QUICK SEARCH:   [advanced] Author: Keyword(s):
Home     Help     Feedback     Subscriptions     Archive     Search     Table of Contents

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

This Article Figures Only Full Text Full Text (PDF) All Versions of this Article: jcs.00439v1 116/11/2361    most recent Alert me when this article is cited Alert me if a correction is posted Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Palmer, E. A. Articles by McCracken, A. A. Search for Related Content PubMed PubMed Citation Articles by Palmer, E. A. Articles by McCracken, A. A. Social Bookmarking                         What's this?

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

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 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

CiteULike    Complore    Connotea    Del.icio.us    Digg    Reddit    Technorati    Twitter    What's this?

This article has been cited by other articles:

				M. J. Davies, E. Miranda, B. D. Roussel, R. J. Kaufman, S. J. Marciniak, and D. A. Lomas Neuroserpin Polymers Activate NF-{kappa}B by a Calcium Signaling Pathway That Is Independent of the Unfolded Protein Response J. Biol. Chem., July 3, 2009; 284(27): 18202 - 18209. [Abstract] [Full Text] [PDF]

				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]

				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]