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Related Concept Videos

Yeast Signaling01:28

Yeast Signaling

Yeasts are single-celled organisms, but unlike bacteria, they are eukaryotes (cells with a nucleus). Cell signaling in yeast is similar to signaling in other eukaryotic cells. A ligand, such as a protein or a small molecule released from a yeast cell, attaches to a receptor on the cell surface. The binding stimulates second-messenger kinases to activate or inactivate transcription factors that further regulate gene expression. Many of the yeast intracellular signaling cascades have similar...
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Eukaryotic cells use different mechanisms to eliminate toxic waste obsolete and worn-out substances. Lysosomes play a pivotal role in this, and hence, these substances are carried to the lysosome from other parts of the cell and extracellular space through different pathways. The most elaborately studied pathways to the lysosome are the endocytic pathways.
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ER Retrieval Pathway01:45

ER Retrieval Pathway

In the secretory pathway, vesicles transport proteins from one cellular compartment to another in forward transport to deliver the protein to its correct location. Occasionally, misfolded proteins and incorrect proteins escape their original compartments, and a retrieval pathway is used to return the escaped proteins to their original compartment.
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Export of Misfolded Proteins out of the ER01:32

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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...
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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Expression, Purification, and Liposome Binding of Budding Yeast SNX-BAR Heterodimers
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Expression, Purification, and Liposome Binding of Budding Yeast SNX-BAR Heterodimers

Published on: December 6, 2019

A detour for yeast oxysterol binding proteins.

Christopher T Beh1, Christopher R McMaster, Keith G Kozminski

  • 1Department of Molecular Biology and Biochemistry, Simon Fraser University, Burnaby, British Columbia V5A 1S6, Canada. ctbeh@sfu.ca

The Journal of Biological Chemistry
|February 16, 2012
PubMed
Summary

Oxysterol binding protein-related proteins (Osh proteins) may not transfer sterols. Instead, they regulate lipid pathways and membrane organization at cellular contact sites.

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Area of Science:

  • Cell Biology
  • Lipid Metabolism
  • Molecular Biology

Background:

  • Oxysterol binding protein-related proteins (Osh proteins) are involved in sterol transport between cellular membranes.
  • Previous models proposed Osh proteins function as non-vesicular sterol transfer proteins.

Purpose of the Study:

  • To re-evaluate the function of Osh proteins in light of recent research.
  • To propose new models for Osh protein function based on current evidence.

Main Methods:

  • Literature review and synthesis of recent studies on Osh proteins.
  • Development of new conceptual models for Osh protein function.

Main Results:

  • Osh proteins are proposed to be sterol-dependent regulators of phosphoinositide and sphingolipid pathways.
  • Osh proteins coordinate lipid signaling and membrane reorganization.
  • Osh proteins are involved in assembling tethering complexes at membrane contact sites.

Conclusions:

  • Osh proteins may not primarily function as sterol transfer proteins.
  • Osh proteins play a crucial role in regulating lipid signaling and membrane dynamics at membrane contact sites.
  • New models highlight Osh proteins' function in coordinating molecular exchanges at cellular interfaces.