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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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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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Bacterial growth is closely tied to nutrient availability, with cells proliferating exponentially under favorable conditions and entering a stationary phase when resources become scarce. This transition is mediated by a regulatory mechanism known as the stringent response, which allows bacteria to adapt to nutrient deprivation by modulating gene expression and metabolic activity.During nutrient scarcity, intracellular amino acid levels decline. It results in the accumulation of uncharged tRNAs...
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Bacterial protein secretion involves translocation systems to ensure proteins reach their designated locations, including the plasma membrane, periplasm, outer membrane, or the external environment. These translocation systems are vital for bacterial physiology, supporting processes like membrane assembly, enzymatic activity in the periplasm, and interactions with the external environment. The division of labor between Sec and Tat pathways ensures efficiency in handling proteins with diverse...
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Other Stress Responses in Bacteria01:30

Other Stress Responses in Bacteria

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Bacteria have global regulatory systems that control several types of stress mechanisms. These include Pho regulon and the heat shock response, which are essential systems for environmental adaptation, such as nutrient limitation and proteotoxic stress. The Pho regulon and the heat shock response exemplify bacterial resilience, enabling rapid adaptation to fluctuating environmental conditions.Pho RegulonBacteria require phosphorus for essential cellular processes, including nucleic acid...
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Directing Proteins to the Rough Endoplasmic Reticulum01:34

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The organelle-specific signaling sequences direct proteins synthesized in the cytosol to their final destination like ER, mitochondria, peroxisomes, etc. Some of the proteins directed to ER are then trafficked via vesicles to other organelles within the cell or the extracellular environment through the Golgi complex. For example, the rough ER synthesizes soluble proteins for transportation to the lysosomes or secretion out of the cell. It can also synthesize transmembrane proteins that can...
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Effectors Targeting the Unfolded Protein Response during Intracellular Bacterial Infection.

Manal H Alshareef1,2,3, Elizabeth L Hartland1,2, Kathleen McCaffrey1,2

  • 1Centre for Innate Immunity and Infectious Diseases, Hudson Institute of Medical Research, Clayton, VIC 3168, Australia.

Microorganisms
|April 3, 2021
PubMed
Summary
This summary is machine-generated.

The unfolded protein response (UPR) helps cells manage endoplasmic reticulum stress during bacterial infections. However, bacteria can exploit the UPR, impacting host defense, inflammation, and immunity.

Keywords:
ER stressUPRbacteriaeffector proteinsinfectionsecretion systems

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Area of Science:

  • Cellular biology
  • Immunology
  • Microbiology

Background:

  • The unfolded protein response (UPR) is a cellular stress response to endoplasmic reticulum (ER) dysfunction.
  • ER stress is frequently observed during bacterial infections, but the UPR's role in host defense is not fully elucidated.
  • The UPR can either resolve ER stress or trigger apoptosis, influencing infection outcomes.

Purpose of the Study:

  • To explore the dual role of the UPR in host defense against bacterial pathogens.
  • To discuss how bacterial effector proteins manipulate the UPR for their survival and proliferation.
  • To examine the implications of UPR modulation for inflammation and immunity during infection.

Main Methods:

  • Literature review and synthesis of existing research on UPR and bacterial infections.
  • Analysis of mechanisms by which bacteria interact with the UPR.
  • Case study examples of different bacterial pathogens and their UPR manipulation.

Main Results:

  • The UPR plays a complex role in bacterial infections, acting as both a defense mechanism and a target for bacterial exploitation.
  • Bacterial effector proteins can hijack the UPR to promote intracellular survival and replication.
  • UPR activation can lead to apoptosis, limiting bacterial growth but potentially causing host tissue damage.

Conclusions:

  • The UPR's involvement in bacterial infections is multifaceted, with significant implications for host immunity and inflammation.
  • Understanding the interplay between the UPR and bacterial pathogens is crucial for developing new therapeutic strategies.
  • Targeting or modulating the UPR presents potential avenues for controlling bacterial infections and associated pathologies.