spacer gif spacer gif spacer gif spacer gif spacer gif
 QUICK SEARCH:   [advanced]


spacer gif
     Home     Help     Feedback     Subscriptions     Archive     Search     Table of Contents    

First published online 23 April 2003
doi: 10.1242/jcs.00439


This Article
Right arrow Figures Only
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow All Versions of this Article:
jcs.00439v1
116/11/2361    most recent
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Palmer, E. A.
Right arrow Articles by McCracken, A. A.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Palmer, E. A.
Right arrow Articles by McCracken, A. A.
Journal of Cell Science 116, 2361-2373 (2003)
doi: 10.1242/jcs.00439


Research Article

Differential requirements of novel A1PiZ degradation deficient (ADD) genes in ER-associated protein degradation

Elizabeth A. Palmer1, Kristina B. Kruse1, Sheara W. Fewell2, Sean M. Buchanan2, Jeffrey L. Brodsky2 and Ardythe A. McCracken1,*

1 Biology Department, University of Nevada, Reno, NV 89557, USA
2 Department of Biological Sciences, University of Pittsburgh, Pittsburgh, PA 15260, USA

* Author for correspondence (e-mail: mccracke{at}unr.edu)

Accepted 24 February 2003

In the eukaryotic cell, a protein quality control process termed endoplasmic reticulum-associated degradation (ERAD) rids the ER of aberrant proteins and unassembled components of protein complexes that fail to reach a transport-competent state. To identify novel genes required for ERAD, we devised a rapid immunoassay to screen yeast lacking uncharacterized open reading frames that were known targets of the unfolded protein response (UPR), a cellular response that is induced when aberrant proteins accumulate in the ER. Six genes required for the efficient degradation of the Z variant of the {alpha}1-proteinase inhibitor (A1PiZ), a known substrate for ERAD, were identified, and analysis of other ERAD substrates in the six A1PiZ-degradation-deficient (add) mutants suggested diverse requirements for the Add proteins in ERAD. Finally, we report on bioinformatic analyses of the new Add proteins, which will lead to testable models to elucidate their activities.

Key words: ERAD, Protein quality control, Degradation




This article has been cited by other articles:


Home page
Mol. Biol. CellHome page
C. M. Scott, K. B. Kruse, B. Z. Schmidt, D. H. Perlmutter, A. A. McCracken, and J. L. Brodsky
ADD66, a Gene Involved in the Endoplasmic Reticulum-associated Degradation of {alpha}-1-Antitrypsin-Z in Yeast, Facilitates Proteasome Activity and Assembly
Mol. Biol. Cell, October 1, 2007; 18(10): 3776 - 3787.
[Abstract] [Full Text] [PDF]


Home page
Mol. Biol. CellHome page
K. B. Kruse, J. L. Brodsky, and A. A. McCracken
Characterization of an ERAD Gene as VPS30/ATG6 Reveals Two Alternative and Functionally Distinct Protein Quality Control Pathways: One for Soluble Z Variant of Human {alpha}-1 Proteinase Inhibitor (A1PiZ) and Another for Aggregates of A1PiZ
Mol. Biol. Cell, January 1, 2006; 17(1): 203 - 212.
[Abstract] [Full Text] [PDF]




© The Company of Biologists Ltd 2003