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Related Concept Videos

Role of ER in the Secretory Pathway01:17

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Eukaryotic cells have a special pathway that enables communication between various intracellular membrane-bound compartments and also with the extracellular environment. This pathway is termed as the secretory pathway.
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The mammalian target of rapamycin or mTOR protein was discovered in 1994 due to its direct interaction with rapamycin. The protein gets its name from a yeast homolog called TOR. The mTOR protein complex in mammalian cells plays a major role in balancing anabolic processes such as the synthesis of proteins, lipids, and nucleotides and catabolic processes, such as autophagy in response to environmental cues, such as availability of nutrients and growth factors.
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Smooth Endoplasmic Reticulum01:21

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Smooth endoplasmic reticulum or smooth ER is a sub-organelle with specialized functions in animal cells and plant cells. It is often associated with the tubule morphology of the endoplasmic reticulum.
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Endoplasmic Reticulum01:39

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The Endoplasmic Reticulum (ER) in eukaryotic cells is a substantial network of interconnected membranes with diverse functions, from calcium storage to biomolecule synthesis. A primary component of the endomembrane system, the ER manufactures phospholipids critical for membrane function throughout the cell. Additionally, the two distinct regions of the ER specialize in the manufacture of specific lipids and proteins.
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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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A sizable fraction of proteins destined for ER are first synthesized in the cell cytosol and then transported across the ER membrane–a process called post-translational translocation. Similar to cotranslationally translocated proteins, these proteins also use the Sec translocon complex to enter the ER lumen.
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Endoplasmic reticulum stress in malignancy.

Hanna J Clarke1, Joseph E Chambers1, Elizabeth Liniker1

  • 1Department of Medicine, Cambridge Institute for Medical Research (CIMR), Wellcome Trust/MRC Building, University of Cambridge, Hills Road, Cambridge CB2 0XY, UK.

Cancer Cell
|May 15, 2014
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Summary
This summary is machine-generated.

Malignant cells are susceptible to protein misfolding due to nutrient issues and protein synthesis problems. This leads to endoplasmic reticulum stress, impacting cancer cell growth and survival, and offering potential new therapeutic targets.

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Area of Science:

  • Oncology
  • Cell Biology
  • Biochemistry

Background:

  • Malignant cells exhibit unique metabolic and protein synthesis characteristics.
  • Nutrient deprivation and protein synthesis dysregulation contribute to cellular stress in cancer.

Purpose of the Study:

  • To review the role of endoplasmic reticulum (ER) stress in cancer pathology.
  • To explore ER dysfunction as a potential therapeutic target in oncology.

Main Methods:

  • Literature review of studies on ER stress and cancer.
  • Analysis of evidence linking ER dysfunction to cancer cell proliferation and survival.

Main Results:

  • Protein misfolding is common in cancer cells, leading to ER stress.
  • ER stress significantly influences cancer cell proliferation and survival.
  • ER dysfunction is implicated in the pathology of various cancers.

Conclusions:

  • Endoplasmic reticulum stress is a key factor in cancer development and progression.
  • Targeting ER dysfunction presents a promising strategy for novel cancer therapies.