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- W2487788434 abstract "Publisher Summary Secreted proteins and proteins that reside on the cell surface or within the secretory pathway begin their maturation process in the endoplasmic reticulum (ER). The ER serves as a master regulator for the complex and error prone process of protein maturation, quality control, and trafficking. Furthermore, the ER must match its capacity for protein processing with the cell's dynamic need for protein synthesis, dictated by developmental and environmental cues. The ER regulates its own protein processing capacity through an inter-organelle signaling pathway termed the unfolded protein response (UPR). This chapter highlights some of the most recently discovered roles for the UPR in normal cell physiology. Physiological studies have begun to reveal that the specific nature of the UPR's activation can be quite different for different cell types, and that the pathway's function can range from stress response to general housekeeping. During physiological instances of its activation, the UPR can be modulated on several different levels to achieve results that are fine-tuned to specific cellular contexts. Furthermore, in many physiological cases, each UPR signaling branch appears to be tuned separately. Certain physiological instances of UPR activation confirm the pathway's role as a stress response pathway that becomes active when it senses high levels of unfolded proteins in the ER. The housekeeping role of the UPR, though subtle, may be a key aspect of the UPR's physiological function. In fact, other signal transduction pathways might also serve housekeeping functions that have been overlooked due to subtle activation levels." @default.
- W2487788434 created "2016-08-23" @default.
- W2487788434 creator A5030069081 @default.
- W2487788434 creator A5069025755 @default.
- W2487788434 date "2010-01-01" @default.
- W2487788434 modified "2023-09-27" @default.
- W2487788434 title "Regulating Endoplasmic Reticulum Function through the Unfolded Protein Response" @default.
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