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Visualization of Endoplasmic Reticulum Subdomains in Cultured Cells
Published on: February 18, 2014
Identification of an intermediate compartment involved in protein transport from endoplasmic reticulum to Golgi
A Schweizer1, J A Fransen, K Matter
1Department of Pharmacology, University of Basel, Switzerland.
Insights
Researchers identified a novel tubulovesicular compartment, defined by p53 protein, as a key intermediate in endoplasmic reticulum (ER)-to-Golgi protein transport. This compartment plays a crucial role in moving proteins from the ER to the Golgi apparatus.
Area of Science:
- Cell Biology
- Molecular Biology
- Protein Transport
Background:
- The endoplasmic reticulum (ER) to Golgi apparatus pathway is essential for protein modification and trafficking.
- Understanding intermediate compartments in this pathway is crucial for deciphering cellular protein processing.
Purpose of the Study:
- To investigate the function of a specific tubulovesicular compartment near the cis-Golgi apparatus.
- To determine the role of this compartment in endoplasmic reticulum (ER)-to-Golgi protein transport.
Main Methods:
- Utilized light and immunoelectron microscopy in Vero cells.
- Studied the transport of vesicular stomatitis virus strain ts045 G protein under different temperature conditions.
Main Results:
- Identified a 53-kDa transmembrane protein, p53, defining the tubulovesicular compartment.
- Observed G protein accumulation in the ER at 39.5°C with access to the p53 compartment.
- Demonstrated G protein export from the ER into the p53 compartment at 15°C, which formed a compact structure near the Golgi.
- Showed G protein migration through the Golgi and resumption of normal p53 compartment structure at 32°C.
Conclusions:
- Established the p53-defined compartment as the 15°C intermediate in the ER-to-Golgi protein transport pathway.
- Highlighted the dynamic nature of this compartment during protein trafficking.
Abstract:
We have studied the role of a previously described tubulovesicular compartment near the cis-Golgi apparatus in endoplasmic reticulum (ER)-to-Golgi protein transport by light and immunoelectron microscopy in Vero cells. The compartment is defined by a 53-kDa transmembrane protein designated p53. When transport of the vesicular stomatitis virus strain ts045 G protein was arrested at 39.5 degrees C, the G protein accumulated in the ER but had access to the p53 compartment. At 15 degrees C, the G protein was exported from the ER into the p53 compartment which formed a compact structure composed of vesicular and tubular profiles in close proximity to the Golgi. Upon raising the temperature to 32 degrees C, the G protein migrated through the Golgi apparatus while the p53 compartment resumed its normal structure again. These results establish the p53 compartment as the 15 degrees C intermediate of the ER-to-Golgi protein transport pathway.
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