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Cell surface control of the multiubiquitination and deubiquitination of high-affinity immunoglobulin E receptors

R Paolini1, J P Kinet

  • 1Molecular Allergy and Immunology Section, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Rockville, MD 20852.

The EMBO Journal
|February 1, 1993
PubMed

Insights

Protein multiubiquitination is key for degradation. This study reveals activation-induced multiubiquitination of Fc epsilon RI receptors is rapidly reversible, suggesting a novel on/off switch for cell surface signaling.

Area of Science:

  • Cell Biology
  • Immunology
  • Molecular Biology

Background:

  • Multiubiquitination targets proteins for degradation.
  • Cell surface receptors like PDGF and TCR receptors undergo multiubiquitination upon activation.
  • This process may regulate ligand-receptor complex degradation.

Purpose of the Study:

  • To investigate the role of multiubiquitination in Fc epsilon RI receptor signaling.
  • To determine if Fc epsilon RI receptor multiubiquitination is reversible.
  • To explore the implications of reversible multiubiquitination for cell surface receptor function.

Main Methods:

  • Studied antigen-induced Fc epsilon RI receptor engagement in cells.
  • Analyzed multiubiquitination of Fc epsilon RI beta and gamma chains.
  • Investigated the effect of receptor disengagement on ubiquitination status.

Main Results:

  • Antigen engagement immediately multiubiquitinates Fc epsilon RI beta and gamma chains.
  • Ubiquitination occurs independently of receptor phosphorylation and only on activated receptors.
  • Multiubiquitination is rapidly reversible upon receptor disengagement at the cell surface.

Conclusions:

  • Fc epsilon RI receptor multiubiquitination is a dynamic, cell surface-controlled process.
  • Receptor engagement and disengagement regulate Fc epsilon RI multiubiquitination and deubiquitination.
  • This reversible multiubiquitination may represent a novel mechanism for regulating cell surface receptor signaling.

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