Assessing Mitochondrial Unfolded Protein Response in Mammalian Cells

2017 ◽  
pp. 363-378 ◽  
Author(s):  
Fiona Durand ◽  
Nicholas Hoogenraad
Keyword(s):  
Unfolded Protein Response ◽  
Mammalian Cells ◽  
Unfolded Protein ◽  
Protein Response ◽  
Mitochondrial Unfolded Protein Response

scholarly journals ClpX stimulates the mitochondrial unfolded protein response (UPRmt) in mammalian cells

2015 ◽  
Vol 1853 (10) ◽  
pp. 2580-2591 ◽  
Author(s):  
Natalie Al-Furoukh ◽  
Alessandro Ianni ◽  
Hendrik Nolte ◽  
Soraya Hölper ◽  
Marcus Krüger ◽  
...  
Keyword(s):  
Unfolded Protein Response ◽  
Mammalian Cells ◽  
Unfolded Protein ◽  
Protein Response ◽  
Mitochondrial Unfolded Protein Response

scholarly journals At the heart of mitochondrial quality control: many roads to the top

2021 ◽  
Author(s):  
Roberta A. Gottlieb ◽  
Honit Piplani ◽  
Jon Sin ◽  
Savannah Sawaged ◽  
Syed M. Hamid ◽  
...  
Keyword(s):  
Quality Control ◽  
Unfolded Protein Response ◽  
Mitochondrial Biogenesis ◽  
Mitochondrial Dynamics ◽  
Mitochondrial Quality Control ◽  
Unfolded Protein ◽  
Selective Elimination ◽  
Protein Response ◽  
Mitochondrial Unfolded Protein Response

AbstractMitochondrial quality control depends upon selective elimination of damaged mitochondria, replacement by mitochondrial biogenesis, redistribution of mitochondrial components across the network by fusion, and segregation of damaged mitochondria by fission prior to mitophagy. In this review, we focus on mitochondrial dynamics (fusion/fission), mitophagy, and other mechanisms supporting mitochondrial quality control including maintenance of mtDNA and the mitochondrial unfolded protein response, particularly in the context of the heart.

scholarly journals The Mitochondrial Unfolded Protein Response Is Mediated Cell-Non-autonomously by Retromer-Dependent Wnt Signaling

Cell ◽  
2018 ◽  
Vol 174 (4) ◽  
pp. 870-883.e17 ◽  
Author(s):  
Qian Zhang ◽  
Xueying Wu ◽  
Peng Chen ◽  
Limeng Liu ◽  
Nan Xin ◽  
...  
Keyword(s):  
Wnt Signaling ◽  
Unfolded Protein Response ◽  
Unfolded Protein ◽  
Protein Response ◽  
Mitochondrial Unfolded Protein Response

Alterations in an IRE1-RNA complex in the mammalian unfolded protein response

2001 ◽  
Vol 114 (17) ◽  
pp. 3207-3212
Author(s):  
Anne Bertolotti ◽  
David Ron
Keyword(s):  
Unfolded Protein Response ◽  
Mammalian Cells ◽  
Dynamic Change ◽  
Rna Molecules ◽  
Unfolded Protein ◽  
Rna Fragments ◽  
Stressed Cells ◽  
Rna Complex ◽  
Protein Response

IRE1 proteins mediate cellular responses to accumulation of malfolded proteins in the endoplasmic reticulum in the yeast and mammalian unfolded protein responses. A sensitive in vivo u.v. crosslinking assay showed that IRE1 proteins are intimately associated with RNA in mammalian cells. The IRE1-associated RNA fragments recovered by this assay were different in stressed and unstressed cells. The amount of RNA associated with IRE1 that could be revealed by end-labeling with T4 kinase was greater in IRE1-containing complexes isolated from stressed cells. Furthermore, the RNA fragments recovered from complexes found in stressed cells were shorter than those from unstressed cells, revealing a dynamic change in the IRE1-RNA complex during the UPR. Formation of the complex between IRE1 and RNA was dependent on both the kinase and endonuclease domains of IRE1, and involved pre-existing RNA species. When viewed in the context of the known importance of Ire1p-HAC1 mRNA interactions to the yeast unfolded protein response, these findings suggest that full-length mammalian IRE1s also engage RNA molecules as downstream effectors.

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