Note to users. If you're seeing this message, it means that your browser cannot find this page's style/presentation instructions -- or possibly that you are using a browser that does not support current Web standards. Find out more about why this message is appearing, and what you can do to make your experience of our site the best it can be.

Science 28 February 2003:
Vol. 299. no. 5611, pp. 1330 - 1331
DOI: 10.1126/science.1082718
Prev | Table of Contents | Next

Perspectives

CELL BIOLOGY:
Protein Degradation Unlocked

Richard N. Sifers

Protein quality control ensures that newly synthesized misfolded proteins are transported out of the endoplasmic reticulum (ER) and degraded by the proteasome. In his Perspective, Sifers explains the findings of two new studies (Molinari et al., Oda et al.) that identify an ER protein called EDEM as an important molecule in the degradation of misfolded proteins.

The author is in the Departments of Pathology, and Molecular and Cellular Biology, Baylor College of Medicine, Houston, TX 77030, USA. E-mail: rsifers{at}bcm.tmc.edu

Read the Full Text


THIS ARTICLE HAS BEEN CITED BY OTHER ARTICLES:
The mammalian UPR boosts glycoprotein ERAD by suppressing the proteolytic downregulation of ER mannosidase I.
D. J. Termine, K. W. Moremen, and R. N. Sifers (2009)
J. Cell Sci. 122, 976-984
   Abstract »    Full Text »    PDF »
A Novel Protein, Luman/CREB3 Reruitment Factor, Inhibits Luman Activation of the Unfolded Protein Response.
T. E. Audas, Y. Li, G. Liang, and R. Lu (2008)
Mol. Cell. Biol. 28, 3952-3966
   Abstract »    Full Text »    PDF »
Niemann-Pick Type C1 I1061T Mutant Encodes a Functional Protein That Is Selected for Endoplasmic Reticulum-associated Degradation Due to Protein Misfolding.
M. E. Gelsthorpe, N. Baumann, E. Millard, S. E. Gale, S. J. Langmade, J. E. Schaffer, and D. S. Ory (2008)
J. Biol. Chem. 283, 8229-8236
   Abstract »    Full Text »    PDF »
Energetics of Substrate Binding and Catalysis by Class 1 (Glycosylhydrolase Family 47) {alpha}-Mannosidases Involved in N-Glycan Processing and Endoplasmic Reticulum Quality Control.
K. Karaveg and K. W. Moremen (2005)
J. Biol. Chem. 280, 29837-29848
   Abstract »    Full Text »    PDF »
Degradation of Mutated Bovine Pancreatic Trypsin Inhibitor in the Yeast Vacuole Suggests Post-endoplasmic Reticulum Protein Quality Control.
C. M. Coughlan, J. L. Walker, J. C. Cochran, K. D. Wittrup, and J. L. Brodsky (2004)
J. Biol. Chem. 279, 15289-15297
   Abstract »    Full Text »    PDF »
Elucidation of the molecular logic by which misfolded {alpha}1-antitrypsin is preferentially selected for degradation.
Y. Wu, M. T. Swulius, K. W. Moremen, and R. N. Sifers (2003)
PNAS 100, 8229-8234
   Abstract »    Full Text »    PDF »


To Advertise     Find Products

Science. ISSN 0036-8075 (print), 1095-9203 (online)