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Related Concept Videos

The Unfolded Protein Response01:37

The Unfolded Protein Response

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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...
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Regulation of the Unfolded Protein Response01:31

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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...
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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.
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Intrinsically Disordered Proteins02:18

Intrinsically Disordered Proteins

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Intrinsically disordered proteins are a group of proteins that do not fold into specific three-dimensional structures. Their structural flexibility allows them to complement ordered proteins to perform functions that are inaccessible to rigid structures. They are more common in eukaryotes than prokaryotes and may either be exclusively intrinsically disordered or hybrid proteins, consisting of a mix of ordered and disordered regions. The absence of a rigid structure in these proteins can be...
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Responses to Heat and Cold Stress02:45

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Every organism has an optimum temperature range within which healthy growth and physiological functioning can occur. At the ends of this range, there will be a minimum and maximum temperature that interrupt biological processes.
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Studying Triple Negative Breast Cancer Using Orthotopic Breast Cancer Model
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The Unfolded Protein Response in Breast Cancer.

Eoghan P McGrath1,2, Susan E Logue3,4, Katarzyna Mnich5,6

  • 1Apoptosis Research Centre, National University of Ireland (NUI), Galway, University Road, Galway, H91 TK33 Galway, Ireland. E.MCGRATH14@nuigalway.ie.

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Summary

New breast cancer treatments targeting the unfolded protein response (UPR) show promise. UPR signaling in breast cancer promotes malignancy and therapy resistance, suggesting UPR as a therapeutic target.

Keywords:
autophagybreast cancercell deathendoplasmic reticulum (ER) stresstherapyunfolded protein response (UPR)

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Area of Science:

  • Oncology
  • Molecular Biology
  • Cellular Biology

Background:

  • Breast cancer is a leading cause of death, with significant challenges including therapy resistance and lack of therapeutic targets.
  • The unfolded protein response (UPR) is a cellular stress pathway crucial for maintaining endoplasmic reticulum (ER) homeostasis.
  • UPR signaling plays diverse roles in physiology and disease, including promoting cancer progression.

Purpose of the Study:

  • To review the multifaceted roles of UPR signaling in breast cancer.
  • To highlight the contribution of UPR to therapy resistance in breast cancer.
  • To explore the potential of targeting UPR pathways for novel breast cancer treatments.

Main Methods:

  • Literature review of studies investigating UPR signaling in breast cancer.
  • Analysis of UPR's role in promoting malignant phenotypes.
  • Examination of UPR's involvement in acquired or intrinsic therapy resistance.

Main Results:

  • UPR signaling is activated in breast cancer and promotes a malignant phenotype.
  • UPR activation confers resistance to various established breast cancer therapies.
  • Dysregulation of UPR pathways is a common feature in breast cancer.

Conclusions:

  • Targeting the unfolded protein response (UPR) presents a promising therapeutic strategy for breast cancer.
  • UPR inhibition, alone or in combination with existing treatments, may overcome therapy resistance.
  • Further research into UPR-mediated mechanisms is crucial for developing effective breast cancer therapies.