BAT3 Guides Misfolded Glycoproteins Out of the Endoplasmic Reticulum
Author(s)Ploegh, Hidde; Claessen, Jasper H. L.
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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.
DepartmentMassachusetts Institute of Technology. Department of Biology; Whitehead Institute for Biomedical Research
Public Library of Science
Claessen, Jasper H. L., and Hidde L. Ploegh. “BAT3 Guides Misfolded Glycoproteins Out of the Endoplasmic Reticulum.” Ed. Emanuele Buratti. PLoS ONE 6.12 (2011): e28542. Web. 8 Feb. 2012.
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