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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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Rab Proteins01:14

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Rab proteins constitute the largest family of monomeric GTPases, of which 70 members are present in humans. Rab proteins and their effectors regulate consecutive stages of vesicle transport such as vesicle transport, docking, and fusion to the correct recipient membrane.
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Ras and Rho are small monomeric GTPases that act downstream of receptor tyrosine kinase (RTK) and regulate various cellular processes. These GTPases switch between active and inactive states by binding to guanine nucleotides.
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Regulation of the Unfolded Protein Response01:31

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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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The Unfolded Protein Response01:37

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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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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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Novel RNA-Binding Proteins Isolation by the RaPID Methodology
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Ras moves to stay in place.

Malte Schmick1, Astrid Kraemer1, Philippe I H Bastiaens2

  • 1Department of Systemic Cell Biology, Max Planck Institute of Molecular Physiology, Otto-Hahn-Strasse 11, 44227 Dortmund, Germany.

Trends in Cell Biology
|March 12, 2015
PubMed
Summary
This summary is machine-generated.

Ras GTPases are crucial for cell signaling, but mutations cause problems. A dynamic system maintains Ras at the plasma membrane, ensuring proper signaling function.

Keywords:
PDEδ–Arl2 delivery systemRas localizationRas signalingrecycling endosomespatial cycles

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Area of Science:

  • Cellular biology
  • Molecular signaling
  • Biophysics

Background:

  • Ras proteins are key intracellular signaling hubs.
  • Aberrant Ras signaling, often due to mutations, is linked to diseases.
  • Ras localization at the plasma membrane (PM) is critical for its signaling capacity.

Purpose of the Study:

  • To elucidate the mechanisms maintaining Ras enrichment at the plasma membrane.
  • To understand how Ras localization impacts its signaling function.
  • To investigate the reaction-diffusion system governing Ras GTPase distribution.

Main Methods:

  • Analysis of membrane affinities through lipidation and interaction motifs.
  • Modeling of vesicular transport dynamics to the PM.
  • Investigating the role of solubilization factors in regulating Ras diffusion.

Main Results:

  • Ras PM localization is dynamically maintained by lipidation, vesicular transport, and diffusion regulation.
  • This system counteracts the entropic tendency of Ras to distribute across all membranes.
  • The out-of-equilibrium localization is essential for Ras signaling functionality.

Conclusions:

  • A reaction-diffusion system actively maintains Ras GTPases at the plasma membrane.
  • This non-equilibrium localization is fundamental for Ras-mediated intracellular signaling.
  • Understanding this system provides insights into Ras-related diseases and potential therapeutic targets.