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Updated: Jan 26, 2026

Oligomerization Dynamics of Cell Surface Receptors in Living Cells by Total Internal Reflection Fluorescence Microscopy Combined with Number and Brightness Analysis
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Oligomerization Dynamics of Cell Surface Receptors in Living Cells by Total Internal Reflection Fluorescence Microscopy Combined with Number and Brightness Analysis

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Oligomeric Architecture of Mouse Activating Nkrp1 Receptors on Living Cells

Ljubina Adámková1, Zuzana Kvíčalová2, Daniel Rozbeský3

  • 1Laboratory of Structural Biology and Cell Signaling, Institute of Microbiology, The Czech Academy of Sciences, Vídeňská 1083, 14220 Prague 4, Czech Republic. ljubina.adamkova@biomed.cas.cz.

International Journal of Molecular Sciences
|April 19, 2019
PubMed

Insights

Mouse activating Nkrp1 proteins

Area of Science:

  • Immunology
  • Molecular Biology
  • Cell Biology

Background:

  • Activating Nkrp1 proteins are type II transmembrane receptors in mice.
  • Their function and oligomerization, especially in C57BL/6 strains, remain unclear.

Purpose of the Study:

  • To investigate the oligomerization state of mouse activating Nkrp1 proteins.
  • To identify key structural elements involved in Nkrp1 receptor dimerization.

Main Methods:

  • Expression of enhanced green fluorescent protein-tagged Nkrp1 proteins in mammalian lymphoid cells.
  • Evaluation of Nkrp1 protein oligomerization using Förster resonance energy transfer (FRET).
  • Detection of Nkrp1 oligomers by Western blotting and structural characterization of recombinant ectodomains.

Main Results:

  • Nkrp1 isoforms c1, c2, and f predominantly formed homodimers.
  • Nkrp1a showed a higher proportion of monomers on the cell surface.
  • Stalk cysteines are crucial for dimerization, with cysteine at position 74 being particularly influential.

Conclusions:

  • This study provides new insights into the oligomerization patterns of Nkrp1 receptors on lymphoid cells.
  • Understanding Nkrp1 oligomerization is essential for elucidating their biological functions.
Keywords:
Förster resonance energy transferNkrp1cysteinedimerizationdisulfide bond arrangement

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