The Chaperone BAG6 Captures Dislocated Glycoproteins in the Cytosol
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Claessen-2014-The Chaperone BAG6 C.pdf
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Author(s)
Claessen, Jasper H. L.
Sanyal, Sumana
Ploegh, Hidde
Date Issued
March 2014
Journal
PLoS ONE
Publisher
Public Library of Science
Citation
Claessen, Jasper H. L., Sumana Sanyal, and Hidde L Ploegh. “The Chaperone BAG6 Captures Dislocated Glycoproteins in the Cytosol.” Edited by F. Gisou van der Goot. PLoS ONE 9, no. 3 (March 3, 2014): e90204.
Version
Final published version
Abstract
Secretory and membrane (glyco)proteins are subject to quality control in the endoplasmic reticulum (ER) to ensure that only functional proteins reach their destination. Proteins deemed terminally misfolded and hence functionally defective may be dislocated to the cytosol, where the proteasome degrades them. What we know about this process stems mostly from overexpression of tagged misfolded proteins, or from situations where viruses have hijacked the quality control machinery to their advantage. We know of only very few endogenous substrates of ER quality control, most of which are degraded as part of a signaling pathway, such as Insig-1, but such examples do not necessarily represent terminally misfolded proteins. Here we show that endogenous dislocation clients are captured specifically in association with the cytosolic chaperone BAG6, or retrieved en masse via their glycan handle.
MIT Department
Massachusetts Institute of Technology. Department of Biology
Whitehead Institute for Biomedical Research
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DOI of Published Version
https://doi.org/10.1371/journal.pone.0090204
