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Related Concept Videos

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...
Role of ER in the Secretory Pathway01:17

Role of ER in the Secretory Pathway

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.
Components of the secretory pathway
About a third of proteins synthesized in the cell are sorted via the secretory route. They shuffle between different compartments in membrane-bound vesicles until they reach their final destination. The main intracellular compartments involved...
Post-translational Translocation of Proteins to the RER01:27

Post-translational Translocation of Proteins to the RER

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.
Targeting proteins to the ER
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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...
Directing Proteins to the Rough Endoplasmic Reticulum01:34

Directing Proteins to the Rough Endoplasmic Reticulum

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...
Cotranslational Protein Translocation01:20

Cotranslational Protein Translocation

Translocation of proteins across membranes is an ancient process that occurs even in bacteria and archaebacteria. In fact, the components of the translocation machinery are still conserved between prokaryotes and eukaryotes.
Sec61 channel partners for cotranslational translocation
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TRB3 function in cardiac endoplasmic reticulum stress.

Joan Avery1, Sharon Etzion, Brian J DeBosch

  • 1Center for Cardiovascular Research, Department of Internal Medicine, Washington University School of Medicine, St Louis, MO 63110, USA.

Circulation Research
|April 3, 2010
PubMed
Summary
This summary is machine-generated.

Tribbles (TRB)3 expression increases with endoplasmic reticulum (ER) stress in heart cells. This protein antagonizes cardiac glucose metabolism and survival, impacting heart remodeling and function.

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Area of Science:

  • Cardiovascular Biology
  • Cellular Stress Response
  • Molecular Signaling

Background:

  • Tribbles (TRB)3 is an intracellular pseudokinase regulating signal transduction.
  • TRB3 inhibits Akt protein kinases and its expression is induced by ER stress, hypoxia, and starvation in non-cardiac cells.

Purpose of the Study:

  • To investigate TRB3 expression and function in cardiac myocytes and mouse hearts.
  • To understand the role of TRB3 in cardiac response to ER stress and myocardial infarction.

Main Methods:

  • Examined TRB3 expression in cultured cardiac myocytes and mouse heart tissue.
  • Utilized TRB3 knockdown and cardiac-specific TRB3 overexpression transgenic mouse models.
  • Assessed Akt activation, insulin signaling, cardiac function, metabolism, and apoptosis post-myocardial infarction.

Main Results:

  • ER stress inducers increased TRB3 expression and inhibited insulin-stimulated Akt activation in cardiac myocytes.
  • TRB3 knockdown reversed ER stress effects on insulin signaling.
  • Myocardial infarction elevated TRB3 in the infarct border zone.
  • Transgenic TRB3 mice showed normal contractile function but impaired glucose oxidation and increased susceptibility to infarct expansion and apoptosis.

Conclusions:

  • TRB3 induction is a key component of the cardiac myocyte ER stress response.
  • TRB3 antagonizes cardiac glucose metabolism and cardiac myocyte survival.
  • TRB3 plays a role in pathological cardiac remodeling and response to ischemic injury.