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Eukaryotic Cell, February 2009, p. 133, Vol. 8, No. 2
1535-9778/09/$08.00+0     doi:10.1128/EC.00397-08
Copyright © 2009, American Society for Microbiology. All Rights Reserved.

SPOTLIGHT

Articles of Significant Interest Selected from This Issue by the Editors

Eukaryotic Cell Inaugurates a New Section of the Journal

Every author appreciates being noticed, and each of us appreciates it when a colleague brings to our attention a piece of work that displays particular novelty or is in some other way truly a cut above.

With increasing frequency, the editors of Eukaryotic Cell (EC) have noted and brought attention to articles of special quality. These, they note, would be of particular interest to many of our readers, but they might be missed in the ever more hectic world in which we work. To address this, and as a means of bringing more attention to the excellent articles published in EC, we are initiating a new section of the journal, Spotlight.

Beginning with this issue, the editors will select one or more articles of special note and these will be listed in the Spotlight section at the front of each issue. Each Spotlight page will be jointly composed by the article's corresponding author and the editor who handled the article. It will include a short descriptive title followed by a one-paragraph account of the work that highlights the source of its novelty and/or significance. An embedded link will instantly take readers to the referenced title and abstract within the journal.

We look forward to inaugurating this special section as an additional way of advancing the science and the scientists behind the work we publish. We look forward to your participation in the process.

The EC Editors

Aberrant N Glycosylation and Glycoprotein Folding Quality Control System of Trypanosoma brucei

N glycosylation is the key to quality control and glycoprotein folding in the endoplasmic reticulum (ER) and ER-associated degradation of misfolded proteins. The Trypanosoma brucei N glycosylation pathway deviates from that described in higher eukaryotes and presents unique features that could be therapeutically exploitable. Izquierdo et al. (p. 230-240) show that T. brucei UDP-glucose:glycoprotein glucosyltransferase, the ER protein-folding sensor, presents an unusually wide substrate specificity and high efficiency in vivo and is essential for parasite survival under stress. The results suggest that T. brucei lacks a classical unfolded protein response and instead has an unregulated and constitutively active ER protein folding system.

Eukaryotic Cell, February 2009, p. 133, Vol. 8, No. 2
1535-9778/09/$08.00+0     doi:10.1128/EC.00397-08
Copyright © 2009, American Society for Microbiology. All Rights Reserved.




This Article
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