![[Feedback]](/icons/banner/feedbackACT.gif){kind=icon}
![[For Subscribers]](/icons/banner/subscriberACT.gif){kind=icon}
![[Archive]](/icons/banner/archiveACT.gif){kind=icon}
![[Search]](/icons/banner/searchACT.gif){kind=icon}
![[Contents]](/icons/banner/tocACT.gif){kind=icon}
|
|
|
|
|
||
Vol. 10, Issue 10, 3409-3423, October 1999
and
*Departments of *Zoology and In all cells examined, specific endoplasmic reticulum (ER) membrane
arrays are induced in response to increased levels of the ER membrane
protein 3-hydroxy 3-methylglutaryl coenzyme A (HMG-CoA) reductase. In
yeast, expression of Hmg1p, one of two yeast HMG-CoA reductase
isozymes, induces assembly of nuclear-associated ER stacks called
karmellae. Understanding the features of HMG-CoA reductase that signal
karmellae biogenesis would provide useful insights into the regulation
of membrane biogenesis. The HMG-CoA reductase protein consists of two
domains, a multitopic membrane domain and a cytosolic catalytic domain.
Previous studies had indicated that the HMG-CoA reductase membrane
domain was exclusively responsible for generation of ER membrane
proliferations. Surprisingly, we discovered that this conclusion was
incorrect: sequences at the carboxyl terminus of HMG-CoA reductase can
profoundly affect karmellae biogenesis. Specifically, truncations of
Hmg1p that removed or shortened the carboxyl terminus were unable to
induce karmellae assembly. This result indicated that the membrane
domain of Hmg1p was not sufficient to signal for karmellae assembly. Using Botany, University of
Washington, Seattle, Washington 98195; and Rosetta
Inpharmatics, Kirkland, Washington 98034
-galactosidase fusions, we demonstrated that the carboxyl terminus was unlikely to simply serve as an oligomerization domain. Our
working hypothesis is that a truncated or misfolded cytosolic domain
prevents proper signaling for karmellae by interfering with the
required tertiary structure of the membrane domain.
This article has been cited by other articles:
|
|
 |
|
  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]
|
|
|
|
 |
|
 Y. Tanaka, K. Ueda, T. Ozawa, I. Kitajima, S. Okamura, M. Morita, S. Yokota, and T. Imanaka Mutation Study of Antithrombin: The Roles of Disulfide Bonds in Intracellular Accumulation and Formation of Russell Body-Like Structures J. Biochem., March 1, 2005; 137(3): 273 - 285. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 R. Amarilio, S. Ramachandran, H. Sabanay, and S. Lev Differential Regulation of Endoplasmic Reticulum Structure through VAP-Nir Protein Interaction J. Biol. Chem., February 18, 2005; 280(7): 5934 - 5944. [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]
|
|
|
|
 |
|
 Y. Du, M. Pypaert, P. Novick, and S. Ferro-Novick Aux1p/Swa2p Is Required for Cortical Endoplasmic Reticulum Inheritance in Saccharomyces cerevisiae Mol. Biol. Cell, September 1, 2001; 12(9): 2614 - 2628. [Abstract] [Full Text] [PDF]
|
|
