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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...
Immunoglobulin-like Cell Adhesion Molecules01:31

Immunoglobulin-like Cell Adhesion Molecules

Immunoglobulin-like cell adhesion molecules or Ig-CAMs are a versatile group of cell surface glycoproteins belonging to the immunoglobulin protein superfamily. Ig-CAMs possess the characteristic immunoglobulin protein domains and other domains such as the fibronectin type III domain. The Ig domains are glycosylated to varying degrees in different Ig-CAMs.
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Integral membrane proteins are proteins adhered to the lipid bilayer of a cell organelle or membrane. They can be of two types: transmembrane integral proteins that span the lipid bilayer and monotopic proteins that are attached to either side of the membrane but do not pass through it.
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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...
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...
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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...

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The irre cell recognition module (IRM) proteins.

Karl-Friedrich Fischbach1, Gerit Arne Linneweber, Till Felix Malte Andlauer

  • 1Department of Neurobiology, Institute for Biology III, Faculty of Biology, Albert-Ludwigs-University Freiburg, Germany. kff@uni-freiburg.de

Journal of Neurogenetics
|January 10, 2009
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Summary

The irre cell recognition module (IRM) proteins in Drosophila are crucial for cell interactions like axonal pathfinding and myoblast fusion. Understanding IRM function reveals how complex neural networks form.

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Area of Science:

  • Developmental neurobiology
  • Cellular and molecular biology
  • Genetics and genomics

Background:

  • Establishing precise neural connections requires understanding cell recognition events.
  • The immunoglobulin superfamily contains conserved proteins vital for cell interactions.
  • Drosophila serves as a model organism to study these fundamental biological processes.

Purpose of the Study:

  • To review the pleiotropic functions of the irre cell recognition module (IRM) proteins.
  • To highlight the role of IRM proteins in various cell recognition events.
  • To elucidate the contribution of IRM proteins to neural network formation.

Main Methods:

  • Review of existing scientific literature on IRM proteins in Drosophila.
  • Analysis of studies detailing the functions of IrreC/Rst, Kirre, SNS, and Hbs proteins.
  • Synthesis of evidence from diverse cellular interaction contexts.

Main Results:

  • IRM proteins, including IrreC/Rst, Kirre, SNS, and Hbs, are involved in multiple cell recognition events.
  • These proteins mediate myoblast fusion, cell sorting, axonal pathfinding, and target recognition in Drosophila.
  • IRM proteins function as a cohesive module in diverse cellular interactions.

Conclusions:

  • IRM proteins play essential, multifaceted roles in Drosophila development.
  • Understanding IRM function is key to deciphering the rules governing neural network assembly.
  • Further research into IRM proteins can illuminate broader principles of cell recognition.