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Updated: Jun 26, 2026

Visualization of Endoplasmic Reticulum Subdomains in Cultured Cells
Published on: February 18, 2014
Structural framework of the GABARAP-calreticulin interface--implications for substrate binding to endoplasmic
Yvonne Thielmann1, Oliver H Weiergräber, Jeannine Mohrlüder
1Institut für Neurowissenschaften und Biophysik, Molekulare Biophysik, Forschungszentrum Jülich, Germany.
The 4-aminobutyrate type A receptor-associated protein (GABARAP) interacts with calreticulin. Structural analysis reveals a novel binding mode, impacting chaperone function in vesicle trafficking.
Area of Science:
- Cell Biology
- Structural Biology
- Neuroscience
Background:
- The 4-aminobutyrate type A receptor-associated protein (GABARAP) is crucial for intracellular vesicle trafficking, especially in neurons.
- Calreticulin acts as a molecular chaperone involved in protein folding and quality control.
Purpose of the Study:
- To elucidate the structural basis of the GABARAP-calreticulin interaction.
- To understand the functional implications of this interaction for cellular processes.
Main Methods:
- Spectroscopic techniques
- X-ray crystallography
- Molecular modeling
Main Results:
- The crystal structure of GABARAP bound to its key epitope on calreticulin was determined.
- Molecular modeling suggested a novel mechanism for substrate interaction with full-length calreticulin.
Conclusions:
- The findings provide atomic-level insight into GABARAP-calreticulin binding.
- This interaction may represent a conserved mechanism within the calreticulin/calnexin chaperone family.
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