Please use this identifier to cite or link to this item: https://doi.org/10.1126/science.1234055
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. https://doi.org/10.1126/science.1234055
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
URI: http://scholarbank.nus.edu.sg/handle/10635/128885
ISSN: 00368075
DOI: 10.1126/science.1234055
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