Please use this identifier to cite or link to this item:
Title: Futile protein folding cycles in the ER are terminated by the unfolded protein O-mannosylation pathway
Authors: Xu, C.
Wang, S.
Thibault, G.
Ng, D.T.W. 
Issue Date: 2013
Citation: Xu, C., Wang, S., Thibault, G., Ng, D.T.W. (2013). Futile protein folding cycles in the ER are terminated by the unfolded protein O-mannosylation pathway. Science 340 (6135) : 978-981. ScholarBank@NUS Repository.
Abstract: Newly synthesized polypeptides fold and assemble with assistance from protein chaperones. Full maturation can take multiple attempts, exchanging chaperones at each round. Improperly folded molecules must exit folding cycles and be degraded. In the endoplasmic reticulum (ER), prolonged substrate cycling is detrimental because it expends chaperone and energy resources and increases toxic reactive oxygen species. In budding yeast, we found that unfolded protein O-mannosylation terminated failed folding attempts through the Pmt1/Pmt2 complex. O-mannosylation incapacitated target molecule folding and removed them from folding cycles by reducing engagement with the Kar2 chaperone. In an in vitro protein refolding assay, the modification intrinsically and irreversibly disabled the folding potential of the substrate. Thus, protein folding termination can involve a covalent glycosylation event.
Source Title: Science
ISSN: 00368075
DOI: 10.1126/science.1234055
Appears in Collections:Staff Publications

Show full item record
Files in This Item:
There are no files associated with this item.


checked on Sep 19, 2022


checked on Sep 19, 2022

Page view(s)

checked on Sep 22, 2022

Google ScholarTM



Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.