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- W3048757087 startingPage "e1008654" @default.
- W3048757087 abstract "Newly-translated glycoproteins in the endoplasmic reticulum (ER) often undergo cycles of chaperone binding and release in order to assist in folding. Quality control is required to distinguish between proteins that have completed native folding, those that have yet to fold, and those that have misfolded. Using quantitative modeling, we explore how the design of the quality-control pathway modulates its efficiency. Our results show that an energy-consuming cyclic quality-control process, similar to the observed physiological system, outperforms alternative designs. The kinetic parameters that optimize the performance of this system drastically change with protein production levels, while remaining relatively insensitive to the protein folding rate. Adjusting only the degradation rate, while fixing other parameters, allows the pathway to adapt across a range of protein production levels, aligning with in vivo measurements that implicate the release of degradation-associated enzymes as a rapid-response system for perturbations in protein homeostasis. The quantitative models developed here elucidate design principles for effective glycoprotein quality control in the ER, improving our mechanistic understanding of a system crucial to maintaining cellular health." @default.
- W3048757087 created "2020-08-18" @default.
- W3048757087 creator A5027746139 @default.
- W3048757087 creator A5048469544 @default.
- W3048757087 date "2021-02-01" @default.
- W3048757087 modified "2023-10-16" @default.
- W3048757087 title "Design principles for the glycoprotein quality control pathway" @default.
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- W3048757087 doi "https://doi.org/10.1371/journal.pcbi.1008654" @default.
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- W3048757087 hasPublicationYear "2021" @default.
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