. The crystalloid ER tubules contain 2000 intramembrane particles per micrometer2 with a mean diameter of 10.4 nm, as determined by freeze-fracture. The crystalloid ER membranes are low in cholesterol, as indicated by the small number of filipin-cholesterol complexes in freeze-fracture images after treatment with filipin. The addition of cholesterol or related sterols to UT-1 cells promoted a rapid and stepwise disappearance of the crystalloid ER. Initially, the crystalloid ER fragmented into randomly arranged vesicles and tubules. Subsequently, membrane-bound structures disappeared from the cell so that after incubation with cholesterol for 24-72 h, the cells appeared completely normal. We found no morphological evidence that autophagic vacuoles participate in the degradation. We conclude: (1) that the crystalloid ER is more extensive than necessary merely to support HMG CoA reductase; and (2) that upon exposure to cholesterol the crystalloid ER is degraded by a process that does not involve autophagy.
This article has been cited by other articles:
|
|
 |
|
  T. Sprocati, P. Ronchi, A. Raimondi, M. Francolini, and N. Borgese Dynamic and reversible restructuring of the ER induced by PDMP in cultured cells J. Cell Sci., August 1, 2006; 119(15): 3249 - 3260. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 Z. A. Almsherqi, S. D. Kohlwein, and Y. Deng Cubic membranes: a legend beyond the Flatland* of cell membrane organization J. Cell Biol., June 19, 2006; 173(6): 839 - 844. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 J. Loertscher, L. L. Larson, C. K. Matson, M. L. Parrish, A. Felthauser, A. Sturm, C. Tachibana, M. Bard, and R. Wright Endoplasmic Reticulum-Associated Degradation Is Required for Cold Adaptation and Regulation of Sterol Biosynthesis in the Yeast Saccharomyces cerevisiae. Eukaryot. Cell, April 1, 2006; 5(4): 712 - 722. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 R. Sannerud, M. Marie, C. Nizak, H. A. Dale, K. Pernet-Gallay, F. Perez, B. Goud, and J. Saraste Rab1 Defines a Novel Pathway Connecting the Pre-Golgi Intermediate Compartment with the Cell Periphery Mol. Biol. Cell, April 1, 2006; 17(4): 1514 - 1526. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 J. Lefman, P. Zhang, T. Hirai, R. M. Weis, J. Juliani, D. Bliss, M. Kessel, E. Bos, P. J. Peters, and S. Subramaniam Three-Dimensional Electron Microscopic Imaging of Membrane Invaginations in Escherichia coli Overproducing the Chemotaxis Receptor Tsr J. Bacteriol., August 1, 2004; 186(15): 5052 - 5061. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
E. L. Snapp, R. S. Hegde, M. Francolini, F. Lombardo, S. Colombo, E. Pedrazzini, N. Borgese, and J. Lippincott-Schwartz Formation of stacked ER cisternae by low affinity protein interactions J. Cell Biol., October 27, 2003; 163(2): 257 - 269. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 A. J. Koning, L. L. Larson, E. J. Cadera, M. L. Parrish, and R. L. Wright Mutations That Affect Vacuole Biogenesis Inhibit Proliferation of the Endoplasmic Reticulum in Saccharomyces cerevisiae Genetics, April 1, 2002; 160(4): 1335 - 1352. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
D. A. Profant, C. J. Roberts, A. J. Koning, and R. L. Wright The Role of the 3-Hydroxy 3-Methylglutaryl Coenzyme A Reductase Cytosolic Domain in Karmellae Biogenesis Mol. Biol. Cell, October 1, 1999; 10(10): 3409 - 3423. [Abstract] [Full Text]
|
|
|
|
|
|
F. Becker, L. Block-Alper, G. Nakamura, J. Harada, K. D. Wittrup, and D. I. Meyer Expression of the 180-kD Ribosome Receptor Induces Membrane Proliferation and Increased Secretory Activity in Yeast J. Cell Biol., July 26, 1999; 146(2): 273 - 284. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
L. Ostedgaard, B Zeiher, and M. Welsh Processing of CFTR bearing the P574H mutation differs from wild-type and deltaF508-CFTR J. Cell Sci., January 7, 1999; 112(13): 2091 - 2098. [Abstract] [PDF]
|
|
|
|
|
|
L McLaughlin, B Burchell, M Pritchard, C. Wolf, and T Friedberg Treatment of mammalian cells with the endoplasmic reticulum-proliferator compactin strongly induces recombinant and endogenous xenobiotic metabolizing enzymes and 3-hydroxy-3-methylglutaryl-CoA reductase in vitro J. Cell Sci., January 2, 1999; 112(4): 515 - 523. [Abstract] [PDF]
|
|
|
|
|
|
A Yamamoto, R Masaki, and Y Tashiro Formation of crystalloid endoplasmic reticulum in COS cells upon overexpression of microsomal aldehyde dehydrogenase by cDNA transfection J. Cell Sci., January 7, 1996; 109(7): 1727 - 1738. [Abstract] [PDF]
|
|
