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- W2184728668 abstract ", or bakers’ yeast, are utilized in the biotechnology industry to express, fold, and assemble foreign protein therapeutics [1]. Simply modifying yeast to express high levels of heterologous protein does not necessarily maximize production and secretion, as this action triggers the Unfolded Protein Response (UPR), which eliminates quantities of desired protein through promoted ER-Associated Degradation (ERAD). The yeast UPR may even retard transcription and/or translation of the desired protein, thus decreasing yields. Consequently, a combined approach of mathematical modeling and experiments has been employed in an attempt to obtain a thorough understanding of the yeast UPR, which will be utilized to forward engineer the system to maximize foreign protein therapeutic production. The yeast UPR has been traditionally modeled as the negative feedback loop shown in Figure 1 in which low levels of the chaperone BiP (Binding Protein) relative to unfolded protein (UP) in the ER signal the need for increased production of UPR component proteins--including BiP--that help cells cope with these high ER UP levels. The UPR signal is transduced from the ER to the nucleus and cytoplasm by the ER membrane-spanning endonuclease Ire1p, which enhances translation of Hac1p, a transcription factor that upregulates BiP and other UPR-related gene expression. Traditional modeling identifies BiP as the primary regulator of Ire1p: BiP typically binds Ire1p but is sequestered exclusively by UP when UP is in excess; unbound Ire1p is then free to dimerize," @default.
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- W2184728668 date "2006-01-01" @default.
- W2184728668 modified "2023-09-27" @default.
- W2184728668 title "Modeling Ire1p Regulation and Activation in the Yeast UPR" @default.
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