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Degradation of a cytosolic protein requires endoplasmic reticulum-associated degradation machinery.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Dancy, Beverley M. Michaelis, Susan Maurer, Matthew J. Metzger, Meredith Boyle
Description	Author Affiliation: Metzger MB ( Department of Cell Biology, The Johns Hopkins University School of Medicine, Baltimore, Maryland 21205, USA.)
Abstract	Protein misfolding is monitored by a variety of cellular 'quality control' systems. Endoplasmic reticulum (ER) quality control handles misfolded secretory and membrane proteins and is well characterized. However, less is known about the quality control of misfolded cytosolic proteins (CytoQC). To study CytoQC, we have employed a genetic system in Saccharomyces cerevisiae using a transplantable degron, CL1 (1). Attachment of CL1 to the cytosolic protein Ura3p destabilizes Ura3p, targeting it for rapid proteasomal degradation. We have performed a comprehensive analysis of Ura3p-CL1 degradation requirements. As shown previously, we observe that the ER-localized ubiquitin E2 (Ubc6p, Ubc7p, and Cue1p) and E3 (Doa10p) machinery involved in ER-associated degradation (ERAD) are also responsible for the degradation of the cytosolic substrate Ura3p-CL1. Importantly, we find that the cytosol/ER membrane-localized chaperones Ydj1p and Ssa1p, known to be necessary for the ERAD of membrane proteins with misfolded cytosolic domains, are also required for the ubiquitination and degradation of Ura3p-CL1. In addition, we show a role for the Cdc48p-Npl4p-Ufd1p complex in the degradation of Ura3p-CL1. When ubiquitination is blocked, a portion of Ura3p-CL1 is ER membrane-localized. Furthermore, access to the cytosolic face of the ER is required for the degradation of CL1 degron-containing proteins. The ER is distributed throughout the cytosol, and our data, together with previous studies, suggest that the cytosolic face of the ER membrane serves as a 'platform' for the degradation of Ura3p-CL1, which may also be the case for other CytoQC substrates.
ISSN	00219258
e-ISSN	1083351X
Journal	Journal of Biological Chemistry
Issue Number	47
Volume Number	283
Language	English
Publisher	American Society for Biochemistry and Molecular Biology (United States)
Publisher Date	2008-11-21
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Cytosol Metabolism Endoplasmic Reticulum Fungal Proteins Physiology Gene Expression Regulation, Fungal Saccharomyces Cerevisiae Adenosine Triphosphatases Carrier Proteins HSP40 Heat-Shock Proteins HSP70 Heat-Shock Proteins Membrane Proteins Models, Biological Molecular Chaperones Plasmids Proteasome Endopeptidase Complex Saccharomyces Cerevisiae Proteins Solubility Ubiquitin-Conjugating Enzymes Research Support, N.I.H., Extramural Biochemistry Molecular Biology
Content Type	Text
Resource Type	Article
Subject	Cell Biology Biochemistry Molecular Biology

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