BAT3 Guides Misfolded Glycoproteins Out of the Endoplasmic Reticulum
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...
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| Format: | Online |
| Language: | English |
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Public Library of Science
2011
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| Online Access: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3234288/ |
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pubmed-3234288 |
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pubmed-32342882011-12-15 BAT3 Guides Misfolded Glycoproteins Out of the Endoplasmic Reticulum Claessen, Jasper H. L. Ploegh, Hidde L. Research Article 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. Public Library of Science 2011-12-08 /pmc/articles/PMC3234288/ /pubmed/22174835 http://dx.doi.org/10.1371/journal.pone.0028542 Text en Claessen, Ploegh. http://creativecommons.org/licenses/by/4.0/ 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 properly credited. |
| repository_type |
Open Access Journal |
| institution_category |
Foreign Institution |
| institution |
US National Center for Biotechnology Information |
| building |
NCBI PubMed |
| collection |
Online Access |
| language |
English |
| format |
Online |
| author |
Claessen, Jasper H. L. Ploegh, Hidde L. |
| spellingShingle |
Claessen, Jasper H. L. Ploegh, Hidde L. BAT3 Guides Misfolded Glycoproteins Out of the Endoplasmic Reticulum |
| author_facet |
Claessen, Jasper H. L. Ploegh, Hidde L. |
| author_sort |
Claessen, Jasper H. L. |
| title |
BAT3 Guides Misfolded Glycoproteins Out of the Endoplasmic Reticulum |
| title_short |
BAT3 Guides Misfolded Glycoproteins Out of the Endoplasmic Reticulum |
| title_full |
BAT3 Guides Misfolded Glycoproteins Out of the Endoplasmic Reticulum |
| title_fullStr |
BAT3 Guides Misfolded Glycoproteins Out of the Endoplasmic Reticulum |
| title_full_unstemmed |
BAT3 Guides Misfolded Glycoproteins Out of the Endoplasmic Reticulum |
| title_sort |
bat3 guides misfolded glycoproteins out of the endoplasmic reticulum |
| description |
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. |
| publisher |
Public Library of Science |
| publishDate |
2011 |
| url |
https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3234288/ |
| _version_ |
1611492907240390656 |