Glycoprotein Maturation and the UPR [PDF]
, 2011 Glycosylation is a complex form of protein modification occurring in the secretory pathway. The addition of N- and O-glycans affects intracellular processes like the folding and trafficking of most glycoproteins. To better understand the impact of glycosylation in protein folding and maturation, parameters like glycosylation site occupancy and ...
Hülsmeier, A J, Welti, M, Hennet, T
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ER stress in antigen‐presenting cells promotes NKT cell activation through endogenous neutral lipids [PDF]
, 2020 CD1d-restricted invariant natural killer T (iNKT) cells constitute a common glycolipid-reactive innate-like T-cell subset with a broad impact on innate and adaptive immunity.
Cheng, Tan‐Yun +12 more
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ER Stress-Induced eIF2-alpha Phosphorylation Underlies Sensitivity of Striatal Neurons to Pathogenic Huntingtin [PDF]
, 2013 A hallmark of Huntington's disease is the pronounced sensitivity of striatal neurons to polyglutamine-expanded huntingtin expression. Here we show that cultured striatal cells and murine brain striatum have remarkably low levels of phosphorylation of ...
Ashery, U. +6 more
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Mitochondrial retrograde signaling to the endoplasmic-reticulum regulates unfolded protein responses
Molecular & Cellular Oncology, 2019 Unfolded protein response (UPRs) directs adaption or apoptosis depending on the severity of endoplasmic-reticulum (ER) stress. We found that apoptotic signaling by inositol requiring enzyme 1α (IRE1α), a transducer of UPRs, is suppressed by mitochondrial
Keisuke Takeda, Shigeru Yanagi
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Endoplasmic reticulum stress-induced PCD and caspase-like activities involved.
Frontiers in Plant Science, 2014 Plant cells, like cells from other kingdoms, have the ability to self-destruct in a genetically controlled manner. This process is defined as Programmed Cell Death (PCD).
Yao-min eCAI, Jia eYU, Patrick eGALLOIS
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Redox controls UPR to control redox [PDF]
Journal of Cell Science, 2014 In many physiological contexts, intracellular reduction–oxidation (redox) conditions and the unfolded protein response (UPR) are important for the control of cell life and death decisions. UPR is triggered by the disruption of endoplasmic reticulum (ER) homeostasis, also known as ER stress. Depending on the duration and severity of the disruption, this
Davide, Eletto +3 more
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BLISTER-regulated vegetative growth is dependent on the protein kinase domain of ER stress modulator IRE1A in Arabidopsis thaliana [PDF]
, 2019 The unfolded protein response (UPR) is required for protein homeostasis in the endoplasmic reticulum (ER) when plants are challenged by adverse environmental conditions.
Hong, Zheng-Hui +4 more
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A Whole-Genome RNA Interference Screen Reveals a Role for Spry2 in Insulin Transcription and the Unfolded Protein Response. [PDF]
, 2017 Insulin production by the pancreatic β-cell is required for normal glucose homeostasis. While key transcription factors that bind to the insulin promoter are known, relatively little is known about the upstream regulators of insulin transcription.
Ang, Kenny +12 more
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IRE1β negatively regulates IRE1α signaling in response to endoplasmic reticulum stress [PDF]
, 2020 IRE1β is an ER stress sensor uniquely expressed in epithelial cells lining mucosal surfaces. Here, we show that intestinal epithelial cells expressing IRE1β have an attenuated unfolded protein response to ER stress.
Acosta-Alvear +54 more
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Molecular mechanisms involved in endoplasmic reticulum stress development: What do we know today [PDF]
Medicinski PodmladakEndoplasmic reticulum (ER) is an intracellular organelle involved in protein synthesis and folding. When the balance between cell needs for proteins and ER capacity to fold proteins is disrupted, nonfunctional, unfolded, or misfolded proteins accumulate ...
Vidičević-Novaković Sašenka +1 more
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