Endosomal trafficking of the ligated FcεRI receptor

Gul'nar V. Fattakhova, Madhan Masilamani, Sriram Narayanan, Francisco Borrego, Alasdair M. Gilfillan, Dean D. Metcalfe, John E. Coligan

Research output: Contribution to journalArticlepeer-review

18 Scopus citations


In addition to initiating signaling cascades leading to mast cell mediator release, aggregation of the high affinity IgE receptor (FcεRI) leads to rapid internalization of the cross-linked receptor. However, little is known about the trafficking of the internalized FcεRI. Here we demonstrate that in RBL-2H3 cells, aggregated FcεRI appears in the early endosomal antigen 1 (EEA1+) domains of the early endosomes within 15 min after ligation. Minimal co-localization of FcεRI with Rab5 was observed by 30 min, followed by its appearance in the Rab7+ late endosomes and lysosomes at later time points. During endosomal sorting, FcεRIα and γ subunits remain associated. In Syk-deficient RBL-2H3 cells, the rate of transport to lysosomes is markedly increased. Taken together, our data demonstrate time-dependent sorting of aggregated FcεRI within the endosomal-lysosomal network, and that Syk may play an essential role in regulating the trafficking and retention of FcεRI in endosomes.

Original languageEnglish
Pages (from-to)793-802
Number of pages10
JournalMolecular Immunology
Issue number5
StatePublished - Feb 2009
Externally publishedYes


  • Co-localization
  • Endosomes
  • FcεRI
  • Syk


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