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BAT 3 Guides Misfolded Glycoproteins Out of the Endoplasmic Reticulum Citation Claessen

Secretory and membrane proteins that fail to acquire their native conformation within the lumen of the Endoplasmic Reticulum (ER) are usually targeted for ubiquitin-dependent degradation by the proteasome. How partially folded polypeptides are kept from aggregation once ejected from the ER into the cytosol is not known. We show that BAT3, a cytosolic chaperone, is recruited to the site of dislocation through its interaction with Derlin2. Furthermore, we observe cytoplasmic BAT3 in a complex with a polypeptide that originates in the ER as a glycoprotein, an interaction that depends on the cytosolic disposition of both, visualized even in the absence of proteasomal inhibition. Cells depleted of BAT3 fail to degrade an established dislocation substrate. We thus implicate a cytosolic chaperone as an active participant in the dislocation of ER glycoproteins. Citation: Claessen JHL, Ploegh HL (2011) BAT3 Guides Misfolded Glycoproteins Out of the Endoplasmic Reticulum. PLoS ONE 6(12): e28542. doi:10.1371/ journal.pone.0028542 Editor: Emanuele Buratti, International Centre for Genetic Engineering and Biotechnology, Italy Received July 21, 2011; Accepted November 10, 2011; Published December 8, 2011 Copyright: 2011 Claessen, Ploegh. This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited. Funding: This work was supported by a research grant from the National Institutes of Health and a fellowship from the Boehringer Ingelheim Fonds to JHLC. The funders had no role in study design, data collection and analysis, decision to publish, or preparation of the manuscript. Competing Interests: The authors have declared that no competing interests exist. * E-mail: ploegh@wi.mit.edu