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CD83 and GRASP55 interact in human dendritic cells.

Marcello F Stein1, Katja Blume1, Christiane S Heilingloh1

  • 1Department of Immune Modulation, Universitätsklinikum Erlangen, Erlangen, Germany.

Biochemical and Biophysical Research Communications
|February 22, 2015
PubMed
Summary

The Golgi protein GRASP55 interacts with the dendritic cell marker CD83 during maturation. This interaction is crucial for proper CD83 glycosylation and surface expression, impacting T-cell stimulation.

Keywords:
CD83Dendritic cellsGRASP55Golgi

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Area of Science:

  • Immunology
  • Cell Biology
  • Glycobiology

Background:

  • CD83 is a key surface marker for mature dendritic cells (DCs), essential for T-cell stimulation.
  • The membrane-bound form of CD83 (mbCD83) is heavily glycosylated upon DC maturation, influencing its function.

Purpose of the Study:

  • To identify interaction partners of CD83 involved in its maturation-dependent regulation.
  • To elucidate the role of GRASP55 in CD83 glycosylation and surface expression.

Main Methods:

  • Yeast two-hybrid screening to identify CD83 interaction partners.
  • Analysis of CD83 glycosylation, co-localization with GRASP55, and surface expression during DC maturation.
  • Mutation of the CD83 C-terminal TELV-motif to assess binding and functional impact.

Main Results:

  • GRASP55 was identified as an interaction partner of CD83.
  • DC maturation induced CD83 expression, glycosylation, GRASP55 interaction, and surface exposure.
  • CD83's C-terminal TELV-motif mediates GRASP55 binding, influencing glycosylation and membrane expression.

Conclusions:

  • GRASP55 interacts with CD83 early in DC maturation.
  • This interaction is vital for regulating CD83 glycosylation and surface expression on dendritic cells.