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Low temperature (15 degrees C) induces COPII dissociation from membranes and slow exit from the endoplasmic reticulum

Emma Martínez-Alonso1, Mónica Tomás, José Ballesta

  • 1Department of Cell Biology, School of Medicine, University of Murcia, 30100, Murcia, Spain.

Histochemistry and Cell Biology
|August 19, 2007
PubMed

Insights

Low temperatures disrupt cell transport by causing COPII proteins to detach from membranes, slowing endoplasmic reticulum exit. Clathrin coats remain unaffected by this cold-induced blockade.

Area of Science:

  • Cell biology
  • Molecular and cell biology
  • Membrane trafficking

Background:

  • Low temperatures cause transport blockades at the endoplasmic reticulum-Golgi intermediate compartment (ERGIC).
  • Previous research indicates COPI complex detachment from membranes as the primary low-temperature effect.

Purpose of the Study:

  • Investigate the impact of low temperatures on COPII and clathrin coat complexes.
  • Determine the effects of cold on ER-to-Golgi transport in HeLa cells.

Main Methods:

  • Immunofluorescence microscopy
  • Cryo-immunoelectron microscopy
  • Cell culture at 15°C

Main Results:

  • COPII proteins dissociated from membranes and accumulated in the cytosol at 15°C.
  • Endoplasmic reticulum (ER) exit was significantly delayed at low temperatures.
  • Clathrin coat complexes were not affected by the low temperature.

Conclusions:

  • Low temperature induces COPII dissociation from cellular membranes.
  • Cold conditions slow the exit of cargo from the endoplasmic reticulum.
  • This study reveals a specific effect of low temperature on COPII-mediated transport, distinct from clathrin-mediated pathways.

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