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Related Concept Videos

The Unfolded Protein Response01:37

The Unfolded Protein Response

The ER is the hub of protein synthesis in a cell. It has robust systems to quality control protein folding and also for degradation of terminally misfolded proteins. Under normal conditions, a small proportion of misfolded proteins that cannot be salvaged need to be transported to the cytoplasm by the ER-associated degradation or ERAD pathways. However, if the ERAD cannot handle the misfolded proteins, the cell activates the unfolded protein response or UPR to adjust the protein folding...
Regulation of the Unfolded Protein Response01:31

Regulation of the Unfolded Protein Response

Inositol-requiring kinase one or IRE1 is the most conserved eukaryotic unfolded protein response (UPR) receptor. It is a type I transmembrane protein kinase receptor with a distinctive site-specific RNase activity. As the binding mechanics of the misfolded proteins with the N-terminal domain of IRE-1 are unclear, three binding models — direct, indirect, and allosteric -- are proposed for receptor activation. Nevertheless, it is known that once a misfolded protein associates with IRE1, it...
Protein Folding Quality Check in the RER01:29

Protein Folding Quality Check in the RER

ER is the primary site for the maturation and folding of soluble and transmembrane secretory proteins. The calnexin cycle is a specific chaperone system that folds and assesses the confirmation of N-glycosylated proteins before they can exit the ER lumen. The primary players of this quality check pipeline are the lectins, ER-resident chaperones, and a glucosyl transferase enzyme. In case the calnexin system in the lumen fails to salvage a misfolded protein, it is transported to the cytoplasm...
Export of Misfolded Proteins out of the ER01:32

Export of Misfolded Proteins out of the ER

After folding, the ER assesses the quality of secretory and membrane proteins. The correctly folded proteins are cleared by the calnexin cycle for transport to their final destination, while misfolded proteins are held back in the ER lumen. The ER chaperones attempt to unfold and refold the misfolded proteins but sometimes fail to achieve the correct native conformation. Such terminally misfolded proteins are then exported to the cytosol by ER-associated degradation or ERAD pathway for...
Molecular Chaperones and Protein Folding03:00

Molecular Chaperones and Protein Folding

The native conformation of a protein is formed by interactions between the side chains of its constituent amino acids. When the amino acids cannot form these interactions, the protein cannot fold by itself and needs chaperones. Notably, chaperones do not relay any additional information required for the folding of polypeptides; the native conformation of a protein is determined solely by its amino acid sequence. Chaperones catalyze protein folding without being a part of the folded protein.
The...
Molecular Chaperones and Protein Folding03:00

Molecular Chaperones and Protein Folding

The native conformation of a protein is formed by interactions between the side chains of its constituent amino acids. When the amino acids cannot form these interactions, the protein cannot fold by itself and needs chaperones. Notably, chaperones do not relay any additional information required for the folding of polypeptides; the native conformation of a protein is determined solely by its amino acid sequence. Chaperones catalyze protein folding without being a part of the folded protein.
The...

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Decrease in membrane phospholipid unsaturation induces unfolded protein response.

Hiroyuki Ariyama1, Nozomu Kono, Shinji Matsuda

  • 1Graduate School of Pharmaceutical Sciences, University of Tokyo, Tokyo 113-0033, Japan.

The Journal of Biological Chemistry
|May 22, 2010
PubMed
Summary

Decreased phospholipid unsaturation, induced by stearoyl-CoA desaturase 1 (SCD1) knockdown, triggers the unfolded protein response (UPR) in mammalian cells. This UPR is influenced by saturated and unsaturated fatty acids and LPCAT3 activity.

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Area of Science:

  • Cellular Biology
  • Lipid Metabolism
  • Molecular Biology

Background:

  • Membrane phospholipid fatty acid composition is crucial for cellular functions.
  • Stearoyl-CoA desaturase 1 (SCD1) regulates fatty acid saturation.
  • Cellular responses to altered phospholipid composition are not well understood.

Purpose of the Study:

  • To investigate how mammalian cells respond to changes in phospholipid fatty acid composition.
  • To elucidate the role of SCD1 in cellular stress responses.
  • To identify key enzymes and fatty acids involved in these responses.

Main Methods:

  • SCD1 knockdown in mammalian cells.
  • Analysis of phospholipid fatty acid composition.
  • Measurement of unfolded protein response (UPR) markers (CHOP, GRP78, XBP1 splicing).
  • Assessment of Lysophosphatidylcholine acyltransferase 3 (LPCAT3) expression and function.
  • Fatty acid supplementation studies.

Main Results:

  • SCD1 knockdown increased saturated fatty acids and decreased monounsaturated fatty acids in phospholipids, inducing UPR.
  • UPR was rescued by unsaturated fatty acids and enhanced by saturated fatty acids.
  • LPCAT3 was upregulated in SCD1 knockdown cells and its knockdown synergistically enhanced UPR.
  • Palmitic acid-induced UPR was enhanced by both SCD1 and LPCAT3 knockdown.

Conclusions:

  • A decrease in membrane phospholipid unsaturation induces UPR in mammalian cells.
  • SCD1 plays a critical role in maintaining phospholipid homeostasis and preventing UPR.
  • LPCAT3 activity influences the cellular response to altered phospholipid saturation and UPR induction.