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Unfolded Protein Response-Dependent Communication and Contact among Endoplasmic Reticulum, Mitochondria, and Plasma Membrane

1
Department of Stress Protein Processing, Institute of Biomedical & Health Sciences, Hiroshima University, 1-2-3 Kasumi, Minami-ku, Hiroshima 734-8553, Japan
2
Department of Biochemistry, Institute of Biomedical & Health Sciences, Hiroshima University, 1-2-3 Kasumi, Minami-ku, Hiroshima 734-8553, Japan
*
Author to whom correspondence should be addressed.
Int. J. Mol. Sci. 2018, 19(10), 3215; https://doi.org/10.3390/ijms19103215
Received: 28 September 2018 / Revised: 10 October 2018 / Accepted: 13 October 2018 / Published: 18 October 2018
(This article belongs to the Special Issue Endoplasmic Reticulum Stress and Unfolded Protein Response)
The function of the endoplasmic reticulum (ER) can be impaired by changes to the extra- and intracellular environment, such as disruption of calcium homeostasis, expression of mutated proteins, and oxidative stress. In response to disruptions to ER homeostasis, eukaryotic cells activate canonical branches of signal transduction cascades, collectively termed the unfolded protein response (UPR). The UPR functions to remove or recover the activity of misfolded proteins that accumulated in the ER and to avoid irreversible cellular damage. Additionally, the UPR plays unique physiological roles in the regulation of diverse cellular events, including cell differentiation and development and lipid biosynthesis. Recent studies have shown that these important cellular events are also regulated by contact and communication among organelles. These reports suggest strong involvement among the UPR, organelle communication, and regulation of cellular homeostasis. However, the precise mechanisms for the formation of contact sites and the regulation of ER dynamics by the UPR remain unresolved. In this review, we summarize the current understanding of how the UPR regulates morphological changes to the ER and the formation of contact sites between the ER and other organelles. We also review how UPR-dependent connections between the ER and other organelles affect cellular and physiological functions. View Full-Text
Keywords: unfolded protein response; ER morphology; mitochondria-associated ER membrane; ER-PM contact sites unfolded protein response; ER morphology; mitochondria-associated ER membrane; ER-PM contact sites
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MDPI and ACS Style

Saito, A.; Imaizumi, K. Unfolded Protein Response-Dependent Communication and Contact among Endoplasmic Reticulum, Mitochondria, and Plasma Membrane. Int. J. Mol. Sci. 2018, 19, 3215. https://doi.org/10.3390/ijms19103215

AMA Style

Saito A, Imaizumi K. Unfolded Protein Response-Dependent Communication and Contact among Endoplasmic Reticulum, Mitochondria, and Plasma Membrane. International Journal of Molecular Sciences. 2018; 19(10):3215. https://doi.org/10.3390/ijms19103215

Chicago/Turabian Style

Saito, Atsushi, and Kazunori Imaizumi. 2018. "Unfolded Protein Response-Dependent Communication and Contact among Endoplasmic Reticulum, Mitochondria, and Plasma Membrane" International Journal of Molecular Sciences 19, no. 10: 3215. https://doi.org/10.3390/ijms19103215

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