| Literature DB >> 18945491 |
Gul'nar V Fattakhova1, Madhan Masilamani, Sriram Narayanan, Francisco Borrego, Alasdair M Gilfillan, Dean D Metcalfe, John E Coligan.
Abstract
In addition to initiating signaling cascades leading to mast cell mediator release, aggregation of the high affinity IgE receptor (FcvarepsilonRI) leads to rapid internalization of the cross-linked receptor. However, little is known about the trafficking of the internalized FcvarepsilonRI. Here we demonstrate that in RBL-2H3 cells, aggregated FcvarepsilonRI appears in the early endosomal antigen 1 (EEA1(+)) domains of the early endosomes within 15min after ligation. Minimal co-localization of FcvarepsilonRI with Rab5 was observed by 30min, followed by its appearance in the Rab7(+) late endosomes and lysosomes at later time points. During endosomal sorting, FcvarepsilonRIalpha and gamma 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 FcvarepsilonRI within the endosomal-lysosomal network, and that Syk may play an essential role in regulating the trafficking and retention of FcvarepsilonRI in endosomes.Entities:
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Year: 2008 PMID： 18945491 PMCID： PMC2668543 DOI： 10.1016/j.molimm.2008.09.002
Source DB: PubMed Journal: Mol Immunol ISSN： 0161-5890 Impact factor: 4.407